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Conserved domains on  [gi|568908697|ref|XP_006529471|]
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DNA annealing helicase and endonuclease ZRANB3 isoform X1 [Mus musculus]

Protein Classification

DEXHc_HARP_SMARCAL1 and SF2_C_SNF domain-containing protein( domain architecture ID 12785066)

protein containing domains DEXHc_HARP_SMARCAL1, SF2_C_SNF, ZnF_RBZ, and HNHc

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
41-260 2.07e-105

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: 329.17  E-value: 2.07e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGIVFALRRDGRCMVADEMGLGKTIQAIAIAYFYKEEWPLLIVVPSSLRYPWIEELEKWIPELEPEEINVVMNK 120
Cdd:cd18010     1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQVIVKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  121 TDIGRIPGSRVTVLGYGLLTTDAETLLDalntQNFRVVIVDESHYMKSRTAARSKILLPMVQKARRAILLTGTPALGRPE 200
Cdd:cd18010    81 KDGLRDGDAKVVIVSYDLLRRLEKQLLA----RKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVILLSGTPALSRPI 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568908697  201 ELFMQIEALFPQKFGTWIEYAKRYCNAHvryFGKRRQWDCrGASNLSELHQLL-NDIMIRR 260
Cdd:cd18010   157 ELFTQLDALDPKLFGRFHDFGRRYCAAK---QGGFGWDYS-GSSNLEELHLLLlATIMIRR 213
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
28-468 9.58e-92

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 309.08  E-value: 9.58e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   28 TQLDFLPDKLRTKLLPFQKDGIVFALRRD---GRCMVADEMGLGKTIQAIAIAYFYKEE---WPLLIVVPSSLRYPWIEE 101
Cdd:COG0553   229 EALESLPAGLKATLRPYQLEGAAWLLFLRrlgLGGLLADDMGLGKTIQALALLLELKERglaRPVLIVAPTSLVGNWQRE 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  102 LEKWIPELEPEEINVVMN-KTDIGRIPGSRVTVLGYGLLTTDAETLLDalntQNFRVVIVDESHYMKSRTAARSKILlpM 180
Cdd:COG0553   309 LAKFAPGLRVLVLDGTRErAKGANPFEDADLVITSYGLLRRDIELLAA----VDWDLVILDEAQHIKNPATKRAKAV--R 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  181 VQKARRAILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRYCNAHVRYfgkrrqwdcrGASNLSELHQLLNDIMIRR 260
Cdd:COG0553   383 ALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKG----------DEEALERLRRLLRPFLLRR 452
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  261 LKSEVLSQLPPKVRQRIPFDLPPA------AVKElnasfEEWQKLMRAPNSGAMETVMGLITRMfKQTAI---------- 324
Cdd:COG0553   453 TKEDVLKDLPEKTEETLYVELTPEqralyeAVLE-----YLRRELEGAEGIRRRGLILAALTRL-RQICShpallleega 526
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  325 ------AKAGAVKDYIKMLLQNDSlKFLVFAHHLSMLQACTEAVIESKSRYIRIDGSVPSSERIHLVNQFQKDPDTRVAI 398
Cdd:COG0553   527 elsgrsAKLEALLELLEELLAEGE-KVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFL 605
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  399 LSIQAAGQGLTFTAASHVVFAELYWDPGHIKQAEDRAHRIGQCSSVNIHYLIANGTLDSLMWAMLNRKAQ 468
Cdd:COG0553   606 ISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRA 675
HNHc cd00085
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ...
1025-1090 5.22e-08

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: 50.55  E-value: 5.22e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568908697 1025 KSHRKSLLNAAWTAKLPLEqlnemlrnPGEGHFWQVDHIRPVyEGGGQCSLDNLQTLCTVCHKERT 1090
Cdd:cd00085     1 RSHRLVLLARDGLCPYCGK--------PGGTEGLEVDHIIPL-SDGGNNDLDNLVLLCRKCHRKKH 57
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
625-647 1.04e-03

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


:

Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 37.30  E-value: 1.04e-03
                            10        20
                    ....*....|....*....|...
gi 568908697    625 WQCGFCTFLNNPGLPYCEMCENP 647
Cdd:smart00547    3 WECPACTFLNFASRSKCFACGAP 25
 
Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
41-260 2.07e-105

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: 329.17  E-value: 2.07e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGIVFALRRDGRCMVADEMGLGKTIQAIAIAYFYKEEWPLLIVVPSSLRYPWIEELEKWIPELEPEEINVVMNK 120
Cdd:cd18010     1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQVIVKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  121 TDIGRIPGSRVTVLGYGLLTTDAETLLDalntQNFRVVIVDESHYMKSRTAARSKILLPMVQKARRAILLTGTPALGRPE 200
Cdd:cd18010    81 KDGLRDGDAKVVIVSYDLLRRLEKQLLA----RKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVILLSGTPALSRPI 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568908697  201 ELFMQIEALFPQKFGTWIEYAKRYCNAHvryFGKRRQWDCrGASNLSELHQLL-NDIMIRR 260
Cdd:cd18010   157 ELFTQLDALDPKLFGRFHDFGRRYCAAK---QGGFGWDYS-GSSNLEELHLLLlATIMIRR 213
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
28-468 9.58e-92

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 309.08  E-value: 9.58e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   28 TQLDFLPDKLRTKLLPFQKDGIVFALRRD---GRCMVADEMGLGKTIQAIAIAYFYKEE---WPLLIVVPSSLRYPWIEE 101
Cdd:COG0553   229 EALESLPAGLKATLRPYQLEGAAWLLFLRrlgLGGLLADDMGLGKTIQALALLLELKERglaRPVLIVAPTSLVGNWQRE 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  102 LEKWIPELEPEEINVVMN-KTDIGRIPGSRVTVLGYGLLTTDAETLLDalntQNFRVVIVDESHYMKSRTAARSKILlpM 180
Cdd:COG0553   309 LAKFAPGLRVLVLDGTRErAKGANPFEDADLVITSYGLLRRDIELLAA----VDWDLVILDEAQHIKNPATKRAKAV--R 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  181 VQKARRAILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRYCNAHVRYfgkrrqwdcrGASNLSELHQLLNDIMIRR 260
Cdd:COG0553   383 ALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKG----------DEEALERLRRLLRPFLLRR 452
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  261 LKSEVLSQLPPKVRQRIPFDLPPA------AVKElnasfEEWQKLMRAPNSGAMETVMGLITRMfKQTAI---------- 324
Cdd:COG0553   453 TKEDVLKDLPEKTEETLYVELTPEqralyeAVLE-----YLRRELEGAEGIRRRGLILAALTRL-RQICShpallleega 526
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  325 ------AKAGAVKDYIKMLLQNDSlKFLVFAHHLSMLQACTEAVIESKSRYIRIDGSVPSSERIHLVNQFQKDPDTRVAI 398
Cdd:COG0553   527 elsgrsAKLEALLELLEELLAEGE-KVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFL 605
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  399 LSIQAAGQGLTFTAASHVVFAELYWDPGHIKQAEDRAHRIGQCSSVNIHYLIANGTLDSLMWAMLNRKAQ 468
Cdd:COG0553   606 ISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRA 675
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
325-450 1.67e-44

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: 157.25  E-value: 1.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  325 AKAGAVKDYIKMLLQNDSlKFLVFAHHLSMLQACTEAVIESKSRYIRIDGSVPSSERIHLVNQFQKDPDTRVAILSIQAA 404
Cdd:cd18793    11 GKLEALLELLEELREPGE-KVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568908697  405 GQGLTFTAASHVVFAELYWDPGHIKQAEDRAHRIGQCSSVNIHYLI 450
Cdd:cd18793    90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
45-273 7.35e-34

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: 132.04  E-value: 7.35e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697    45 QKDGIVFALRRD---GR-CMVADEMGLGKTIQAIA-IAYFYKEE----WPLLIVVPSSLRYPWIEELEKWipeLEPEEIN 115
Cdd:pfam00176    2 QIEGVNWMLSLEnnlGRgGILADEMGLGKTLQTISlLLYLKHVDknwgGPTLIVVPLSLLHNWMNEFERW---VSPPALR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   116 VVM---NKTDIGRIPGSRVTVLGYGLLTTDAETLL---DALNTQNFRVVIVDESHYMKSRTAARSKILLPMvqKARRAIL 189
Cdd:pfam00176   79 VVVlhgNKRPQERWKNDPNFLADFDVVITTYETLRkhkELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSL--KTRNRWI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   190 LTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRYCNAHVRYFGKRRQWdcrgasnlsELHQLLNDIMIRRLKSEVLSQL 269
Cdd:pfam00176  157 LTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVS---------RLHKLLKPFLLRRTKKDVEKSL 227

                   ....
gi 568908697   270 PPKV 273
Cdd:pfam00176  228 PPKV 231
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
60-446 6.19e-23

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 106.04  E-value: 6.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   60 MVADEMGLGKTIQAIA-IAYFYKEE---WPLLIVVPSSLRYPWIEELEKWIPELE-------PEEINVVMNKTdigRIPG 128
Cdd:PLN03142  192 ILADEMGLGKTLQTISlLGYLHEYRgitGPHMVVAPKSTLGNWMNEIRRFCPVLRavkfhgnPEERAHQREEL---LVAG 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  129 srvtvlGYGLLTTDAETLL---DALNTQNFRVVIVDESHYMKSRTAARSKILLPMVQKARraILLTGTPALGRPEELFMQ 205
Cdd:PLN03142  269 ------KFDVCVTSFEMAIkekTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYR--LLITGTPLQNNLHELWAL 340
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  206 IEALFPQKFGTwieyakrycnahvryFGKRRQWDCRGASN-----LSELHQLLNDIMIRRLKSEVLSQLPPKVRQRIPFD 280
Cdd:PLN03142  341 LNFLLPEIFSS---------------AETFDEWFQISGENdqqevVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVG 405
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  281 LPPAAVKELNASFeewQKLMRAPNSGA-----METVMGL-------------------ITRMFKQTAIAKAGAVKDYIKM 336
Cdd:PLN03142  406 MSQMQKQYYKALL---QKDLDVVNAGGerkrlLNIAMQLrkccnhpylfqgaepgppyTTGEHLVENSGKMVLLDKLLPK 482
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  337 LLQNDSlKFLVFAHHLSMLQACTEAVIESKSRYIRIDGSVPSSERIHLVNQFQKDPDTR-VAILSIQAAGQGLTFTAASH 415
Cdd:PLN03142  483 LKERDS-RVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADI 561
                         410       420       430
                  ....*....|....*....|....*....|.
gi 568908697  416 VVFAELYWDPGHIKQAEDRAHRIGQCSSVNI 446
Cdd:PLN03142  562 VILYDSDWNPQVDLQAQDRAHRIGQKKEVQV 592
DEXDc smart00487
DEAD-like helicases superfamily;
33-216 3.13e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 92.94  E-value: 3.13e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697     33 LPDKLRTKLLPFQKDGIVFALRRDGRCMVADEMGLGKTIQA-IAIAYFYKEE--WPLLIVVP-SSLRYPWIEELEKWIPE 108
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAAlLPALEALKRGkgGRVLVLVPtRELAEQWAEELKKLGPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697    109 LEPEEINVV--MNKTDIGRIPGSRVTVLgygLLTTDaETLLDAL-----NTQNFRVVIVDESHYMKSRTAARS-KILLPM 180
Cdd:smart00487   81 LGLKVVGLYggDSKREQLRKLESGKTDI---LVTTP-GRLLDLLendklSLSNVDLVILDEAHRLLDGGFGDQlEKLLKL 156
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 568908697    181 VQKARRAILLTGTPALGRPE--ELFMQIEALFPQKFGT 216
Cdd:smart00487  157 LPKNVQLLLLSATPPEEIENllELFLNDPVFIDVGFTP 194
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
334-439 7.15e-15

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: 71.47  E-value: 7.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   334 IKMLLQNDSLKFLVFAHHLSMLQaCTEAVIESKSRYIRIDGSVPSSERIHLVNQFqKDPDTRVaILSIQAAGQGLTFTAA 413
Cdd:pfam00271    7 LELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDF-RKGKIDV-LVATDVAERGLDLPDV 83
                           90       100
                   ....*....|....*....|....*.
gi 568908697   414 SHVVFAELYWDPGHIKQAEDRAHRIG 439
Cdd:pfam00271   84 DLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
368-439 6.68e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 64.93  E-value: 6.68e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568908697    368 RYIRIDGSVPSSERIHLVNQFQKDPdtRVAILSIQAAGQGLTFTAASHVVFAELYWDPGHIKQAEDRAHRIG 439
Cdd:smart00490   13 KVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DpdE NF041062
protein DpdE;
58-200 2.65e-11

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 68.07  E-value: 2.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   58 RCMVADEMGLGKTIQAIAIAYFYKEEWP---LLIVVPSSLRYPWIEELEkwipelepeeinvvmNKTDIGRIPGSRVTVL 134
Cdd:NF041062  172 RYLLADEVGLGKTIEAGLVIRQHLLDNPdarVLVLVPDALVRQWRRELR---------------DKFFLDDFPGARVRVL 236
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568908697  135 GYglltTDAETLLDalNTQNFRVVIVDESHYM-------KSRTAARSKILLPMVQKARRAILLTGTPALGRPE 200
Cdd:NF041062  237 SH----EEPERWEP--LLDAPDLLVVDEAHQLarlawsgDPPERARYRELAALAHAAPRLLLLSATPVLGNEE 303
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
40-419 7.45e-11

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 66.20  E-value: 7.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   40 KLLPFQKDGI--VFALRRDG--RCMVADEMGLGKTIQAIAIAYFYKEEWPLLIVVPS-SLRYPWIEELEKWIPelepeEI 114
Cdd:COG1061    80 ELRPYQQEALeaLLAALERGggRGLVVAPTGTGKTVLALALAAELLRGKRVLVLVPRrELLEQWAEELRRFLG-----DP 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  115 NVVMNKTDIGRipgsRVTVLGYGLLTTDAEtlLDALNtQNFRVVIVDESHymksRTAARS-KILLPMVQKARRaILLTGT 193
Cdd:COG1061   155 LAGGGKKDSDA----PITVATYQSLARRAH--LDELG-DRFGLVIIDEAH----HAGAPSyRRILEAFPAAYR-LGLTAT 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  194 PAL--GRPEELFMqiealfpqkfgtwieyakrycnahvrYFGKRRQWDcrgasnlseLHQLLNDIMIRrlksevlsqlPP 271
Cdd:COG1061   223 PFRsdGREILLFL--------------------------FDGIVYEYS---------LKEAIEDGYLA----------PP 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  272 KVRQRipfdlppaavkelnasFEEWQKLMRapnsgAMETVMGLITRMFKQTAIAKAGAVKDYIKMLLQNDslKFLVFAHH 351
Cdd:COG1061   258 EYYGI----------------RVDLTDERA-----EYDALSERLREALAADAERKDKILRELLREHPDDR--KTLVFCSS 314
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568908697  352 LSMLQACTEAVIESKSRYIRIDGSVPSSERIHLVNQFQKDPDTrvAILSIQAAGQGLTFTAASHVVFA 419
Cdd:COG1061   315 VDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELR--ILVTVDVLNEGVDVPRLDVAILL 380
HNHc cd00085
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ...
1025-1090 5.22e-08

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: 50.55  E-value: 5.22e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568908697 1025 KSHRKSLLNAAWTAKLPLEqlnemlrnPGEGHFWQVDHIRPVyEGGGQCSLDNLQTLCTVCHKERT 1090
Cdd:cd00085     1 RSHRLVLLARDGLCPYCGK--------PGGTEGLEVDHIIPL-SDGGNNDLDNLVLLCRKCHRKKH 57
McrA COG1403
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];
994-1087 6.03e-06

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


Pssm-ID: 441013 [Multi-domain]  Cd Length: 64  Bit Score: 44.97  E-value: 6.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  994 LRAQVFATEHGVCQHCGvdaqelflrmrdapkshrksllnaawtaklpleqlnemlrNPGEGHFWQVDHIRPVYEGGGQc 1073
Cdd:COG1403    10 LRRAVLKRDNGRCQYCG----------------------------------------RPFSGDALEVDHIIPRSRGGTD- 48
                          90
                  ....*....|....
gi 568908697 1074 SLDNLQTLCTVCHK 1087
Cdd:COG1403    49 TWENLVLLCRRCNR 62
HNH pfam01844
HNH endonuclease; His-Asn-His (HNH) proteins are a very common family of small nucleic ...
1057-1092 7.24e-06

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: 43.88  E-value: 7.24e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 568908697  1057 FWQVDHIRPVYEGGGQcSLDNLQTLCTVCHKERTAQ 1092
Cdd:pfam01844   13 ALTVDHIIPLSDGGAD-DIENLILLCPSCHNKKHNR 47
HNHc smart00507
HNH nucleases;
1058-1086 2.01e-04

HNH nucleases;


Pssm-ID: 214702 [Multi-domain]  Cd Length: 52  Bit Score: 40.13  E-value: 2.01e-04
                            10        20
                    ....*....|....*....|....*....
gi 568908697   1058 WQVDHIRPvYEGGGQCSLDNLQTLCTVCH 1086
Cdd:smart00507   24 LEVDHIIP-LSDGGNDDLDNLVLLCPKCH 51
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
625-647 1.04e-03

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 37.30  E-value: 1.04e-03
                            10        20
                    ....*....|....*....|...
gi 568908697    625 WQCGFCTFLNNPGLPYCEMCENP 647
Cdd:smart00547    3 WECPACTFLNFASRSKCFACGAP 25
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
323-440 5.57e-03

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 40.67  E-value: 5.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  323 AIAKAGAVKDYIKMLLQNDSLKFLVFAHHLSMLQACTEAVIESKSRYIRIDGSVPSSERIHLVNQFqKDPDTRVAIlSIQ 402
Cdd:PRK01297  316 AVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGF-REGKIRVLV-ATD 393
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568908697  403 AAGQGLTFTAASHVVFAELYWDPghikqaEDRAHRIGQ 440
Cdd:PRK01297  394 VAGRGIHIDGISHVINFTLPEDP------DDYVHRIGR 425
 
Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
41-260 2.07e-105

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: 329.17  E-value: 2.07e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGIVFALRRDGRCMVADEMGLGKTIQAIAIAYFYKEEWPLLIVVPSSLRYPWIEELEKWIPELEPEEINVVMNK 120
Cdd:cd18010     1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQVIVKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  121 TDIGRIPGSRVTVLGYGLLTTDAETLLDalntQNFRVVIVDESHYMKSRTAARSKILLPMVQKARRAILLTGTPALGRPE 200
Cdd:cd18010    81 KDGLRDGDAKVVIVSYDLLRRLEKQLLA----RKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVILLSGTPALSRPI 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568908697  201 ELFMQIEALFPQKFGTWIEYAKRYCNAHvryFGKRRQWDCrGASNLSELHQLL-NDIMIRR 260
Cdd:cd18010   157 ELFTQLDALDPKLFGRFHDFGRRYCAAK---QGGFGWDYS-GSSNLEELHLLLlATIMIRR 213
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
28-468 9.58e-92

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 309.08  E-value: 9.58e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   28 TQLDFLPDKLRTKLLPFQKDGIVFALRRD---GRCMVADEMGLGKTIQAIAIAYFYKEE---WPLLIVVPSSLRYPWIEE 101
Cdd:COG0553   229 EALESLPAGLKATLRPYQLEGAAWLLFLRrlgLGGLLADDMGLGKTIQALALLLELKERglaRPVLIVAPTSLVGNWQRE 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  102 LEKWIPELEPEEINVVMN-KTDIGRIPGSRVTVLGYGLLTTDAETLLDalntQNFRVVIVDESHYMKSRTAARSKILlpM 180
Cdd:COG0553   309 LAKFAPGLRVLVLDGTRErAKGANPFEDADLVITSYGLLRRDIELLAA----VDWDLVILDEAQHIKNPATKRAKAV--R 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  181 VQKARRAILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRYCNAHVRYfgkrrqwdcrGASNLSELHQLLNDIMIRR 260
Cdd:COG0553   383 ALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKG----------DEEALERLRRLLRPFLLRR 452
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  261 LKSEVLSQLPPKVRQRIPFDLPPA------AVKElnasfEEWQKLMRAPNSGAMETVMGLITRMfKQTAI---------- 324
Cdd:COG0553   453 TKEDVLKDLPEKTEETLYVELTPEqralyeAVLE-----YLRRELEGAEGIRRRGLILAALTRL-RQICShpallleega 526
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  325 ------AKAGAVKDYIKMLLQNDSlKFLVFAHHLSMLQACTEAVIESKSRYIRIDGSVPSSERIHLVNQFQKDPDTRVAI 398
Cdd:COG0553   527 elsgrsAKLEALLELLEELLAEGE-KVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFL 605
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  399 LSIQAAGQGLTFTAASHVVFAELYWDPGHIKQAEDRAHRIGQCSSVNIHYLIANGTLDSLMWAMLNRKAQ 468
Cdd:COG0553   606 ISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRA 675
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
325-450 1.67e-44

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: 157.25  E-value: 1.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  325 AKAGAVKDYIKMLLQNDSlKFLVFAHHLSMLQACTEAVIESKSRYIRIDGSVPSSERIHLVNQFQKDPDTRVAILSIQAA 404
Cdd:cd18793    11 GKLEALLELLEELREPGE-KVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568908697  405 GQGLTFTAASHVVFAELYWDPGHIKQAEDRAHRIGQCSSVNIHYLI 450
Cdd:cd18793    90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
41-212 2.06e-35

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 133.07  E-value: 2.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGIVFALRRD---GRCMVADEMGLGKTIQAIAIAYFYKEE----WPLLIVVPSSLRYPWIEELEKWIPEL---- 109
Cdd:cd17919     1 LRPYQLEGLNFLLELYengPGGILADEMGLGKTLQAIAFLAYLLKEgkerGPVLVVCPLSVLENWEREFEKWTPDLrvvv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  110 ---EPEEINVVMNKTDIGRipgSRVTVLGYGLLTTDAETLLDalntQNFRVVIVDESHYMKSRTAARSKILLPMvqKARR 186
Cdd:cd17919    81 yhgSQRERAQIRAKEKLDK---FDVVLTTYETLRRDKASLRK----FRWDLVVVDEAHRLKNPKSQLSKALKAL--RAKR 151
                         170       180
                  ....*....|....*....|....*.
gi 568908697  187 AILLTGTPALGRPEELFMQIEALFPQ 212
Cdd:cd17919   152 RLLLTGTPLQNNLEELWALLDFLDPP 177
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
45-273 7.35e-34

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: 132.04  E-value: 7.35e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697    45 QKDGIVFALRRD---GR-CMVADEMGLGKTIQAIA-IAYFYKEE----WPLLIVVPSSLRYPWIEELEKWipeLEPEEIN 115
Cdd:pfam00176    2 QIEGVNWMLSLEnnlGRgGILADEMGLGKTLQTISlLLYLKHVDknwgGPTLIVVPLSLLHNWMNEFERW---VSPPALR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   116 VVM---NKTDIGRIPGSRVTVLGYGLLTTDAETLL---DALNTQNFRVVIVDESHYMKSRTAARSKILLPMvqKARRAIL 189
Cdd:pfam00176   79 VVVlhgNKRPQERWKNDPNFLADFDVVITTYETLRkhkELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSL--KTRNRWI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   190 LTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRYCNAHVRYFGKRRQWdcrgasnlsELHQLLNDIMIRRLKSEVLSQL 269
Cdd:pfam00176  157 LTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVS---------RLHKLLKPFLLRRTKKDVEKSL 227

                   ....
gi 568908697   270 PPKV 273
Cdd:pfam00176  228 PPKV 231
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
41-214 1.43e-28

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: 114.31  E-value: 1.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGIVFALRRD-GRCMVADEMGLGKTIQAIAIAyfyKEEW------PLLIVVPSSLRYPWIEELEK--WIPELEP 111
Cdd:cd18011     1 PLPHQIDAVLRALRKPpVRLLLADEVGLGKTIEAGLII---KELLlrgdakRVLILCPASLVEQWQDELQDkfGLPFLIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  112 EEINVVMNKTDIGRIPGSR-VTVLGYGLLTTDaETLLDALNTQNFRVVIVDESHYMKSRTAA----RSKILLPMVQKARR 186
Cdd:cd18011    78 DRETAAQLRRLIGNPFEEFpIVIVSLDLLKRS-EERRGLLLSEEWDLVVVDEAHKLRNSGGGketkRYKLGRLLAKRARH 156
                         170       180
                  ....*....|....*....|....*...
gi 568908697  187 AILLTGTPALGRPEELFMQIEALFPQKF 214
Cdd:cd18011   157 VLLLTATPHNGKEEDFRALLSLLDPGRF 184
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
37-262 1.05e-26

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: 109.19  E-value: 1.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   37 LRTKLLPFQKDGI--VFALRRDG-RCMVADEMGLGKTIQAIA-IAYFYKEEW--PLLIVVPSSLRYPWIEELEKWIPELE 110
Cdd:cd18012     1 LKATLRPYQKEGFnwLSFLRHYGlGGILADDMGLGKTLQTLAlLLSRKEEGRkgPSLVVAPTSLIYNWEEEAAKFAPELK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  111 PeeinVVMNKTD-----IGRIPGSRVTVLGYGLLTTDaetlLDALNTQNFRVVIVDESHYMKSRTAARSKILlpMVQKAR 185
Cdd:cd18012    81 V----LVIHGTKrkrekLRALEDYDLVITSYGLLRRD----IELLKEVKFHYLVLDEAQNIKNPQTKTAKAV--KALKAD 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568908697  186 RAILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRYCNAHVRYFGKRRqwdcrgasnLSELHQLLNDIMIRRLK 262
Cdd:cd18012   151 HRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEA---------LEELKKLISPFILRRLK 218
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
41-260 6.17e-26

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: 107.33  E-value: 6.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDG---IVFALRRDGRCMVADEMGLGKTIQAIA----IAYFYKEEWPLLIVVPSSLRYPWIEELEKWIPelepee 113
Cdd:cd17995     1 LRDYQLEGvnwLLFNWYNRRNCILADEMGLGKTIQSIAflehLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  114 INVVM-----------------NKTDIGRiPGSRV---TVlgygLLTTdAETLL---DALNTQNFRVVIVDESHYMKSRT 170
Cdd:cd17995    75 MNVVVyhgsgesrqiiqqyemyFKDAQGR-KKKGVykfDV----LITT-YEMVIadaEELRKIPWRVVVVDEAHRLKNRN 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  171 AARSKILLPMVQKARraILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRYCnahvryfgkrrqwDCRGASNLSELH 250
Cdd:cd17995   149 SKLLQGLKKLTLEHK--LLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFG-------------DLKTAEQVEKLQ 213
                         250
                  ....*....|
gi 568908697  251 QLLNDIMIRR 260
Cdd:cd17995   214 ALLKPYMLRR 223
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
60-446 6.19e-23

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 106.04  E-value: 6.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   60 MVADEMGLGKTIQAIA-IAYFYKEE---WPLLIVVPSSLRYPWIEELEKWIPELE-------PEEINVVMNKTdigRIPG 128
Cdd:PLN03142  192 ILADEMGLGKTLQTISlLGYLHEYRgitGPHMVVAPKSTLGNWMNEIRRFCPVLRavkfhgnPEERAHQREEL---LVAG 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  129 srvtvlGYGLLTTDAETLL---DALNTQNFRVVIVDESHYMKSRTAARSKILLPMVQKARraILLTGTPALGRPEELFMQ 205
Cdd:PLN03142  269 ------KFDVCVTSFEMAIkekTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYR--LLITGTPLQNNLHELWAL 340
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  206 IEALFPQKFGTwieyakrycnahvryFGKRRQWDCRGASN-----LSELHQLLNDIMIRRLKSEVLSQLPPKVRQRIPFD 280
Cdd:PLN03142  341 LNFLLPEIFSS---------------AETFDEWFQISGENdqqevVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVG 405
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  281 LPPAAVKELNASFeewQKLMRAPNSGA-----METVMGL-------------------ITRMFKQTAIAKAGAVKDYIKM 336
Cdd:PLN03142  406 MSQMQKQYYKALL---QKDLDVVNAGGerkrlLNIAMQLrkccnhpylfqgaepgppyTTGEHLVENSGKMVLLDKLLPK 482
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  337 LLQNDSlKFLVFAHHLSMLQACTEAVIESKSRYIRIDGSVPSSERIHLVNQFQKDPDTR-VAILSIQAAGQGLTFTAASH 415
Cdd:PLN03142  483 LKERDS-RVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADI 561
                         410       420       430
                  ....*....|....*....|....*....|.
gi 568908697  416 VVFAELYWDPGHIKQAEDRAHRIGQCSSVNI 446
Cdd:PLN03142  562 VILYDSDWNPQVDLQAQDRAHRIGQKKEVQV 592
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
59-214 3.15e-22

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: 95.14  E-value: 3.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   59 CMVADEMGLGKTIQAIA-IAYFYK--EEWPLLIVVPSSLRYPWIEELEKWIPEL----------EPEEI--NVVMNKTDI 123
Cdd:cd17998    22 GILADEMGLGKTIQVIAfLAYLKEigIPGPHLVVVPSSTLDNWLREFKRWCPSLkvepyygsqeERKHLryDILKGLEDF 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  124 GripgsrVTVLGYGLLTTDAE--TLLDalnTQNFRVVIVDESHYMKSRTAARSKILlpMVQKARRAILLTGTPALGRPEE 201
Cdd:cd17998   102 D------VIVTTYNLATSNPDdrSFFK---RLKLNYVVYDEGHMLKNMTSERYRHL--MTINANFRLLLTGTPLQNNLLE 170
                         170
                  ....*....|...
gi 568908697  202 LFMQIEALFPQKF 214
Cdd:cd17998   171 LMSLLNFIMPKPF 183
DEXDc smart00487
DEAD-like helicases superfamily;
33-216 3.13e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 92.94  E-value: 3.13e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697     33 LPDKLRTKLLPFQKDGIVFALRRDGRCMVADEMGLGKTIQA-IAIAYFYKEE--WPLLIVVP-SSLRYPWIEELEKWIPE 108
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAAlLPALEALKRGkgGRVLVLVPtRELAEQWAEELKKLGPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697    109 LEPEEINVV--MNKTDIGRIPGSRVTVLgygLLTTDaETLLDAL-----NTQNFRVVIVDESHYMKSRTAARS-KILLPM 180
Cdd:smart00487   81 LGLKVVGLYggDSKREQLRKLESGKTDI---LVTTP-GRLLDLLendklSLSNVDLVILDEAHRLLDGGFGDQlEKLLKL 156
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 568908697    181 VQKARRAILLTGTPALGRPE--ELFMQIEALFPQKFGT 216
Cdd:smart00487  157 LPKNVQLLLLSATPPEEIENllELFLNDPVFIDVGFTP 194
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
40-260 4.79e-21

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: 92.80  E-value: 4.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   40 KLLPFQKDGI---VFALRRDGRCMVADEMGLGKTIQAIA-IAYFYKEEW---PLLIVVPSSLRYPWIEELEKWIPELepe 112
Cdd:cd17993     1 ELRDYQLTGLnwlAHSWCKGNNGILADEMGLGKTVQTISfLSYLFHSQQqygPFLVVVPLSTMPAWQREFAKWAPDM--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  113 eiNVVmnkTDIGRIpGSRVTVLGY-------------GLLTTDAETLLD--ALNTQNFRVVIVDESHYMKSRTAARSKIL 177
Cdd:cd17993    78 --NVI---VYLGDI-KSRDTIREYefyfsqtkklkfnVLLTTYEIILKDkaFLGSIKWQYLAVDEAHRLKNDESLLYEAL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  178 LPMVQKARraILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRYCNAHVRYfgkrrqwdcrgasnLSELHQLLNDIM 257
Cdd:cd17993   152 KEFKTNNR--LLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEEQEKG--------------IADLHKELEPFI 215

                  ...
gi 568908697  258 IRR 260
Cdd:cd17993   216 LRR 218
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
55-260 1.33e-20

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: 91.99  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   55 RDGRCMVADEMGLGKTIQAIA-IAYFYKEEW---PLLIVVPSSLRYPWIEELEKWIPelepeEINVVMNKTDIgripGSR 130
Cdd:cd18054    38 KNNSVILADEMGLGKTIQTISfLSYLFHQHQlygPFLLVVPLSTLTSWQREFEIWAP-----EINVVVYIGDL----MSR 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  131 VTV------------LGYGLLTTDAETLLD---ALNTQNFRVVIVDESHYMKSRTAARSKILLPMVQKARraILLTGTPA 195
Cdd:cd18054   109 NTIreyewihsqtkrLKFNALITTYEILLKdktVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHR--LLITGTPL 186
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568908697  196 LGRPEELFMQIEALFPQKFGTWIEYAKRYcnahvryfGKRRQwdcrgaSNLSELHQLLNDIMIRR 260
Cdd:cd18054   187 QNSLKELWSLLHFIMPEKFEFWEDFEEDH--------GKGRE------NGYQSLHKVLEPFLLRR 237
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
41-260 4.37e-20

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: 90.81  E-value: 4.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGIVFALRR-------DGR-CMVADEMGLGKTIQAIAIAyfykeeWPLL--------------IVVPSSLRYPW 98
Cdd:cd18004     1 LRPHQREGVQFLYDCltgrrgyGGGgAILADEMGLGKTLQAIALV------WTLLkqgpygkptakkalIVCPSSLVGNW 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   99 IEELEKWIPE-------LEPEEINVVMNKTDIGRIPGSRVTVLGYGLLTTDAETLldaLNTQNFRVVIVDESHYMKSRTA 171
Cdd:cd18004    75 KAEFDKWLGLrrikvvtADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKL---SKKISIDLLICDEGHRLKNSES 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  172 ARSKILLPMvqKARRAILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRY-----------CNAHVRYFGKRRQWdc 240
Cdd:cd18004   152 KTTKALNSL--PCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFeepilrsrdpdASEEDKELGAERSQ-- 227
                         250       260
                  ....*....|....*....|
gi 568908697  241 rgasnlsELHQLLNDIMIRR 260
Cdd:cd18004   228 -------ELSELTSRFILRR 240
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
41-260 6.91e-20

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: 90.04  E-value: 6.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGIVFALRRDGrcMVADEMGLGKTIQAIA-----------IAYFYKEEWPL----------LIVVPSSLRYPWI 99
Cdd:cd18008     1 LLPYQKQGLAWMLPRGG--ILADEMGLGKTIQALAlilatrpqdpkIPEELEENSSDpkklylskttLIVVPLSLLSQWK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  100 EELEKWIpelEPEEINVVM-----NKTDIGRIPGSRVTVLGYGLLTTD------------AETLLDALNTQNFRVVIVDE 162
Cdd:cd18008    79 DEIEKHT---KPGSLKVYVyhgskRIKSIEELSDYDIVITTYGTLASEfpknkkgggrdsKEKEASPLHRIRWYRVILDE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  163 SHYMKSRTAARSKillpMVQ--KARRAILLTGTPALGRPEELFMQIealfpqKFGtwieyakrycnaHVRYFGKRRQWDC 240
Cdd:cd18008   156 AHNIKNRSTKTSR----AVCalKAERRWCLTGTPIQNSLDDLYSLL------RFL------------RVEPFGDYPWFNS 213
                         250       260
                  ....*....|....*....|....*...
gi 568908697  241 RGASNLSE--------LHQLLNDIMIRR 260
Cdd:cd18008   214 DISKPFSKndrkalerLQALLKPILLRR 241
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
41-216 2.45e-19

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: 88.59  E-value: 2.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGIVFALRR--DGR-CMVADEMGLGKTIQAIAI------------------AYFYKEEW------PLLIVVPSS 93
Cdd:cd18005     1 LRDYQREGVEFMYDLykNGRgGILGDDMGLGKTVQVIAFlaavlgktgtrrdrennrPRFKKKPPassakkPVLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   94 LRYPWIEELEKWiPELEPEEINVVMNKtdigRIPGSRVTVLGYGLLTTDAETL---LDALNTQNFRVVIVDESHYMKSRT 170
Cdd:cd18005    81 VLYNWKDELDTW-GHFEVGVYHGSRKD----DELEGRLKAGRLEVVVTTYDTLrrcIDSLNSINWSAVIADEAHRIKNPK 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 568908697  171 AARSKILLPMVQKARraILLTGTPALGRPEELFMQIEALFPQKFGT 216
Cdd:cd18005   156 SKLTQAMKELKCKVR--IGLTGTLLQNNMKELWCLLDWAVPGALGS 199
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
60-260 4.47e-19

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: 87.56  E-value: 4.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   60 MVADEMGLGKTIQAIAIAYFYKEE---W-PLLIVVPSSLRYPWIEELEKWIPELE-------PEEINVVMN----KTDIG 124
Cdd:cd18002    23 ILADEMGLGKTVQSIAVLAHLAEEhniWgPFLVIAPASTLHNWQQEISRFVPQFKvlpywgnPKDRKVLRKfwdrKNLYT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  125 RIPGSRVTVLGYGLLTTDAETlldaLNTQNFRVVIVDESHYMKSRTAARSKILLPMvqKARRAILLTGTPALGRPEELFM 204
Cdd:cd18002   103 RDAPFHVVITSYQLVVQDEKY----FQRVKWQYMVLDEAQAIKSSSSSRWKTLLSF--HCRNRLLLTGTPIQNSMAELWA 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568908697  205 QIEALFPQKFGTWIEYAKrycnahvrYFGKRRQWDCRGASNLSE-----LHQLLNDIMIRR 260
Cdd:cd18002   177 LLHFIMPTLFDSHDEFNE--------WFSKDIESHAENKTGLNEhqlkrLHMILKPFMLRR 229
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
41-260 4.56e-19

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: 86.34  E-value: 4.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGI---VFALRRDGRCMVADEMGLGKTIQAIAIAY-FYKE---EWPLLIVVPSSLRYPWIEELEKWIPELEpee 113
Cdd:cd17994     1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTIQTIVFLYsLYKEghsKGPFLVSAPLSTIINWEREFEMWAPDFY--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  114 inVVMnktdigrIPGSRVTVLGYGLLTTDAETlldaLNTQNFRVVIVDESHYMKSRTAARSKILlpMVQKARRAILLTGT 193
Cdd:cd17994    78 --VVT-------YVGDHVLLTSYELISIDQAI----LGSIDWAVLVVDEAHRLKNNQSKFFRIL--NSYKIGYKLLLTGT 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568908697  194 PALGRPEELFMQIEALFPQKFGTWIEYAKRYCNahvryFGKRRQwdcrgasnLSELHQLLNDIMIRR 260
Cdd:cd17994   143 PLQNNLEELFHLLNFLTPERFNNLQGFLEEFAD-----ISKEDQ--------IKKLHDLLGPHMLRR 196
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
62-262 1.20e-18

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: 86.27  E-value: 1.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   62 ADEMGLGKTIQAIA-IAYFY---KEEWPLLIVVPSSLRYPWIEELEKWIPELE-------PEEinvvmNKTDIGRIPGSR 130
Cdd:cd17996    28 ADEMGLGKTIQTISlITYLMekkKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSkivykgtPDV-----RKKLQSQIRAGK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  131 VTVlgygLLTTDAETLLD--ALNTQNFRVVIVDESHYMKSRTAARSKILLPMVQkARRAILLTGTPALGRPEELFMQIEA 208
Cdd:cd17996   103 FNV----LLTTYEYIIKDkpLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYH-ARYRLLLTGTPLQNNLPELWALLNF 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568908697  209 LFPQKFGTwIEYAKRYCNAHVRYFGKRRQWDCRGASNL---SELHQLLNDIMIRRLK 262
Cdd:cd17996   178 LLPKIFKS-CKTFEQWFNTPFANTGEQVKIELNEEETLliiRRLHKVLRPFLLRRLK 233
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
41-224 2.27e-18

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: 85.67  E-value: 2.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGIVF------ALRRDGR--CMVADEMGLGKTIQAIAIAYFYKEEWP---------LLIVVPSSLRYPWIEELE 103
Cdd:cd18066     1 LRPHQREGIEFlyecvmGMRVNERfgAILADEMGLGKTLQCISLIWTLLRQGPyggkpvikrALIVTPGSLVKNWKKEFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  104 KWipeLEPEEINVVMNKTD-----IGRIPGSRVTVLGYGLLTTDaetlLDALNTQNFRVVIVDESHYMKSRTAARSKILL 178
Cdd:cd18066    81 KW---LGSERIKVFTVDQDhkveeFIASPLYSVLIISYEMLLRS----LDQISKLNFDLVICDEGHRLKNTSIKTTTALT 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 568908697  179 PMvqKARRAILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRY 224
Cdd:cd18066   154 SL--SCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVY 197
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
62-262 6.97e-18

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: 83.91  E-value: 6.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   62 ADEMGLGKTIQAIAIAYFYKE----EWPLLIVVPSSLRYPWIEELEKWIPELepeeiNVVM---NKTDIGRIPGSRVTVL 134
Cdd:cd17997    28 ADEMGLGKTLQTISLLGYLKHykniNGPHLIIVPKSTLDNWMREFKRWCPSL-----RVVVligDKEERADIIRDVLLPG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  135 GYGLLTTDAETLL---DALNTQNFRVVIVDESHYMKSRTAARSKILLPMVQKARraILLTGTPALGRPEELFMQIEALFP 211
Cdd:cd17997   103 KFDVCITSYEMVIkekTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNR--LLLTGTPLQNNLHELWALLNFLLP 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568908697  212 QKFGTWIEYakrycnahvryfgkrRQW----DCRGASN--LSELHQLLNDIMIRRLK 262
Cdd:cd17997   181 DVFTSSEDF---------------DEWfnvnNCDDDNQevVQRLHKVLRPFLLRRIK 222
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
40-272 1.49e-17

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: 83.56  E-value: 1.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   40 KLLPFQKDGI--VFALRRDG-RCMVADEMGLGKTIQAIAIAYFYKE----EWPLLIVVPSSLRYPWIEELEKWIPELepE 112
Cdd:cd18064    15 KLRDYQVRGLnwLISLYENGiNGILADEMGLGKTLQTISLLGYMKHyrniPGPHMVLVPKSTLHNWMAEFKRWVPTL--R 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  113 EINVVMNKTDIGR------IPGS-RVTVLGYGLLTTDAETlldaLNTQNFRVVIVDESHYMKSRTAARSKILLPMvqKAR 185
Cdd:cd18064    93 AVCLIGDKDQRAAfvrdvlLPGEwDVCVTSYEMLIKEKSV----FKKFNWRYLVIDEAHRIKNEKSKLSEIVREF--KTT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  186 RAILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKrycnahvrYFGKRrqwDCRGASNLSE-LHQLLNDIMIRRLKSE 264
Cdd:cd18064   167 NRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDS--------WFDTN---NCLGDQKLVErLHMVLRPFLLRRIKAD 235

                  ....*...
gi 568908697  265 VLSQLPPK 272
Cdd:cd18064   236 VEKSLPPK 243
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
40-262 4.48e-17

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: 81.66  E-value: 4.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   40 KLLPFQKDGI--VFALRRDG-RCMVADEMGLGKTIQAIAIAYFYKEE--W-PLLIVVPSSLRYPWIEELEKWIPEL---- 109
Cdd:cd18009     3 VMRPYQLEGMewLRMLWENGiNGILADEMGLGKTIQTIALLAHLRERgvWgPFLVIAPLSTLPNWVNEFARFTPSVpvll 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  110 ------EPEEINVVMNKTDiGRIPGSRVTVLGYGLLTTDAetllDALNTQNFRVVIVDESHYMKSrtaARSKIL--LPMV 181
Cdd:cd18009    83 yhgtkeERERLRKKIMKRE-GTLQDFPVVVTSYEIAMRDR----KALQHYAWKYLIVDEGHRLKN---LNCRLIqeLKTF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  182 QKARRaILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRY----CNAhvRYFGKRRQWDCRGASNLSELHQLLNDIM 257
Cdd:cd18009   155 NSDNR-LLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFdfssLSD--NAADISNLSEEREQNIVHMLHAILKPFL 231

                  ....*
gi 568908697  258 IRRLK 262
Cdd:cd18009   232 LRRLK 236
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
41-194 7.56e-17

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


Pssm-ID: 350765 [Multi-domain]  Cd Length: 239  Bit Score: 81.18  E-value: 7.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGIVFALRR----------DGRCMVADEMGLGKTIQAIAIAYFYKEEWPL----LIVVPSSLRYPWIEELEKWI 106
Cdd:cd18007     1 LKPHQVEGVRFLWSNlvgtdvgsdeGGGCILAHTMGLGKTLQVITFLHTYLAAAPRrsrpLVLCPASTLYNWEDEFKKWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  107 P-ELEPEEINVVMN--KTDIGRIP--------GSrVTVLGYGL---LTTDAET---------LLDALNTQNfrVVIVDES 163
Cdd:cd18007    81 PpDLRPLLVLVSLSasKRADARLRkinkwhkeGG-VLLIGYELfrnLASNATTdprlkqefiAALLDPGPD--LLVLDEG 157
                         170       180       190
                  ....*....|....*....|....*....|.
gi 568908697  164 HYMKSRTAARSKILlpMVQKARRAILLTGTP 194
Cdd:cd18007   158 HRLKNEKSQLSKAL--SKVKTKRRILLTGTP 186
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
62-261 3.08e-16

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: 78.93  E-value: 3.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   62 ADEMGLGKTIQAIA-IAYF--YKEEW-PLLIVVPSSLRYPWIEELEKWIPEL----------EPEEINVVMNKTDigrip 127
Cdd:cd18003    25 ADEMGLGKTIQTIAlLAHLacEKGNWgPHLIVVPTSVMLNWEMEFKRWCPGFkiltyygsakERKLKRQGWMKPN----- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  128 GSRVTVLGYGLLTTDAEtlldALNTQNFRVVIVDESHYMKSRTAARSKILLPMvqKARRAILLTGTPALGRPEELFMQIE 207
Cdd:cd18003   100 SFHVCITSYQLVVQDHQ----VFKRKKWKYLILDEAHNIKNFKSQRWQTLLNF--NTQRRLLLTGTPLQNSLMELWSLMH 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568908697  208 ALFPQKFGTWIEYakrycnahvryfgkrRQWDCRGASNLSELHQLLNDIMIRRL 261
Cdd:cd18003   174 FLMPHIFQSHQEF---------------KEWFSNPLTAMSEGSQEENEELVRRL 212
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
41-260 3.97e-16

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: 78.93  E-value: 3.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGI---VFALRRDGRCMVADEMGLGKTIQAIAIAY---------FYKEEWPLLIVVPSSLRYPWIEELEKWIPE 108
Cdd:cd17999     1 LRPYQQEGInwlAFLNKYNLHGILCDDMGLGKTLQTLCILAsdhhkransFNSENLPSLVVCPPTLVGHWVAEIKKYFPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  109 LEPEEINVVMNKTDIGRIPG----SRVTVLGYGLLTTDAETLLDalntQNFRVVIVDESHYMKSrtaARSKILLPMVQ-K 183
Cdd:cd17999    81 AFLKPLAYVGPPQERRRLREqgekHNVIVASYDVLRNDIEVLTK----IEWNYCVLDEGHIIKN---SKTKLSKAVKQlK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  184 ARRAILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRYcnahVRYFGKRRQWDC------RGASNLSELHQLLNDIM 257
Cdd:cd17999   154 ANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRF----LKPILASRDSKAsakeqeAGALALEALHKQVLPFL 229

                  ...
gi 568908697  258 IRR 260
Cdd:cd17999   230 LRR 232
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
59-260 6.06e-16

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: 78.55  E-value: 6.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   59 CMVADEMGLGKTIQAIA-IAYFYKEEW---PLLIVVPSSLRYPWIEELEKWIPELepeeiNVVMNKTDIGRIPGSR---- 130
Cdd:cd18053    42 CILADEMGLGKTIQTISfLNYLFHEHQlygPFLLVVPLSTLTSWQREIQTWAPQM-----NAVVYLGDINSRNMIRthew 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  131 ----VTVLGYGLLTTDAETLLDA---LNTQNFRVVIVDESHYMKSRTAARSKILLPMvqKARRAILLTGTPALGRPEELF 203
Cdd:cd18053   117 mhpqTKRLKFNILLTTYEILLKDksfLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDF--KSNHRLLITGTPLQNSLKELW 194
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568908697  204 MQIEALFPQKFGTWIEYAKRYcnahvryfGKRRQwdcrgaSNLSELHQLLNDIMIRR 260
Cdd:cd18053   195 SLLHFIMPEKFSSWEDFEEEH--------GKGRE------YGYASLHKELEPFLLRR 237
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
41-260 8.40e-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: 77.48  E-value: 8.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGIVFALRRDGR---CMVADEMGLGKTIQAIAI----AYFYKEEWPLLIVVPSSLRYPWIEELEKWIPELE--- 110
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEqhgCILGDEMGLGKTCQTISLlwylAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSvit 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  111 ---PEEINVVMNKtDIGRIPGSRVtvlgygLLTTDAETLLDA--LNTQNFRVVIVDESHYMKSRTAARSKILLPmvQKAR 185
Cdd:cd18006    81 ymgDKEKRLDLQQ-DIKSTNRFHV------LLTTYEICLKDAsfLKSFPWASLVVDEAHRLKNQNSLLHKTLSE--FSVD 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568908697  186 RAILLTGTPALGRPEELFMQIEALFPQKFGtwIEYAKRYcnahVRYFGKRRqwdcRGASNLSELHQLLNDIMIRR 260
Cdd:cd18006   152 FRLLLTGTPIQNSLQELYALLSFIEPNVFP--KDKLDDF----IKAYSETD----DESETVEELHLLLQPFLLRR 216
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
41-260 1.71e-15

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: 77.51  E-value: 1.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGIVFAL-----RRDGR---CMVADEMGLGKTIQAIAIAYFYKEEWP--------LLIVVPSSLRYPWIEELEK 104
Cdd:cd18067     1 LRPHQREGVKFLYrcvtgRRIRGshgCIMADEMGLGKTLQCITLMWTLLRQSPqckpeidkAIVVSPSSLVKNWANELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  105 WI-PELEPEEINVVMNKTDIGRIPGS---RVTVLGYGLLTTDAETL---LDALNTQNFRVVIVDESHYMKSRTAARSKIL 177
Cdd:cd18067    81 WLgGRLQPLAIDGGSKKEIDRKLVQWasqQGRRVSTPVLIISYETFrlhVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  178 LPMvqKARRAILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRYCNAHVRyfG-------KRRQwdcRGASNLSELH 250
Cdd:cd18067   161 DSL--NTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILK--GrdadaseKERQ---LGEEKLQELI 233
                         250
                  ....*....|
gi 568908697  251 QLLNDIMIRR 260
Cdd:cd18067   234 SIVNRCIIRR 243
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
334-439 7.15e-15

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: 71.47  E-value: 7.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   334 IKMLLQNDSLKFLVFAHHLSMLQaCTEAVIESKSRYIRIDGSVPSSERIHLVNQFqKDPDTRVaILSIQAAGQGLTFTAA 413
Cdd:pfam00271    7 LELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDF-RKGKIDV-LVATDVAERGLDLPDV 83
                           90       100
                   ....*....|....*....|....*.
gi 568908697   414 SHVVFAELYWDPGHIKQAEDRAHRIG 439
Cdd:pfam00271   84 DLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
41-260 7.69e-15

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: 75.09  E-value: 7.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGI---VFALRRDGRCMVADEMGLGKTIQAIAI---AYFYKEEWPLLIVVPSSLRYPWIEELEKWIpelepeEI 114
Cdd:cd18060     1 LREYQLEGVnwlLFNWYNRQNCILADEMGLGKTIQSIAFlqeVYNVGIHGPFLVIAPLSTITNWEREFNTWT------EM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  115 NVVMN-----------------KTDIGR-IPGSrvtvLGYGLLTTDAETLLD---ALNTQNFRVVIVDESHYMKSRTAar 173
Cdd:cd18060    75 NTIVYhgslasrqmiqqyemycKDSRGRlIPGA----YKFDALITTFEMILSdcpELREIEWRCVIIDEAHRLKNRNC-- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  174 sKIL--LPMVQKARRaILLTGTPALGRPEELFMQIEALFPQKFGTWIEYakrycnahVRYFGkrrqwDCRGASNLSELHQ 251
Cdd:cd18060   149 -KLLdsLKHMDLEHK-VLLTGTPLQNTVEELFSLLHFLEPSQFPSESEF--------LKDFG-----DLKTEEQVQKLQA 213

                  ....*....
gi 568908697  252 LLNDIMIRR 260
Cdd:cd18060   214 ILKPMMLRR 222
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
60-262 1.00e-14

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: 75.48  E-value: 1.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   60 MVADEMGLGKTIQAIAIAYFYKEE----WPLLIVVPSSLRYPWIEELEKWIPELEPEEI--NVVMNKTDIGRIPGSRVTV 133
Cdd:cd18063    46 ILADEMGLGKTIQTIALITYLMEHkrlnGPYLIIVPLSTLSNWTYEFDKWAPSVVKISYkgTPAMRRSLVPQLRSGKFNV 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  134 lgygLLTTDAETLLDA--LNTQNFRVVIVDESHYMKSRTAARSKILLPMVQKARRaILLTGTPALGRPEELFMQIEALFP 211
Cdd:cd18063   126 ----LLTTYEYIIKDKhiLAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRR-ILLTGTPLQNKLPELWALLNFLLP 200
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568908697  212 QKFGTWIEYaKRYCNAHVRYFGKRRQWDCRGAS-NLSELHQLLNDIMIRRLK 262
Cdd:cd18063   201 TIFKSCSTF-EQWFNAPFAMTGERVDLNEEETIlIIRRLHKVLRPFLLRRLK 251
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
41-211 2.06e-14

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: 72.74  E-value: 2.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGIVFALRRDGRC---MVADEMGLGKTIQAIA----IAYFYKEEWPLLIVVPSSLRYPWIEELEKWIPELEpee 113
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRvggILGDEMGLGKTIQIIAflaaLHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFR--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  114 iNVVMNKTDIGRIPGS------------RVTVLGYGLLTTDAETLL---DALNTQNFRVVIVDESHYMKSRTAARSKIL- 177
Cdd:cd18000    78 -VVVLHSSGSGTGSEEklgsierksqliRKVVGDGGILITTYEGFRkhkDLLLNHNWQYVILDEGHKIRNPDAEITLACk 156
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568908697  178 -LPMVQKarraILLTGTPALGRPEELFMQIEALFP 211
Cdd:cd18000   157 qLRTPHR----LILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
41-194 3.51e-14

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: 73.17  E-value: 3.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGI-----VFALRRDGrcMVADEMGLGKTIQAIA-IAYFYKEEW--PLLIVVPSSLRYPWIEELEKWIPELEPE 112
Cdd:cd18001     1 LYPHQREGVawlwsLHDGGKGG--ILADDMGLGKTVQICAfLSGMFDSGLikSVLVVMPTSLIPHWVKEFAKWTPGLRVK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  113 E---INVVMNKTDIGRIPGSRVTVLG-YGLLTTDAETlLDALNTQNFR--VVIVDESHYMKSRTAARSKILLPMVQKARr 186
Cdd:cd18001    79 VfhgTSKKERERNLERIQRGGGVLLTtYGMVLSNTEQ-LSADDHDEFKwdYVILDEGHKIKNSKTKSAKSLREIPAKNR- 156

                  ....*...
gi 568908697  187 aILLTGTP 194
Cdd:cd18001   157 -IILTGTP 163
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
60-262 1.05e-13

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: 72.38  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   60 MVADEMGLGKTIQAIAIAYFYKE----EWPLLIVVPSSLRYPWIEELEKWIPELepeeINVVMNKTDIGR---IPGSR-- 130
Cdd:cd18062    46 ILADEMGLGKTIQTIALITYLMEhkriNGPFLIIVPLSTLSNWVYEFDKWAPSV----VKVSYKGSPAARrafVPQLRsg 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  131 ---VTVLGYGLLTTDAETLLDAlntqNFRVVIVDESHYMKSRTAARSKILLPMVQKARRaILLTGTPALGRPEELFMQIE 207
Cdd:cd18062   122 kfnVLLTTYEYIIKDKQILAKI----RWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRR-LLLTGTPLQNKLPELWALLN 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568908697  208 ALFPQKFGTWIEYaKRYCNAHVRYFGKRRQWDCRGAS-NLSELHQLLNDIMIRRLK 262
Cdd:cd18062   197 FLLPTIFKSCSTF-EQWFNAPFAMTGEKVDLNEEETIlIIRRLHKVLRPFLLRRLK 251
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
44-224 1.94e-13

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: 71.00  E-value: 1.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   44 FQKDGIVFALRR----DG-RCMVADEMGLGKTIQAIAIAYFYKEEWPL---LIVVPSSLRYPWIEELEKWIPelEPEEIN 115
Cdd:cd18069    11 FLYDNIIESLERykgsSGfGCILAHSMGLGKTLQVISFLDVLLRHTGAktvLAIVPVNTLQNWLSEFNKWLP--PPEALP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  116 VVMNKTdigripgSRVTVLGYGLLTTDAETLLDA----------LNTQNFR------VVIVDESHYMKSRTAARSKILLP 179
Cdd:cd18069    89 NVRPRP-------FKVFILNDEHKTTAARAKVIEdwvkdggvllMGYEMFRlrpgpdVVICDEGHRIKNCHASTSQALKN 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568908697  180 MvqKARRAILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRY 224
Cdd:cd18069   162 I--RSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 204
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
60-262 2.01e-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: 71.20  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   60 MVADEMGLGKTIQAIAIAYFYKE----EWPLLIVVPSSLRYPWIEELEKWIPELE------PEEINVVMNKTDIgrIPGS 129
Cdd:cd18065    38 ILADEMGLGKTLQTIALLGYLKHyrniPGPHMVLVPKSTLHNWMNEFKRWVPSLRavcligDKDARAAFIRDVM--MPGE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  130 -RVTVLGYGLLTTDAETlldaLNTQNFRVVIVDESHYMKSRTAARSKILLPMvqKARRAILLTGTPALGRPEELFMQIEA 208
Cdd:cd18065   116 wDVCVTSYEMVIKEKSV----FKKFNWRYLVIDEAHRIKNEKSKLSEIVREF--KTTNRLLLTGTPLQNNLHELWALLNF 189
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568908697  209 LFPQKFGTWIEYAKrycnahvrYFGKRrqwDCRGASNLSE-LHQLLNDIMIRRLK 262
Cdd:cd18065   190 LLPDVFNSADDFDS--------WFDTK---NCLGDQKLVErLHAVLKPFLLRRIK 233
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
41-260 3.27e-13

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: 70.48  E-value: 3.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGI---VFALRRDGRCMVADEMGLGKTIQAIAIAY-FYKE---EWPLLIVVPSSLRYPWIEELEKWIPEL---- 109
Cdd:cd18057     1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTVQTIVFLYsLYKEghsKGPYLVSAPLSTIINWEREFEMWAPDFyvvt 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  110 ------------EPE---EINVVMNKTDIGRIPGS-----RVTVLGYGLLTTDAETlldaLNTQNFRVVIVDESHYMKSR 169
Cdd:cd18057    81 ytgdkesrsvirENEfsfEDNAIRSGKKVFRMKKEaqikfHVLLTSYELITIDQAI----LGSIEWACLVVDEAHRLKNN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  170 TAARSKILLPMvqKARRAILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRYCnahvryfgkrrqwDCRGASNLSEL 249
Cdd:cd18057   157 QSKFFRVLNSY--KIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA-------------DISKEDQIKKL 221
                         250
                  ....*....|.
gi 568908697  250 HQLLNDIMIRR 260
Cdd:cd18057   222 HDLLGPHMLRR 232
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
41-226 3.39e-13

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: 70.69  E-value: 3.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGIVF-----------ALRRDGR-CMVADEMGLGKTIQAIAIAY--FYKEEWP----LLIVVPSSLRYPWIEEL 102
Cdd:cd18068     1 LKPHQVDGVQFmwdccceslkkTKKSPGSgCILAHCMGLGKTLQVVTFLHtvLLCEKLEnfsrVLVVCPLNTVLNWLNEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  103 EKWIPELEPEEINVVMNKTDIGRIPGSR-----------VTVLGYGL---LTTD---------AETLLDALNTQNFRVVI 159
Cdd:cd18068    81 EKWQEGLKDEEKIEVNELATYKRPQERSyklqrwqeeggVMIIGYDMyriLAQErnvksreklKEIFNKALVDPGPDFVV 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568908697  160 VDESHYMKSRTAARSKILLPMvqKARRAILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRYCN 226
Cdd:cd18068   161 CDEGHILKNEASAVSKAMNSI--RTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVN 225
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
59-260 6.08e-13

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: 69.30  E-value: 6.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   59 CMVADEMGLGKTIQAIAIAY---FYKEEWPLLIVVPSSLRYPWIEELEKWIpelepeEIN-VVMNKTDIgripgSRVTVL 134
Cdd:cd18058    22 CILADEMGLGKTIQSITFLSeifLMGIRGPFLIIAPLSTITNWEREFRTWT------EMNaIVYHGSQI-----SRQMIQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  135 GY-------------------GLLTTDAETLLDA--LNTQNFRVVIVDESHYMKSRTAARSKILLPMVQKARraILLTGT 193
Cdd:cd18058    91 QYemyyrdeqgnplsgifkfqVVITTFEMILADCpeLKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALEHK--VLLTGT 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568908697  194 PALGRPEELFMQIEALFPQKFGTWIEYAKRycnahvryFGkrrqwDCRGASNLSELHQLLNDIMIRR 260
Cdd:cd18058   169 PLQNSVEELFSLLNFLEPSQFPSETTFLEE--------FG-----DLKTEEQVKKLQSILKPMMLRR 222
HELICc smart00490
helicase superfamily c-terminal domain;
368-439 6.68e-13

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 64.93  E-value: 6.68e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568908697    368 RYIRIDGSVPSSERIHLVNQFQKDPdtRVAILSIQAAGQGLTFTAASHVVFAELYWDPGHIKQAEDRAHRIG 439
Cdd:smart00490   13 KVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
41-260 2.01e-12

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: 67.75  E-value: 2.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGI---VFALRRDGRCMVADEMGLGKTIQAIAIAY-FYKE--EWPLLIVVPSSLRYPWIEELEKWIpelepeEI 114
Cdd:cd18059     1 LREYQLEGVnwlLFNWYNTRNCILADEMGLGKTIQSITFLYeIYLKgiHGPFLVIAPLSTIPNWEREFRTWT------EL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  115 NVVMNKTDIG------------RIPGSRVTVLGY---GLLTTDAETLLDALNTQN--FRVVIVDESHYMKSRTAarsKIL 177
Cdd:cd18059    75 NVVVYHGSQAsrrtiqlyemyfKDPQGRVIKGSYkfhAIITTFEMILTDCPELRNipWRCVVIDEAHRLKNRNC---KLL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  178 --LPMVQKARRaILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRycnahvryFGkrrqwDCRGASNLSELHQLLND 255
Cdd:cd18059   152 egLKMMDLEHK-VLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQE--------FG-----DLKTEEQVQKLQAILKP 217

                  ....*
gi 568908697  256 IMIRR 260
Cdd:cd18059   218 MMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
41-260 2.71e-12

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: 67.78  E-value: 2.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGI---VFALRRDGRCMVADEMGLGKTIQAIAIAY-FYKE---EWPLLIVVPSSLRYPWIEELEKWIPEL---- 109
Cdd:cd18056     1 LHPYQLEGLnwlRFSWAQGTDTILADEMGLGKTVQTAVFLYsLYKEghsKGPFLVSAPLSTIINWEREFEMWAPDMyvvt 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  110 ------------EPE---EINVVMNKTDIGRIPGS-----RVTVLGYGLLTTDaetlLDALNTQNFRVVIVDESHYMKSR 169
Cdd:cd18056    81 yvgdkdsraiirENEfsfEDNAIRGGKKASRMKKEasvkfHVLLTSYELITID----MAILGSIDWACLIVDEAHRLKNN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  170 TAARSKILLPMvqKARRAILLTGTPALGRPEELFMQIEALFPQKFGTWIEYAKRYCnahvryfgkrrqwDCRGASNLSEL 249
Cdd:cd18056   157 QSKFFRVLNGY--SLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFA-------------DIAKEDQIKKL 221
                         250
                  ....*....|.
gi 568908697  250 HQLLNDIMIRR 260
Cdd:cd18056   222 HDMLGPHMLRR 232
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
43-226 2.99e-12

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: 67.37  E-value: 2.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   43 PFQKDGIVFALRRDGRCMVADeMGLGKT---IQAIAIAYFYKEEWPLLIVVPSSL-RYPWIEELEKWipELEPEEINVVM 118
Cdd:cd18013     3 PYQKVAINFIIEHPYCGLFLD-MGLGKTvttLTALSDLQLDDFTRRVLVIAPLRVaRSTWPDEVEKW--NHLRNLTVSVA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  119 NKTDIGRIP----GSRVTVLGYGLLttdaETLLDALNTQ-NFRVVIVDESHYMKSRTAARSKILLPMVQKARRAILLTGT 193
Cdd:cd18013    80 VGTERQRSKaantPADLYVINRENL----KWLVNKSGDPwPFDMVVIDELSSFKSPRSKRFKALRKVRPVIKRLIGLTGT 155
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568908697  194 PALGRPEELFMQIEAL-FPQKFGTWIE-YAKRYCN 226
Cdd:cd18013   156 PSPNGLMDLWAQIALLdQGERLGRSITaYRERWFD 190
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
60-204 3.45e-12

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: 67.49  E-value: 3.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   60 MVADEMGLGKTIQAIAIAYFYkeewPLLIVVPSSLRYPWIEELEKWIpelEPEEINVVM----NKT-DIGRIPGSRVTVL 134
Cdd:cd18071    52 ILADDMGLGKTLTTISLILAN----FTLIVCPLSVLSNWETQFEEHV---KPGQLKVYTyhggERNrDPKLLSKYDIVLT 124
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568908697  135 GYGLLTTDAETLLDA-LNTQNFRVVIVDESHYMKSRTAARSKILLPMvqKARRAILLTGTPALGRPEELFM 204
Cdd:cd18071   125 TYNTLASDFGAKGDSpLHTINWLRVVLDEGHQIRNPNAQQTKAVLNL--SSERRWVLTGTPIQNSPKDLGS 193
DpdE NF041062
protein DpdE;
58-200 2.65e-11

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 68.07  E-value: 2.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   58 RCMVADEMGLGKTIQAIAIAYFYKEEWP---LLIVVPSSLRYPWIEELEkwipelepeeinvvmNKTDIGRIPGSRVTVL 134
Cdd:NF041062  172 RYLLADEVGLGKTIEAGLVIRQHLLDNPdarVLVLVPDALVRQWRRELR---------------DKFFLDDFPGARVRVL 236
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568908697  135 GYglltTDAETLLDalNTQNFRVVIVDESHYM-------KSRTAARSKILLPMVQKARRAILLTGTPALGRPE 200
Cdd:NF041062  237 SH----EEPERWEP--LLDAPDLLVVDEAHQLarlawsgDPPERARYRELAALAHAAPRLLLLSATPVLGNEE 303
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
60-260 4.01e-11

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. CHD3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350813 [Multi-domain]  Cd Length: 232  Bit Score: 64.26  E-value: 4.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   60 MVADEMGLGKTIQAIAIAY-FYKE---EWPLLIVVPSSLRYPWIEELEKWIPEL----------------EPE---EINV 116
Cdd:cd18055    23 ILADEMGLGKTIQTIVFLYsLYKEghtKGPFLVSAPLSTIINWEREFQMWAPDFyvvtytgdkdsraiirENEfsfDDNA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  117 VMNKTDIGRIPGS-----RVTVLGYGLLTTDAetllDALNTQNFRVVIVDESHYMKSRTAARSKILLPMvqKARRAILLT 191
Cdd:cd18055   103 VKGGKKAFKMKREaqvkfHVLLTSYELVTIDQ----AALGSIRWACLVVDEAHRLKNNQSKFFRVLNGY--KIDHKLLLT 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568908697  192 GTPALGRPEELFMQIEALFPQKFGTWIEYAKRYCnahvryfgkrrqwDCRGASNLSELHQLLNDIMIRR 260
Cdd:cd18055   177 GTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFA-------------DISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
41-260 7.07e-11

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: 63.49  E-value: 7.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGIVFAL-----RRDgrCMVADEMGLGKTIQAIAIAY-FYKE--EWPLLIVVPSSLRYPWIEELEKWIpelepe 112
Cdd:cd18061     1 LREYQLEGLNWLLfnwynRRN--CILADEMGLGKTIQSITFLYeILLTgiRGPFLIIAPLSTIANWEREFRTWT------ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  113 EINVVMNKTDI------------GRIPGSRVTVLGYGL--LTTDAETLLDA---LNTQNFRVVIVDESHYMKSRTAARSK 175
Cdd:cd18061    73 DLNVVVYHGSLisrqmiqqyemyFRDSQGRIIRGAYRFqaIITTFEMILGGcpeLNAIDWRCVIIDEAHRLKNKNCKLLE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  176 ILLPMvqKARRAILLTGTPALGRPEELFMQIEALFPQKFGTWieyakrycNAHVRYFGkrrqwDCRGASNLSELHQLLND 255
Cdd:cd18061   153 GLKLM--NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSE--------STFMQEFG-----DLKTEEQVQKLQAILKP 217

                  ....*
gi 568908697  256 IMIRR 260
Cdd:cd18061   218 MMLRR 222
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
40-419 7.45e-11

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 66.20  E-value: 7.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   40 KLLPFQKDGI--VFALRRDG--RCMVADEMGLGKTIQAIAIAYFYKEEWPLLIVVPS-SLRYPWIEELEKWIPelepeEI 114
Cdd:COG1061    80 ELRPYQQEALeaLLAALERGggRGLVVAPTGTGKTVLALALAAELLRGKRVLVLVPRrELLEQWAEELRRFLG-----DP 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  115 NVVMNKTDIGRipgsRVTVLGYGLLTTDAEtlLDALNtQNFRVVIVDESHymksRTAARS-KILLPMVQKARRaILLTGT 193
Cdd:COG1061   155 LAGGGKKDSDA----PITVATYQSLARRAH--LDELG-DRFGLVIIDEAH----HAGAPSyRRILEAFPAAYR-LGLTAT 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  194 PAL--GRPEELFMqiealfpqkfgtwieyakrycnahvrYFGKRRQWDcrgasnlseLHQLLNDIMIRrlksevlsqlPP 271
Cdd:COG1061   223 PFRsdGREILLFL--------------------------FDGIVYEYS---------LKEAIEDGYLA----------PP 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  272 KVRQRipfdlppaavkelnasFEEWQKLMRapnsgAMETVMGLITRMFKQTAIAKAGAVKDYIKMLLQNDslKFLVFAHH 351
Cdd:COG1061   258 EYYGI----------------RVDLTDERA-----EYDALSERLREALAADAERKDKILRELLREHPDDR--KTLVFCSS 314
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568908697  352 LSMLQACTEAVIESKSRYIRIDGSVPSSERIHLVNQFQKDPDTrvAILSIQAAGQGLTFTAASHVVFA 419
Cdd:COG1061   315 VDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELR--ILVTVDVLNEGVDVPRLDVAILL 380
HNHc cd00085
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ...
1025-1090 5.22e-08

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: 50.55  E-value: 5.22e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568908697 1025 KSHRKSLLNAAWTAKLPLEqlnemlrnPGEGHFWQVDHIRPVyEGGGQCSLDNLQTLCTVCHKERT 1090
Cdd:cd00085     1 RSHRLVLLARDGLCPYCGK--------PGGTEGLEVDHIIPL-SDGGNNDLDNLVLLCRKCHRKKH 57
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
41-194 8.67e-08

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 52.31  E-value: 8.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGI--VFALRRDGRCMVADEMGLGKTIQAIA-IAYFYKEewPLLIVVPS-SLRYPWIEELEKWIPELEPEEINV 116
Cdd:cd17926     1 LRPYQEEALeaWLAHKNNRRGILVLPTGSGKTLTALAlIAYLKEL--RTLIVVPTdALLDQWKERFEDFLGDSSIGLIGG 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568908697  117 VMNKTDIGRIpgsrVTVLGYGLLTTDAETLLDALNtqNFRVVIVDESHYMKSRTAARskiLLPMVQKARRaILLTGTP 194
Cdd:cd17926    79 GKKKDFDDAN----VVVATYQSLSNLAEEEKDLFD--QFGLLIVDEAHHLPAKTFSE---ILKELNAKYR-LGLTATP 146
McrA COG1403
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];
994-1087 6.03e-06

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


Pssm-ID: 441013 [Multi-domain]  Cd Length: 64  Bit Score: 44.97  E-value: 6.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  994 LRAQVFATEHGVCQHCGvdaqelflrmrdapkshrksllnaawtaklpleqlnemlrNPGEGHFWQVDHIRPVYEGGGQc 1073
Cdd:COG1403    10 LRRAVLKRDNGRCQYCG----------------------------------------RPFSGDALEVDHIIPRSRGGTD- 48
                          90
                  ....*....|....
gi 568908697 1074 SLDNLQTLCTVCHK 1087
Cdd:COG1403    49 TWENLVLLCRRCNR 62
HNH pfam01844
HNH endonuclease; His-Asn-His (HNH) proteins are a very common family of small nucleic ...
1057-1092 7.24e-06

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: 43.88  E-value: 7.24e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 568908697  1057 FWQVDHIRPVYEGGGQcSLDNLQTLCTVCHKERTAQ 1092
Cdd:pfam01844   13 ALTVDHIIPLSDGGAD-DIENLILLCPSCHNKKHNR 47
ResIII pfam04851
Type III restriction enzyme, res subunit;
66-194 8.39e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 47.28  E-value: 8.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697    66 GLGKTIQAIAIAYFYKEEWPL---LIVVPS-SLRYPWIEELEKWIPELEPEEINVVMNKTDIGRiPGSRVTVLGYGLLTT 141
Cdd:pfam04851   33 GSGKTLTAAKLIARLFKKGPIkkvLFLVPRkDLLEQALEEFKKFLPNYVEIGEIISGDKKDESV-DDNKIVVTTIQSLYK 111
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568908697   142 DAETLLDALNTQNFRVVIVDESHymksRTAARS-KILLPMVQKARRaILLTGTP 194
Cdd:pfam04851  112 ALELASLELLPDFFDVIIIDEAH----RSGASSyRNILEYFKPAFL-LGLTATP 160
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
41-107 1.77e-04

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: 44.64  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   41 LLPFQKDGIVFALRRDGrcMVADEMGLGKTIQAIAI-------------AYFYKEEWPL----------------LIVVP 91
Cdd:cd18070     1 LLPYQRRAVNWMLVPGG--ILADEMGLGKTVEVLALillhprpdndldaADDDSDEMVCcpdclvaetpvsskatLIVCP 78
                          90
                  ....*....|....*.
gi 568908697   92 SSLRYPWIEELEKWIP 107
Cdd:cd18070    79 SAILAQWLDEINRHVP 94
HNHc smart00507
HNH nucleases;
1058-1086 2.01e-04

HNH nucleases;


Pssm-ID: 214702 [Multi-domain]  Cd Length: 52  Bit Score: 40.13  E-value: 2.01e-04
                            10        20
                    ....*....|....*....|....*....
gi 568908697   1058 WQVDHIRPvYEGGGQCSLDNLQTLCTVCH 1086
Cdd:smart00507   24 LEVDHIIP-LSDGGNDDLDNLVLLCPKCH 51
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
61-193 3.80e-04

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: 42.01  E-value: 3.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   61 VADEMGLGKTIQA--IAIAYFYKEEWPLLIVVP-SSLRYPWIEELEKWIPELEPEEINVVMN--KTDIG-RIPGSRVTVL 134
Cdd:cd00046     6 ITAPTGSGKTLAAllAALLLLLKKGKKVLVLVPtKALALQTAERLRELFGPGIRVAVLVGGSsaEEREKnKLGDADIIIA 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568908697  135 GYGLLTTDAETLlDALNTQNFRVVIVDESHYMKSRTAARSKILLPMVQKAR---RAILLTGT 193
Cdd:cd00046    86 TPDMLLNLLLRE-DRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLknaQVILLSAT 146
DEXHc_viral_Ns3 cd17931
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
66-195 7.33e-04

DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 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: 350689 [Multi-domain]  Cd Length: 151  Bit Score: 41.38  E-value: 7.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697   66 GLGKTIQAIA--IAYFYKEEWPLLIVVPSSLRypwIEELEKWIPELEPEEINVVMNKTDIGRIPgsrVTVLGYGLLTtda 143
Cdd:cd17931    11 GAGKTTRVLPqiIREAIKKRLRTLVLAPTRVV---AAEMYEALRGLPIRYRTGAVKEEHGGNEI---VDYMCHGTFT--- 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568908697  144 ETLLDALNTQNFRVVIVDESHYMKSRT-AARSKILLPMVQKARRAILLTGTPA 195
Cdd:cd17931    82 CRLLSPKRVPNYNLIIMDEAHFTDPASiAARGYIHTRVEMGEAAVIFMTATPP 134
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
625-647 1.04e-03

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 37.30  E-value: 1.04e-03
                            10        20
                    ....*....|....*....|...
gi 568908697    625 WQCGFCTFLNNPGLPYCEMCENP 647
Cdd:smart00547    3 WECPACTFLNFASRSKCFACGAP 25
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
323-440 5.57e-03

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 40.67  E-value: 5.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908697  323 AIAKAGAVKDYIKMLLQNDSLKFLVFAHHLSMLQACTEAVIESKSRYIRIDGSVPSSERIHLVNQFqKDPDTRVAIlSIQ 402
Cdd:PRK01297  316 AVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGF-REGKIRVLV-ATD 393
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568908697  403 AAGQGLTFTAASHVVFAELYWDPghikqaEDRAHRIGQ 440
Cdd:PRK01297  394 VAGRGIHIDGISHVINFTLPEDP------DDYVHRIGR 425
 
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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