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Conserved domains on  [gi|281363531|ref|NP_725650|]
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Mov10 RISC complex RNA helicase, isoform D [Drosophila melanogaster]

Protein Classification

Helz-like helicase( domain architecture ID 13030264)

Helz (helicase with zinc finger)-like helicase; similar to Homo sapiens helicase MOV-10

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
251-499 1.48e-99

DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All 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: 350796 [Multi-domain]  Cd Length: 229  Bit Score: 306.85  E-value: 1.48e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 251 NAEQLEAVQRIVAGPSTQGPYILFGPPGTGKTTTIVEAILQLRLQQPQSRILVTAGSNSACDTIALKLCEYIesnirlqe 330
Cdd:cd18038    3 NDEQKLAVRNIVTGTSRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLLAERLLNAL-------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 331 hfaqqklpEPDHQLIRVYSRSIYekgFASVPSLLLKNSNCSK-SIYDHIKASRIVKYGIIVATLCTVARLVTDTLgRYNF 409
Cdd:cd18038   75 --------VTKREILRLNAPSRD---RASVPPELLPYCNSKAeGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGV-PNGH 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 410 FTHIFIDEAGASTEPEALIGIMGIkQTADCHVILSGDHKQLGAVIKSNRAASLGLSRSLMERLLQSDCYKSDenGNYDRN 489
Cdd:cd18038  143 FTHIFIDEAGQATEPEALIPLSEL-ASKNTQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMERPLYYKD--GEYNPS 219
                        250
                 ....*....|
gi 281363531 490 RQMRLCRNYR 499
Cdd:cd18038  220 YITKLLKNYR 229
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
388-684 1.02e-55

Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];


:

Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 205.36  E-value: 1.02e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 388 IIVATLCTVARLVTDtlgRYNFFTHIFIDEAGASTEPEALIGIMGIKQtadchVILSGDHKQLGAVIKSNRAASL---GL 464
Cdd:COG1112  537 VVGMTPASVARLLPL---GEGSFDLVIIDEASQATLAEALGALARAKR-----VVLVGDPKQLPPVVFGEEAEEVaeeGL 608
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 465 SRSLMERLLQSDcyksdengnydRNRQMRLCRNYRSHPQIVRLFNELYYNGELKAQAPAMDVNLAanwsvltNPQFPIIF 544
Cdd:COG1112  609 DESLLDRLLARL-----------PERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRLA-------DPDSPLVF 670
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 545 QATHGVtnREQNSTSSYNNLEAEVICWYVKRLINDRVvGQEDVGIVAPYTAQGKLVTKLLQS---KGYPNVEVGSVETYQ 621
Cdd:COG1112  671 IDVDGV--YERRGGSRTNPEEAEAVVELVRELLEDGP-DGESIGVITPYRAQVALIRELLREalgDGLEPVFVGTVDRFQ 747
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281363531 622 GREKTIIIASLVKSFT-----NMGFMC-NPRRVNVLLSRAKALLILVGNPVTLRHH---SDFKFVINECKKH 684
Cdd:COG1112  748 GDERDVIIFSLVYSNDedvprNFGFLNgGPRRLNVAVSRARRKLIVVGSRELLDSDpstPALKRLLEYLERA 819
 
Name Accession Description Interval E-value
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
251-499 1.48e-99

DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All 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: 350796 [Multi-domain]  Cd Length: 229  Bit Score: 306.85  E-value: 1.48e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 251 NAEQLEAVQRIVAGPSTQGPYILFGPPGTGKTTTIVEAILQLRLQQPQSRILVTAGSNSACDTIALKLCEYIesnirlqe 330
Cdd:cd18038    3 NDEQKLAVRNIVTGTSRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLLAERLLNAL-------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 331 hfaqqklpEPDHQLIRVYSRSIYekgFASVPSLLLKNSNCSK-SIYDHIKASRIVKYGIIVATLCTVARLVTDTLgRYNF 409
Cdd:cd18038   75 --------VTKREILRLNAPSRD---RASVPPELLPYCNSKAeGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGV-PNGH 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 410 FTHIFIDEAGASTEPEALIGIMGIkQTADCHVILSGDHKQLGAVIKSNRAASLGLSRSLMERLLQSDCYKSDenGNYDRN 489
Cdd:cd18038  143 FTHIFIDEAGQATEPEALIPLSEL-ASKNTQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMERPLYYKD--GEYNPS 219
                        250
                 ....*....|
gi 281363531 490 RQMRLCRNYR 499
Cdd:cd18038  220 YITKLLKNYR 229
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
388-684 1.02e-55

Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 205.36  E-value: 1.02e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 388 IIVATLCTVARLVTDtlgRYNFFTHIFIDEAGASTEPEALIGIMGIKQtadchVILSGDHKQLGAVIKSNRAASL---GL 464
Cdd:COG1112  537 VVGMTPASVARLLPL---GEGSFDLVIIDEASQATLAEALGALARAKR-----VVLVGDPKQLPPVVFGEEAEEVaeeGL 608
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 465 SRSLMERLLQSDcyksdengnydRNRQMRLCRNYRSHPQIVRLFNELYYNGELKAQAPAMDVNLAanwsvltNPQFPIIF 544
Cdd:COG1112  609 DESLLDRLLARL-----------PERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRLA-------DPDSPLVF 670
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 545 QATHGVtnREQNSTSSYNNLEAEVICWYVKRLINDRVvGQEDVGIVAPYTAQGKLVTKLLQS---KGYPNVEVGSVETYQ 621
Cdd:COG1112  671 IDVDGV--YERRGGSRTNPEEAEAVVELVRELLEDGP-DGESIGVITPYRAQVALIRELLREalgDGLEPVFVGTVDRFQ 747
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281363531 622 GREKTIIIASLVKSFT-----NMGFMC-NPRRVNVLLSRAKALLILVGNPVTLRHH---SDFKFVINECKKH 684
Cdd:COG1112  748 GDERDVIIFSLVYSNDedvprNFGFLNgGPRRLNVAVSRARRKLIVVGSRELLDSDpstPALKRLLEYLERA 819
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
251-687 1.80e-55

DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273041 [Multi-domain]  Cd Length: 636  Bit Score: 201.58  E-value: 1.80e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  251 NAEQLEAVQRIVagpSTQGPYILFGPPGTGKTTTIVEAILQLRLQQPqsRILVTAGSNSACDTIALKL------CEYIES 324
Cdd:TIGR00376 159 NESQKEAVLFAL---SSKDLFLIHGPPGTGKTRTVVELIRQLVKRGL--RVLVTAPSNIAVDNLLERLalcdqkIVRLGH 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  325 NIRLQEHFAQQKLP-----EPDHQLIRVYSRSIYE-------------------------------KGFASVPSLLLKN- 367
Cdd:TIGR00376 234 PARLLKSNKQHSLDylienHPKYQIVADIREKIDElieernkktkpspqkrrglsdikilrkalkkREARGIESLKIASm 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  368 ---SNCSKSIYDHIK-----ASRIVKYGIIVATLCTVARLVTDTLGRYnfFTHIFIDEAGASTEPEALIGIMGIKQtadc 439
Cdd:TIGR00376 314 aewIETNKSIDRLLKllpesEERIMNEILAESDATNSMAGSEILNGQY--FDVAVIDEASQAMEPSCLIPLLKARK---- 387
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  440 hVILSGDHKQLGAVIKSNRAAslGLSRSLMERLLQSdcyksdengnYDRNRQMRLCRnYRSHPQIVRLFNELYYNGELKA 519
Cdd:TIGR00376 388 -LILAGDHKQLPPTILSHDAE--ELSLTLFERLIKE----------YPERSRTLNVQ-YRMNQKIMEFPSREFYNGKLTA 453
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  520 QAPAMDVNL------AANWSV--LTNPQfPIIFQATHGV---TNREQNSTSSYNNLEAEVICWYVKRLInDRVVGQEDVG 588
Cdd:TIGR00376 454 HESVANILLrdlpkvEATESEddLETGI-PLLFIDTSGCelfELKEADSTSKYNPGEAELVSEIIQALV-KMGVPANDIG 531
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  589 IVAPYTAQGKLVTKLLQSKgYPNVEVGSVETYQGREKTIIIASLVKSFTN--MGFMCNPRRVNVLLSRAKALLILVGNPV 666
Cdd:TIGR00376 532 VITPYDAQVDLLRQLLEHR-HIDIEVSSVDGFQGREKEVIIISFVRSNRKgeVGFLKDLRRLNVALTRARRKLIVIGDSR 610
                         490       500
                  ....*....|....*....|.
gi 281363531  667 TLRHHSDFKFVINECKKHGTY 687
Cdd:TIGR00376 611 TLSNHKFYKRLIEWCKQHGEV 631
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
500-682 2.14e-52

C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain]  Cd Length: 184  Bit Score: 180.12  E-value: 2.14e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 500 SHPQIVRLFNELYYNGELKAQApamDVNLAANWSVLTNPQFPIIFQATHGVTNREQNSTSSYNNLEAEVICWYVKRLIND 579
Cdd:cd18808    1 MHPEISEFPSKLFYEGKLKAGV---SVAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 580 RVvGQEDVGIVAPYTAQGKLVTKLLQSKG--YPNVEVGSVETYQGREKTIIIASLVKS---FTNMGFMCNPRRVNVLLSR 654
Cdd:cd18808   78 GV-KPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSnesGGSIGFLSDPRRLNVALTR 156
                        170       180
                 ....*....|....*....|....*...
gi 281363531 655 AKALLILVGNPVTLRHHSDFKFVINECK 682
Cdd:cd18808  157 AKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
464-665 3.67e-46

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 463780 [Multi-domain]  Cd Length: 196  Bit Score: 163.10  E-value: 3.67e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  464 LSRSLMERLLQsdcyksdengNYDRNRQMrLCRNYRSHPQIVRLFNELYYNGELKAQAPAMDVNLAANWSVLtNPQFPII 543
Cdd:pfam13087   1 LDRSLFERLQE----------LGPSAVVM-LDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDDFHLP-DPLGPLV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  544 FQATHGVTNREQNSTSSYNNL-EAEVICWYVKRLINDRVVGQEDVGIVAPYTAQGKLVTKLLQSK--GYPNVEVGSVETY 620
Cdd:pfam13087  69 FIDVDGSEEEESDGGTSYSNEaEAELVVQLVEKLIKSGPEEPSDIGVITPYRAQVRLIRKLLKRKlgGKLEIEVNTVDGF 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 281363531  621 QGREKTIIIASLVKSFT--NMGFMCNPRRVNVLLSRAKALLILVGNP 665
Cdd:pfam13087 149 QGREKDVIIFSCVRSNEkgGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
254-456 1.99e-21

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 404072 [Multi-domain]  Cd Length: 248  Bit Score: 94.33  E-value: 1.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  254 QLEAVQRIVAGPSTQgpyILFGPPGTGKTTTIVEAILQLRLQQ-----PQSRILVTAGSNSACDTIALKLCE-------- 320
Cdd:pfam13086   2 QREAIRSALSSSHFT---LIQGPPGTGKTTTIVELIRQLLSYPatsaaAGPRILVCAPSNAAVDNILERLLRkgqkygpk 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  321 -------------------------YIESNIRLQEHFAQQKLPEPDHQLIRVY-SRSIYEKGFASV----PSLLLKNSNC 370
Cdd:pfam13086  79 ivrighpaaiseavlpvsldylvesKLNNEEDAQIVKDISKELEKLAKALRAFeKEIIVEKLLKSRnkdkSKLEQERRKL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  371 SKSIYDHIKASRIVKYG----------IIVATLCTVARlvtDTLGRYNFFTHIFIDEAGASTEPEALIGIM-GIKqtadc 439
Cdd:pfam13086 159 RSERKELRKELRRREQSlereildeaqIVCSTLSGAGS---RLLSSLANFDVVIIDEAAQALEPSTLIPLLrGPK----- 230
                         250
                  ....*....|....*..
gi 281363531  440 HVILSGDHKQLGAVIKS 456
Cdd:pfam13086 231 KVVLVGDPKQLPPTVIS 247
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
251-453 6.99e-06

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 49.20  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 251 NAEQLEAVQRIVagpSTQGPYILFGPPGTGKTTTIVeAILQLrLQQPQSRILVTAGSNSAcdtiALKLCEYIE---SNIr 327
Cdd:COG0507  126 SDEQREAVALAL---TTRRVSVLTGGAGTGKTTTLR-ALLAA-LEALGLRVALAAPTGKA----AKRLSESTGieaRTI- 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 328 lqehfaqqklpepdHQLIRVYSRSiyekgfasvpslllknsncskSIYDHIKASRIVKYGIIVatlctvarlvtdtlgry 407
Cdd:COG0507  196 --------------HRLLGLRPDS---------------------GRFRHNRDNPLTPADLLV----------------- 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 281363531 408 nffthifIDEAG-ASTEP-EALIGIMgikQTADCHVILSGDHKQLGAV 453
Cdd:COG0507  224 -------VDEASmVDTRLmAALLEAL---PRAGARLILVGDPDQLPSV 261
DEXDc smart00487
DEAD-like helicases superfamily;
254-418 8.63e-06

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 47.10  E-value: 8.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531   254 QLEAVQRIVAGPSTQgpyILFGPPGTGKTTTIVEAILQLRLQQPQSRILVTagsnsaCDTIALKlceyiesnIRLQEHFa 333
Cdd:smart00487  13 QKEAIEALLSGLRDV---ILAAPTGSGKTLAALLPALEALKRGKGGRVLVL------VPTRELA--------EQWAEEL- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531   334 QQKLPEPDHQLIRVYSrsiyekgfasvpslllknsncSKSIYDHIKASRIVKYGIIVATLCTVARLVTDTLGRYNFFTHI 413
Cdd:smart00487  75 KKLGPSLGLKVVGLYG---------------------GDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLV 133

                   ....*
gi 281363531   414 FIDEA 418
Cdd:smart00487 134 ILDEA 138
 
Name Accession Description Interval E-value
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
251-499 1.48e-99

DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and similar proteins. Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. All 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: 350796 [Multi-domain]  Cd Length: 229  Bit Score: 306.85  E-value: 1.48e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 251 NAEQLEAVQRIVAGPSTQGPYILFGPPGTGKTTTIVEAILQLRLQQPQSRILVTAGSNSACDTIALKLCEYIesnirlqe 330
Cdd:cd18038    3 NDEQKLAVRNIVTGTSRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLLAERLLNAL-------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 331 hfaqqklpEPDHQLIRVYSRSIYekgFASVPSLLLKNSNCSK-SIYDHIKASRIVKYGIIVATLCTVARLVTDTLgRYNF 409
Cdd:cd18038   75 --------VTKREILRLNAPSRD---RASVPPELLPYCNSKAeGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGV-PNGH 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 410 FTHIFIDEAGASTEPEALIGIMGIkQTADCHVILSGDHKQLGAVIKSNRAASLGLSRSLMERLLQSDCYKSDenGNYDRN 489
Cdd:cd18038  143 FTHIFIDEAGQATEPEALIPLSEL-ASKNTQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMERPLYYKD--GEYNPS 219
                        250
                 ....*....|
gi 281363531 490 RQMRLCRNYR 499
Cdd:cd18038  220 YITKLLKNYR 229
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
388-684 1.02e-55

Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 205.36  E-value: 1.02e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 388 IIVATLCTVARLVTDtlgRYNFFTHIFIDEAGASTEPEALIGIMGIKQtadchVILSGDHKQLGAVIKSNRAASL---GL 464
Cdd:COG1112  537 VVGMTPASVARLLPL---GEGSFDLVIIDEASQATLAEALGALARAKR-----VVLVGDPKQLPPVVFGEEAEEVaeeGL 608
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 465 SRSLMERLLQSDcyksdengnydRNRQMRLCRNYRSHPQIVRLFNELYYNGELKAQAPAMDVNLAanwsvltNPQFPIIF 544
Cdd:COG1112  609 DESLLDRLLARL-----------PERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRLA-------DPDSPLVF 670
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 545 QATHGVtnREQNSTSSYNNLEAEVICWYVKRLINDRVvGQEDVGIVAPYTAQGKLVTKLLQS---KGYPNVEVGSVETYQ 621
Cdd:COG1112  671 IDVDGV--YERRGGSRTNPEEAEAVVELVRELLEDGP-DGESIGVITPYRAQVALIRELLREalgDGLEPVFVGTVDRFQ 747
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281363531 622 GREKTIIIASLVKSFT-----NMGFMC-NPRRVNVLLSRAKALLILVGNPVTLRHH---SDFKFVINECKKH 684
Cdd:COG1112  748 GDERDVIIFSLVYSNDedvprNFGFLNgGPRRLNVAVSRARRKLIVVGSRELLDSDpstPALKRLLEYLERA 819
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
251-687 1.80e-55

DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of this family have been characterized as binding certain single-stranded G-rich DNA sequences (GGGGT and GGGCT). A number of related proteins are characterized as helicases. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273041 [Multi-domain]  Cd Length: 636  Bit Score: 201.58  E-value: 1.80e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  251 NAEQLEAVQRIVagpSTQGPYILFGPPGTGKTTTIVEAILQLRLQQPqsRILVTAGSNSACDTIALKL------CEYIES 324
Cdd:TIGR00376 159 NESQKEAVLFAL---SSKDLFLIHGPPGTGKTRTVVELIRQLVKRGL--RVLVTAPSNIAVDNLLERLalcdqkIVRLGH 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  325 NIRLQEHFAQQKLP-----EPDHQLIRVYSRSIYE-------------------------------KGFASVPSLLLKN- 367
Cdd:TIGR00376 234 PARLLKSNKQHSLDylienHPKYQIVADIREKIDElieernkktkpspqkrrglsdikilrkalkkREARGIESLKIASm 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  368 ---SNCSKSIYDHIK-----ASRIVKYGIIVATLCTVARLVTDTLGRYnfFTHIFIDEAGASTEPEALIGIMGIKQtadc 439
Cdd:TIGR00376 314 aewIETNKSIDRLLKllpesEERIMNEILAESDATNSMAGSEILNGQY--FDVAVIDEASQAMEPSCLIPLLKARK---- 387
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  440 hVILSGDHKQLGAVIKSNRAAslGLSRSLMERLLQSdcyksdengnYDRNRQMRLCRnYRSHPQIVRLFNELYYNGELKA 519
Cdd:TIGR00376 388 -LILAGDHKQLPPTILSHDAE--ELSLTLFERLIKE----------YPERSRTLNVQ-YRMNQKIMEFPSREFYNGKLTA 453
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  520 QAPAMDVNL------AANWSV--LTNPQfPIIFQATHGV---TNREQNSTSSYNNLEAEVICWYVKRLInDRVVGQEDVG 588
Cdd:TIGR00376 454 HESVANILLrdlpkvEATESEddLETGI-PLLFIDTSGCelfELKEADSTSKYNPGEAELVSEIIQALV-KMGVPANDIG 531
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  589 IVAPYTAQGKLVTKLLQSKgYPNVEVGSVETYQGREKTIIIASLVKSFTN--MGFMCNPRRVNVLLSRAKALLILVGNPV 666
Cdd:TIGR00376 532 VITPYDAQVDLLRQLLEHR-HIDIEVSSVDGFQGREKEVIIISFVRSNRKgeVGFLKDLRRLNVALTRARRKLIVIGDSR 610
                         490       500
                  ....*....|....*....|.
gi 281363531  667 TLRHHSDFKFVINECKKHGTY 687
Cdd:TIGR00376 611 TLSNHKFYKRLIEWCKQHGEV 631
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
251-499 2.26e-53

DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds Piwi-interacting RNA (piRNA) precursors to initiate piRNA processing. Mov10L1 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: 350836 [Multi-domain]  Cd Length: 230  Bit Score: 184.49  E-value: 2.26e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 251 NAEQLEAVQRIVAGPSTQGPYILFGPPGTGKTTTIVEAILQLRLQQPQSRILVTAGSNSACDTIALKLceyIESNIRLQe 330
Cdd:cd18078    3 NELQKEAVKRILGGECRPLPYILFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSRL---HESKVLKP- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 331 hfaqqklpepdHQLIRVYSRSIYEKgfASVPSLLLknsncskSIYDHIKASRIVKYGIIVATlCTVARLVTdTLG-RYNF 409
Cdd:cd18078   79 -----------GDMVRLNAVNRFES--TVIDARKL-------YCRLGEDLSKASRHRIVIST-CSTAGLLY-QMGlPVGH 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 410 FTHIFIDEAGASTEPEALIGImGIKQTADCHVILSGDHKQLGAVIKSNRAASLGLSRSLMERLLQSDCYKSDEN-----G 484
Cdd:cd18078  137 FTHVFVDEAGQATEPESLIPL-GLISSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNRPLYLRDPNrfgesG 215
                        250
                 ....*....|....*
gi 281363531 485 NYDRNRQMRLCRNYR 499
Cdd:cd18078  216 GYNPLLVTKLVDNYR 230
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
500-682 2.14e-52

C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), and similar proteins. They are DEAD-like helicases belonging to superfamily (SF)1, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF2 helicases, SF1 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: 350195 [Multi-domain]  Cd Length: 184  Bit Score: 180.12  E-value: 2.14e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 500 SHPQIVRLFNELYYNGELKAQApamDVNLAANWSVLTNPQFPIIFQATHGVTNREQNSTSSYNNLEAEVICWYVKRLIND 579
Cdd:cd18808    1 MHPEISEFPSKLFYEGKLKAGV---SVAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 580 RVvGQEDVGIVAPYTAQGKLVTKLLQSKG--YPNVEVGSVETYQGREKTIIIASLVKS---FTNMGFMCNPRRVNVLLSR 654
Cdd:cd18808   78 GV-KPSSIGVITPYRAQVALIRELLRKRGglLEDVEVGTVDNFQGREKDVIILSLVRSnesGGSIGFLSDPRRLNVALTR 156
                        170       180
                 ....*....|....*....|....*...
gi 281363531 655 AKALLILVGNPVTLRHHSDFKFVINECK 682
Cdd:cd18808  157 AKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
464-665 3.67e-46

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 463780 [Multi-domain]  Cd Length: 196  Bit Score: 163.10  E-value: 3.67e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  464 LSRSLMERLLQsdcyksdengNYDRNRQMrLCRNYRSHPQIVRLFNELYYNGELKAQAPAMDVNLAANWSVLtNPQFPII 543
Cdd:pfam13087   1 LDRSLFERLQE----------LGPSAVVM-LDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDDFHLP-DPLGPLV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  544 FQATHGVTNREQNSTSSYNNL-EAEVICWYVKRLINDRVVGQEDVGIVAPYTAQGKLVTKLLQSK--GYPNVEVGSVETY 620
Cdd:pfam13087  69 FIDVDGSEEEESDGGTSYSNEaEAELVVQLVEKLIKSGPEEPSDIGVITPYRAQVRLIRKLLKRKlgGKLEIEVNTVDGF 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 281363531  621 QGREKTIIIASLVKSFT--NMGFMCNPRRVNVLLSRAKALLILVGNP 665
Cdd:pfam13087 149 QGREKDVIIFSCVRSNEkgGIGFLSDPRRLNVALTRAKRGLIIVGNA 195
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
251-499 9.99e-32

DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of Nonsense Transcripts, or ATP-Dependent Helicase RENT1) is an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. It is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. It is recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) located downstream from the termination codon through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Diseases associated with UPF1 include juvenile amyotrophic lateral sclerosis and epidermolysis bullosa, junctional, non-Herlitz type. UPF1 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: 350797 [Multi-domain]  Cd Length: 234  Bit Score: 123.51  E-value: 9.99e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 251 NAEQLEAVQRIVAGPSTqgpyILFGPPGTGKTTTIVEAILQLRlQQPQSRILVTAGSNSACDTIALK----------LC- 319
Cdd:cd18039    3 NHSQVDAVKTALQRPLS----LIQGPPGTGKTVTSATIVYHLV-KQGNGPVLVCAPSNVAVDQLTEKihqtglkvvrLCa 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 320 ---EYIESNIrlqEHFAQqklpepdHQLIRVYsrsiyEKGFASVPSLLLKNSNCSKSIYD--HIKASR-------IVKYG 387
Cdd:cd18039   78 ksrEAVESPV---SFLAL-------HNQVRNL-----DSAEKLELLKLLKLETGELSSADekRYRKLKrkaerelLRNAD 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 388 IIVATLCTVArlvtDT-LGRYNFfTHIFIDEAGASTEPEALIGIM-GIKQtadchVILSGDHKQLGAVIKSNRAASLGLS 465
Cdd:cd18039  143 VICCTCVGAG----DPrLSKMKF-RTVLIDEATQATEPECLIPLVhGAKQ-----VILVGDHCQLGPVVMCKKAAKAGLS 212
                        250       260       270
                 ....*....|....*....|....*....|....
gi 281363531 466 RSLMERLLQSDcyksdengnydrNRQMRLCRNYR 499
Cdd:cd18039  213 QSLFERLVQLG------------IRPIRLQVQYR 234
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
251-475 1.70e-28

DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 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: 350802 [Multi-domain]  Cd Length: 191  Bit Score: 113.09  E-value: 1.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 251 NAEQLEAVQRIVAGPSTQgpyILFGPPGTGKTTTIVEAILQLrlQQPQSRILVTAGSNSACDTIalklCEyiesniRLQE 330
Cdd:cd18044    3 NDSQKEAVKFALSQKDVA---LIHGPPGTGKTTTVVEIILQA--VKRGEKVLACAPSNIAVDNL----VE------RLVA 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 331 HfaqqKLPepdhqLIRVysrsiyekGFasvPSLLLKnSNCSKSiYDHIKASRIvkygiIVATLCTVArlvTDTLGRYNFF 410
Cdd:cd18044   68 L----KVK-----VVRI--------GH---PARLLE-SVLDHS-LDALVAAQV-----VLATNTGAG---SRQLLPNELF 117
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281363531 411 THIFIDEAGASTEPEALIGIMGIKQtadchVILSGDHKQLGAVIKSNRAASLGLSRSLMERLLQS 475
Cdd:cd18044  118 DVVVIDEAAQALEASCWIPLLKARR-----CILAGDHKQLPPTILSDKAARGGLGVTLFERLVNL 177
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
251-499 3.50e-24

DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. HELZ is a member of the family I class of RNA helicases 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: 350835 [Multi-domain]  Cd Length: 226  Bit Score: 101.79  E-value: 3.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 251 NAEQLEAVQRIVAGPSTQGPYILF-GPPGTGKTTTIVEAILQLrLQQPQSRILVTAGSNSACDT-IALKLCEYIESNirl 328
Cdd:cd18077    3 NAKQKEAVLAITTPLSIQLPPVLLiGPFGTGKTFTLAQAVKHI-LQQPETRILICTHSNSAADLyIKEYLHPYVETG--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 329 qehfaqqklpEPDHQLIRVYSRSIYEKGF-ASVPSLLLKNSNcskSIYDHIKASRIVKYGIIVATLCTVARLVTDTLGRy 407
Cdd:cd18077   79 ----------NPRARPLRVYYRNRWVKTVhPVVQKYCLIDEH---GTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEP- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 408 NFFTHIFIDEAGASTEPEALIGIMgiKQTADCHVILSGDHKQLGAVIKSNRAASLGLSRSLMERLLQsdcyksdengNYD 487
Cdd:cd18077  145 GFFTHILLDEAAQAMECEAIMPLA--LATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYE----------HYP 212
                        250
                 ....*....|....
gi 281363531 488 RNRQMR--LCRNYR 499
Cdd:cd18077  213 SEHPCRilLCENYR 226
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
251-472 1.07e-22

DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in transcription, neurogenesis, and antiviral response. SEXT is an R-loop-associated protein that is thought to function as an RNA/DNA helicase. R-loops consist of RNA/DNA hybrids, formed during transcription when nascent RNA hybridizes to the DNA template strand, displacing the non-template DNA strand. Mutations in SETX are linked to two neurodegenerative disorders: ataxia with oculomotor apraxia type 2 (AOA2) and amyotrophic lateral sclerosis type 4 (ALS4). S. cerevisiae homolog splicing endonuclease 1 (Sen1) is an exclusively nuclear protein, important for nucleolar organization. S. cerevisiae Sen1 and its ortholog, the Schizosaccharomyces pombe Sen1, share conserved domains and belong to the family I class of helicases. Both proteins translocate 5' to 3' and unwind both DNA and RNA duplexes and also RNA/DNA hybrids in vitro. SETX 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: 438712 [Multi-domain]  Cd Length: 218  Bit Score: 96.90  E-value: 1.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 251 NAEQLEAVQRIVagpSTQGPYILF-GPPGTGKTTTIVEAILQLRLQQPQS-----------------------RILVTAG 306
Cdd:cd18042    2 NESQLEAIASAL---QNSPGITLIqGPPGTGKTKTIVGILSVLLAGKYRKyyekvkkklrklqrnlnnkkkknRILVCAP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 307 SNSACDTIALKLceyiesnirLQEHFAQQKLPEPDHQLIRVYSRSIYEKgfasvpslLLKNSNcsksiydhikasrivky 386
Cdd:cd18042   79 SNAAVDEIVLRL---------LSEGFLDGDGRSYKPNVVRVGRQELRAS--------ILNEAD----------------- 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 387 gIIVATLCTVARLVTDTLGRynFFTHIFIDEAGASTEPEALIGI-MGIKqtadcHVILSGDHKQLGAVIKSNRAASLGLS 465
Cdd:cd18042  125 -IVCTTLSSSGSDLLESLPR--GFDTVIIDEAAQAVELSTLIPLrLGCK-----RLILVGDPKQLPATVFSKVAQKLGYD 196

                 ....*..
gi 281363531 466 RSLMERL 472
Cdd:cd18042  197 RSLFERL 203
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
254-456 1.99e-21

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.


Pssm-ID: 404072 [Multi-domain]  Cd Length: 248  Bit Score: 94.33  E-value: 1.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  254 QLEAVQRIVAGPSTQgpyILFGPPGTGKTTTIVEAILQLRLQQ-----PQSRILVTAGSNSACDTIALKLCE-------- 320
Cdd:pfam13086   2 QREAIRSALSSSHFT---LIQGPPGTGKTTTIVELIRQLLSYPatsaaAGPRILVCAPSNAAVDNILERLLRkgqkygpk 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  321 -------------------------YIESNIRLQEHFAQQKLPEPDHQLIRVY-SRSIYEKGFASV----PSLLLKNSNC 370
Cdd:pfam13086  79 ivrighpaaiseavlpvsldylvesKLNNEEDAQIVKDISKELEKLAKALRAFeKEIIVEKLLKSRnkdkSKLEQERRKL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  371 SKSIYDHIKASRIVKYG----------IIVATLCTVARlvtDTLGRYNFFTHIFIDEAGASTEPEALIGIM-GIKqtadc 439
Cdd:pfam13086 159 RSERKELRKELRRREQSlereildeaqIVCSTLSGAGS---RLLSSLANFDVVIIDEAAQALEPSTLIPLLrGPK----- 230
                         250
                  ....*....|....*..
gi 281363531  440 HVILSGDHKQLGAVIKS 456
Cdd:pfam13086 231 KVVLVGDPKQLPPTVIS 247
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
251-475 2.48e-21

DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5-3 helicase, and endonuclease activities, and is involved in DNA replication and DNA repair in the nucleus and mitochondrion. It is involved in Okazaki fragment processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. It is also involved in 5-end resection of DNA during double-strand break (DSB) repair; it is recruited by BLM and mediates the cleavage of 5-ssDNA, while the 3-ssDNA cleavage is prevented by the presence of RPA. DNA2 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: 350799 [Multi-domain]  Cd Length: 203  Bit Score: 92.68  E-value: 2.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 251 NAEQLEAVQRIVAGPStqgpY-ILFGPPGTGKTTTIVEAILQLRLQQpqSRILVTAGSNSACDTIALKLCEYIESNIRLQ 329
Cdd:cd18041    3 NKDQRQAIKKVLNAKD----YaLILGMPGTGKTTTIAALVRILVALG--KSVLLTSYTHSAVDNILLKLKKFGVNFLRLG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 330 EhfaqqklPEPDHQLIRVYSRSIYEKGFASVPSLllknsncsKSIYDHIKasrivkygiIVATLCTVarlVTDTLGRYNF 409
Cdd:cd18041   77 R-------LKKIHPDVQEFTLEAILKSCKSVEEL--------ESKYESVS---------VVATTCLG---INHPIFRRRT 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281363531 410 FTHIFIDEAGASTEPEALIGI-MGIKqtadchVILSGDHKQLGAVIKSNRAASLGLSRSLMERLLQS 475
Cdd:cd18041  130 FDYCIVDEASQITLPICLGPLrLAKK------FVLVGDHYQLPPLVKSREARELGMDESLFKRLSEA 190
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
272-499 1.75e-16

DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, HELZ, Mov10L1, Aquarius, IGHMBP2 (SMUBP2), coronavirus Nsp13, and similar proteins. They belong 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: 438708 [Multi-domain]  Cd Length: 121  Bit Score: 76.12  E-value: 1.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 272 ILFGPPGTGKTTTIVEAILQLRLQQPQSRILVTAGSNSACDTIalklceyiesnirlqehfaqqklpepdhqlirvysrs 351
Cdd:cd17934    3 LIQGPPGTGKTTTIAAIVLQLLKGLRGKRVLVTAQSNVAVDNV------------------------------------- 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 352 iyekgfasvpslllknsncsksiydhikasrivkygiivatlctvarlvtDTLgrynffthiFIDEAGASTEPEALIGIM 431
Cdd:cd17934   46 --------------------------------------------------DVV---------IIDEASQITEPELLIALI 66
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281363531 432 GIKQtadchVILSGDHKQLGAVIKSNRAASLGLSRSLMERLLqsdCYKSDENGnydrnRQMRLCRNYR 499
Cdd:cd17934   67 RAKK-----VVLVGDPKQLPPVVQEDHAALLGLSFILSLLLL---FRLLLPGS-----PKVMLDTQYR 121
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
251-472 2.04e-15

C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB and RXRA. It 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: 350798 [Multi-domain]  Cd Length: 271  Bit Score: 77.18  E-value: 2.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 251 NAEQLEAVQRIVAGPSTqgpyILFGPPGTGKTTTIVEAILQL-----RLQQPQSR------ILVTAGSNSACDTIA---L 316
Cdd:cd18040    3 NPSQNHAVRTALTKPFT----LIQGPPGTGKTVTGVHIAYWFakqnrEIQSVSGEgdggpcVLYCGPSNKSVDVVAellL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 317 KLC---------EYIE--------SNIRLQEHFAQQKLPEPDHQLIRVYSR-----SIYEKGFASVPSLLLK-----NSN 369
Cdd:cd18040   79 KVPglkilrvysEQIEtteypipnEPRHPNKKSERESKPNSELSSITLHHRirqpsNPHSQQIKAFEARFERtqekiTEE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 370 CSKSIYDHIKASRIVKYGIIVATLCTVARLVTDTLGRYNFFTHIFIDEAGASTEPEALIGIMGIKQTAdcHVILSGDHKQ 449
Cdd:cd18040  159 DIKTYKILIWEARFEELETVDVILCTCSEAASQKMRTHANVKQCIVDECGMCTEPESLIPIVSAPRAE--QVVLIGDHKQ 236
                        250       260
                 ....*....|....*....|...
gi 281363531 450 LGAVIKSNRAASLGLSRSLMERL 472
Cdd:cd18040  237 LRPVVQNKEAQKLGLGRSLFERY 259
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
251-499 2.65e-15

N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known as PPAR-alpha-interacting complex protein 285 or PRIC285 and PPAR-gamma DBD-interacting protein 1 or PDIP1) acts as a transcriptional coactivator for a number of nuclear receptors including PPARA, PPARG, THRA, THRB, and RXRA. It 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: 350834 [Multi-domain]  Cd Length: 230  Bit Score: 76.08  E-value: 2.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 251 NAEQLEAVQRIVAGPSTQ---GPYILFGPPGTGKTTTIVEAILQLrLQQPQSRILVTAGSNSACDtialklceyiesnIR 327
Cdd:cd18076    3 NNKQQLAFNFIAGKPSEArfvPPLLIYGPFGTGKTFTLAMAALEV-IREPGTKVLICTHTNSAAD-------------IY 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 328 LQEHFAQQ-KLPEPDHQLIRVYSRsiyEKGFASVPSLLLKNSNCSKS--IYDHIKASRIVKYGIIVATlCTVARLVTDTL 404
Cdd:cd18076   69 IREYFHPYvDKGHPEARPLRIKAT---DRPNAITDPDTITYCCLTKDrqCFRLPTRDELDFHNIVITT-TAMAFNLHVLS 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 405 GrynFFTHIFIDEAGASTEPEALIGIMgiKQTADCHVILSGDHKQLG----AVIKSNRAaslglSRSLMERLLQsdCYKS 480
Cdd:cd18076  145 G---FFTHIFIDEAAQMLECEALIPLS--YAGPKTRVVLAGDHMQMTpklfSVADYNRA-----NHTLLNRLFH--YYQG 212
                        250       260
                 ....*....|....*....|.
gi 281363531 481 DEngnYDRNRQMRLC--RNYR 499
Cdd:cd18076  213 EK---HEVAVKSRVIfsENYR 230
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
245-512 3.82e-10

EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). 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: 350693 [Multi-domain]  Cd Length: 207  Bit Score: 60.13  E-value: 3.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 245 NSTIYSNAEQLEAvqrIVAGpSTQGPYILFGPPGTGKTTTIVEAILQLRLQQPQSRILVTAGSNSACDTIALKLceyies 324
Cdd:cd17935    1 QNTVKFTPTQIEA---IRSG-MQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALNQLFEKI------ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 325 nirlqehfaqqklpepdhqlirvYSRSIYEKGfasvpslLLKNSNCSKsiydhikasrivkygiIVATLCTVARLVTDTL 404
Cdd:cd17935   71 -----------------------MALDIDERH-------LLRLGHGAK----------------IIAMTCTHAALKRGEL 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 405 GRYNF-FTHIFIDEAGASTEPEALIgIMGIKQTADCH-----VILSGDHKQLGAVIKSNRAASLG-LSRSLMERLLqsdc 477
Cdd:cd17935  105 VELGFkYDNILMEEAAQILEIETFI-PLLLQNPEDGPnrlkrLIMIGDHHQLPPVIKNMAFQKYSnMEQSLFTRLV---- 179
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 281363531 478 yksdengnYDRNRQMRLCRNYRSHPQIVRLFNELY 512
Cdd:cd17935  180 --------RLGVPTVDLDAQGRARASISSLYNWRY 206
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
251-472 6.92e-09

EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that represses class II MHC (major histocompatibility complex) gene expression. NFX1 binds a conserved cis-acting element, termed the X-box, in promoters of human class II MHC genes. The Cys-rich region contains several NFX1-type zinc finger domains. Frequently, a R3H domain is present in the C-terminus, and a RING finger domain and a PAM2 motif are present in the N-terminus. The lack of R3H and PAM2 motifs in the plant proteins indicates functional differences. Plant NFX1-like proteins are proposed to modulate growth and survival by coordinating reactive oxygen species, salicylic acid, further biotic stress and abscisic acid responses. A common feature of all members may be E3 ubiquitin ligase, due to the presence of a RING finger domain, as well as DNA binding. NFX1 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: 350694 [Multi-domain]  Cd Length: 178  Bit Score: 56.01  E-value: 6.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 251 NAEQLEAVQRIVagpsTQGPYILFGPPGTGKTTT---IVEAILQLRLQQPQSRILVTAGSNSACDTIALKLCEYIESNIr 327
Cdd:cd17936    3 DPSQLEALKHAL----TSELALIQGPPGTGKTFLgvkLVRALLQNQDLSITGPILVVCYTNHALDQFLEGLLDFGPTKI- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 328 lqehfaqqklpepdhqlIRVYSRsiyekgfasvpslllknsncsksiydhikasrivkygIIVATLCTVARLvTDTLGRY 407
Cdd:cd17936   78 -----------------VRLGAR-------------------------------------VIGMTTTGAAKY-RELLQAL 102
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281363531 408 NfFTHIFIDEAGASTEPeALIGIMgikqTADC-HVILSGDHKQL--GAVIKSNRAASLGLSRSLMERL 472
Cdd:cd17936  103 G-PKVVIVEEAAEVLEA-HILAAL----TPSTeHLILIGDHKQLrpKVNVYELTAKKYNLDVSLFERL 164
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
397-473 6.56e-06

DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. Their helicase core is surrounded by C and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains or domains engaged in protein-protein interactions. SF1 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: 438706 [Multi-domain]  Cd Length: 121  Bit Score: 45.94  E-value: 6.56e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281363531 397 ARLVTDTLGRYNFFTHIFIDEAGASTEPEALIGIMGIKQTAdcHVILSGDHKQLGAVIKSNRAASLGLSRSLMERLL 473
Cdd:cd17914   34 ILLVTPTNKAAAQLDNILVDEAAQILEPETSRLIDLALDQG--RVILVGDHDQLGPVWRGAVLAKICNEQSLFTRLV 108
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
251-453 6.99e-06

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 49.20  E-value: 6.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 251 NAEQLEAVQRIVagpSTQGPYILFGPPGTGKTTTIVeAILQLrLQQPQSRILVTAGSNSAcdtiALKLCEYIE---SNIr 327
Cdd:COG0507  126 SDEQREAVALAL---TTRRVSVLTGGAGTGKTTTLR-ALLAA-LEALGLRVALAAPTGKA----AKRLSESTGieaRTI- 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 328 lqehfaqqklpepdHQLIRVYSRSiyekgfasvpslllknsncskSIYDHIKASRIVKYGIIVatlctvarlvtdtlgry 407
Cdd:COG0507  196 --------------HRLLGLRPDS---------------------GRFRHNRDNPLTPADLLV----------------- 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 281363531 408 nffthifIDEAG-ASTEP-EALIGIMgikQTADCHVILSGDHKQLGAV 453
Cdd:COG0507  224 -------VDEASmVDTRLmAALLEAL---PRAGARLILVGDPDQLPSV 261
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
253-305 8.10e-06

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD 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: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 46.39  E-value: 8.10e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 281363531 253 EQLEAVQRIVAGPSTqgpyILFGPPGTGKTTTiVEAILQLrLQQPQSRILVTA 305
Cdd:cd17933    1 EQKAAVRLVLRNRVS----VLTGGAGTGKTTT-LKALLAA-LEAEGKRVVLAA 47
DEXDc smart00487
DEAD-like helicases superfamily;
254-418 8.63e-06

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 47.10  E-value: 8.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531   254 QLEAVQRIVAGPSTQgpyILFGPPGTGKTTTIVEAILQLRLQQPQSRILVTagsnsaCDTIALKlceyiesnIRLQEHFa 333
Cdd:smart00487  13 QKEAIEALLSGLRDV---ILAAPTGSGKTLAALLPALEALKRGKGGRVLVL------VPTRELA--------EQWAEEL- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531   334 QQKLPEPDHQLIRVYSrsiyekgfasvpslllknsncSKSIYDHIKASRIVKYGIIVATLCTVARLVTDTLGRYNFFTHI 413
Cdd:smart00487  75 KKLGPSLGLKVVGLYG---------------------GDSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLV 133

                   ....*
gi 281363531   414 FIDEA 418
Cdd:smart00487 134 ILDEA 138
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
251-315 3.41e-05

DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along with the concomitant unwinding of DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination, and repair as well as many aspects of RNA metabolism. Superfamily 1 helicases 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: 350801 [Multi-domain]  Cd Length: 127  Bit Score: 44.11  E-value: 3.41e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281363531 251 NAEQLEAVQRIVAGPSTqgpyILFGPPGTGKTTTIVEAILQLRLQqpQSRILVTAGSNSACDTIA 315
Cdd:cd18043    1 DSSQEAAIISARNGKNV----VIQGPPGTGKSQTIANIIANALAR--GKRVLFVSEKKAALDVVR 59
DEXQc_UvrD cd17932
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ...
251-324 8.31e-05

DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD 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: 350690 [Multi-domain]  Cd Length: 189  Bit Score: 44.04  E-value: 8.31e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281363531 251 NAEQLEAVQrivagpSTQGPYILFGPPGTGKTTTIVEAILQL--RLQQPQSRILVTAGSNSACDTIALKLCEYIES 324
Cdd:cd17932    1 NPEQREAVT------HPDGPLLVLAGAGSGKTRVLTHRIAYLilEGGVPPERILAVTFTNKAAKEMRERLRKLLGE 70
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
251-453 9.93e-05

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.


Pssm-ID: 433343 [Multi-domain]  Cd Length: 191  Bit Score: 44.09  E-value: 9.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  251 NAEQLEAVQRIVAgpSTQGPYILFGPPGTGKTTT---IVEAILQLRLqqpqsRILVTAGSNSACDtialklceyiesniR 327
Cdd:pfam13604   3 NAEQAAAVRALLT--SGDRVAVLVGPAGTGKTTAlkaLREAWEAAGY-----RVIGLAPTGRAAK--------------V 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  328 LQEHFAqqklpepdhqlirvysrsiyekgfasvpslllknsncsksiydhIKASrivkygiivatlcTVARLVTDTLGRY 407
Cdd:pfam13604  62 LGEELG--------------------------------------------IPAD-------------TIAKLLHRLGGRA 84
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 281363531  408 NFFTH--IFIDEAG-ASTEPeaLIGIMGIKQTADCHVILSGDHKQLGAV 453
Cdd:pfam13604  85 GLDPGtlLIVDEAGmVGTRQ--MARLLKLAEDAGARVILVGDPRQLPSV 131
CoV_Nsp13-helicase cd21718
helicase domain of coronavirus non-structural protein 13; This model represents the helicase ...
275-662 1.20e-04

helicase domain of coronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from alpha-, beta-, gamma-, and deltacoronavirus, including pathogenic human viruses such as Severe acute respiratory syndrome coronavirus (SARS-CoV), SARS-CoV2 (also called 2019 novel CoV or 2019-nCoV), and Middle East respiratory syndrome-related (MERS) CoV. Helicases catalyze NTP-dependent unwinding of nucleic acid duplexes into single strands and are classified based on the arrangement of conserved motifs into six superfamilies. CoV Nsp13 is a member of the helicase superfamily 1 (SF1); SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Nsp13 is a component of the viral RNA synthesis replication and transcription complex (RTC). It is a multidomain protein containing a Cys/His rich zinc-binding domain (CH/ZBD), a stalk domain, a 1B domain involved in nucleic acid substrate binding, and a SF1 helicase core.


Pssm-ID: 409652 [Multi-domain]  Cd Length: 341  Bit Score: 44.83  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 275 GPPGTGKTTTIVeailQLRLQQPQSRILVTAGSNSACDTIALKLCEYIesnirlqehfaqqklpePDHQLIRVY-SRSIY 353
Cdd:cd21718   32 GPPGTGKSHFAI----GLALYYPGARIVYTACSHAAVDALCEKASKWL-----------------PNDKCSRIVpQRARV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 354 E--KGFASvpslllkNSNCSKSIYDHIKASRIVKYGIIVatlctvarlvtdtlgrynffthifIDEAGASTEPEalIGIM 431
Cdd:cd21718   91 EcfDGFKV-------NNTNAQYIFSTINALPECSADIVV------------------------VDEVSMCTNYD--LSVV 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 432 GIKQTADcHVILSGDHKQLGAviksnraaslglSRSLMERllqsdcyKSDENGNYDRNRQMRLCRN--------YRSHPQ 503
Cdd:cd21718  138 NARLKYK-HIVYVGDPAQLPA------------PRTLLTE-------GSLEPKDYNVVTRLMVGSGpdvflskcYRCPKE 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 504 IVRLFNELYYNGELKAqapamdvnlaanwsvlTNPQFPIIFQaTHGVTNREQNSTSSYNNLEAEVICWYVKRliNDRvvg 583
Cdd:cd21718  198 IVDTVSKLVYDNKLKA----------------IKPKSRQCFK-TFGKGDVRHDNGSAINRPQLEFVKRFLDR--NPR--- 255
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281363531 584 QEDVGIVAPYTAQGKLVTKLLqskGYPnveVGSVETYQGREKTIIIASLVksfTNMGFMCNPRRVNVLLSRAKALLILV 662
Cdd:cd21718  256 WRKAVFISPYNAMNNRASRLL---GLS---TQTVDSSQGSEYDYVIFCQT---TDTAHALNINRFNVAITRAKHGILVI 325
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
269-337 2.45e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 41.98  E-value: 2.45e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281363531   269 GPYILFGPPGTGKTTTIvEAILQLrLQQPQSRILVTAGSNSACDTIALKLCEYIESNIRLQEHFAQQKL 337
Cdd:smart00382   3 EVILIVGPPGSGKTTLA-RALARE-LGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRL 69
UvrD COG0210
Superfamily I DNA or RNA helicase [Replication, recombination and repair];
251-310 4.12e-04

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


Pssm-ID: 439980 [Multi-domain]  Cd Length: 721  Bit Score: 43.77  E-value: 4.12e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281363531 251 NAEQLEAVQrivagpSTQGPYILFGPPGTGKTTTIVEAILQL--RLQQPQSRILVTAGSNSA 310
Cdd:COG0210    8 NPEQRAAVE------HPEGPLLVLAGAGSGKTRVLTHRIAYLiaEGGVDPEQILAVTFTNKA 63
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
251-336 1.05e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 40.21  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 251 NAEQLEAVQRIVAGPStQGPYILFGPPGTGKtTTIVEAILQLrLQQPQSRILVTagsNSACDTIALKLCEYIESNIRLQE 330
Cdd:cd00009    3 QEEAIEALREALELPP-PKNLLLYGPPGTGK-TTLARAIANE-LFRPGAPFLYL---NASDLLEGLVVAELFGHFLVRLL 76

                 ....*.
gi 281363531 331 HFAQQK 336
Cdd:cd00009   77 FELAEK 82
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
234-327 1.16e-03

exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha subunit, RecD. RecD is part of a RecBCD complex. A related family in the Gram-positive bacteria separates in a phylogenetic tree, has an additional N-terminal extension of about 200 residues, and is not supported as a member of a RecBCD complex by neighboring genes. The related family is consequently described by a different model. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273631 [Multi-domain]  Cd Length: 582  Bit Score: 42.44  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531  234 EPATPTSLSLLNSTIYSNAEQLEAVQRIVAGPSTQGPYILFGPPGTGKTTTIVEAILQLRLQQPQS---RILVTAGSNSA 310
Cdd:TIGR01447 125 EARKRTAPSAILENLFPLLNEQNWRKTAVALALKSNFSLITGGPGTGKTTTVARLLLALVKQSPKQgklRIALAAPTGKA 204
                          90
                  ....*....|....*..
gi 281363531  311 cdtiALKLCEYIESNIR 327
Cdd:TIGR01447 205 ----AARLAESLRKAVK 217
AAA_19 pfam13245
AAA domain;
254-315 2.38e-03

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 38.74  E-value: 2.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281363531  254 QLEAVQRIVAGPstqgPYILFGPPGTGKTTTIVEAI-LQLRLQQPQSRILVTAGSNSACDTIA 315
Cdd:pfam13245   1 QREAVRTALPSK----VVLLTGGPGTGKTTTIRHIVaLLVALGGVSFPILLAAPTGRAAKRLS 59
UvrD-helicase pfam00580
UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural ...
251-310 2.64e-03

UvrD/REP helicase N-terminal domain; The Rep family helicases are composed of four structural domains. The Rep family function as dimers. REP helicases catalyze ATP dependent unwinding of double stranded DNA to single stranded DNA. Swiss:P23478, Swiss:P08394 have large insertions near to the carboxy-terminus relative to other members of the family.


Pssm-ID: 395462 [Multi-domain]  Cd Length: 267  Bit Score: 40.31  E-value: 2.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281363531  251 NAEQLEAVQrivagpSTQGPYILFGPPGTGKTTTIVEAILQLRLQQ--PQSRILVTAGSNSA 310
Cdd:pfam00580   2 NPEQRKAVT------HLGGPLLVLAGAGSGKTRVLTERIAYLILEGgiDPEEILAVTFTNKA 57
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
231-305 3.36e-03

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 40.78  E-value: 3.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281363531 231 RPQEPATPTSLSLlnstiysNAEQLEAVQRIVAGPSTQGPYILF-GPPGTGKTTTIVEAILQLRLQQpqsRILVTA 305
Cdd:COG1061   69 EAGDEASGTSFEL-------RPYQQEALEALLAALERGGGRGLVvAPTGTGKTVLALALAAELLRGK---RVLVLV 134
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
586-663 4.08e-03

C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Similar to SF2 helicases, they do not form toroidal, predominantly hexameric structures like SF3-6. SF1 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350173 [Multi-domain]  Cd Length: 89  Bit Score: 37.03  E-value: 4.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363531 586 DVGIVAPYTAQGKLVTKLLQSKG-----YPNVEVGSVETYQGREKTIIIASLVKSFTNmgfmcNPRRVNVLLSRAKALLI 660
Cdd:cd18786   12 KGVVLTPYHRDRAYLNQYLQGLSldefdLQLVGAITIDSSQGLTFDVVTLYLPTANSL-----TPRRLYVALTRARKRLV 86

                 ...
gi 281363531 661 LVG 663
Cdd:cd18786   87 IYD 89
AAA_22 pfam13401
AAA domain;
266-336 4.28e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.09  E-value: 4.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281363531  266 STQGPYILFGPPGTGKTTTIvEAILQLRLQQPQSRILVTAGSnsacDTIALKLCEYIESNIRLQEHFAQQK 336
Cdd:pfam13401   3 FGAGILVLTGESGTGKTTLL-RRLLEQLPEVRDSVVFVDLPS----GTSPKDLLRALLRALGLPLSGRLSK 68
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
275-312 9.40e-03

DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members include UvrD/Rep, Pif1-like, and Upf-1-like proteins. Like SF2, they do not form toroidal, predominantly hexameric structures like SF3-6. Their helicase core is surrounded by C and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains or domains engaged in protein-protein interactions. SF1 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: 438706 [Multi-domain]  Cd Length: 121  Bit Score: 36.70  E-value: 9.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 281363531 275 GPPGTGKTTT---IVEAILQLRLQQPQsRILVTAGSNSACD 312
Cdd:cd17914    6 GPPGTGKTRVlvkIVAALMQNKNGEPG-RILLVTPTNKAAA 45
 
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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