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Conserved domains on  [gi|15242273|ref|NP_200022|]
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P-loop containing nucleoside triphosphate hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

DEAD/DEAH box helicase family protein( domain architecture ID 13511208)

DEAD/DEAH box containing ATP-dependent helicase family protein may catalyze the unwinding of DNA or RNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
415-612 1.43e-70

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: 227.82  E-value: 1.43e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   415 FGRSLFERLVLLG-HNKHLLDVQYRMHPSISRFPNKEFYGGRIKDAENVKESIYQKRFLKGNMFDSFSFINVGRGKEEFG 493
Cdd:pfam13087   1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDDFHLPDPLGPLVFIDVDGSEEEES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   494 D-GHSPKNMVEVAVISEIISNLYKVSCERRmkVSVGVVSPYKGQMRAIQEKIGDKYSSLSGqqftLNVRSVDGFQGGEED 572
Cdd:pfam13087  81 DgGTSYSNEAEAELVVQLVEKLIKSGPEEP--SDIGVITPYRAQVRLIRKLLKRKLGGKLE----IEVNTVDGFQGREKD 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 15242273   573 IIIISTVRSNGNGKVGFLNNRQRANVALTRARHCLWVIGN 612
Cdd:pfam13087 155 VIIFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGN 194
TIGR00376 super family cl36628
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
56-634 5.43e-45

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]


The actual alignment was detected with superfamily member TIGR00376:

Pssm-ID: 273041 [Multi-domain]  Cd Length: 636  Bit Score: 170.38  E-value: 5.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273    56 TKLNSSQEDAILGCLETRNCThknsvkLIWGPPRTGKTKTVATLLFALLKLRCKTVVCAPTNTAIVQVTSRLlslfkenS 135
Cdd:TIGR00376 156 PNLNESQKEAVLFALSSKDLF------LIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERL-------A 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   136 TAENATYRLGNiilsgnrdrmginkndhvlldvflDERIGKLGKLfspfsgwmqrlESLIQFLENPEgKYERhVYELEE- 214
Cdd:TIGR00376 223 LCDQKIVRLGH------------------------PARLLKSNKQ-----------HSLDYLIENHP-KYQI-VADIREk 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   215 ----VERMNEEdereevvvniptfgefvQKNFNSLSE---EVKTCIVDLYthlpkvylpyEDVKKMIASRQTLQRIRYFL 287
Cdd:TIGR00376 266 idelIEERNKK-----------------TKPSPQKRRglsDIKILRKALK----------KREARGIESLKIASMAEWIE 318
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   288 RENSSrvdfeegnfrfdcfKRLsddclkaLRLLPKrfeipdmlENEDIRKFCLQNADIILCTASGAAEMNVErtgnVELL 367
Cdd:TIGR00376 319 TNKSI--------------DRL-------LKLLPE--------SEERIMNEILAESDATNSMAGSEILNGQY----FDVA 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   368 VVDEAAQLKEcesvAALQLPGLRHA--ILIGDEFQLPAMVHNEmcEKAKFGRSLFERLV-LLGHNKHLLDVQYRMHPSIS 444
Cdd:TIGR00376 366 VIDEASQAME----PSCLIPLLKARklILAGDHKQLPPTILSH--DAEELSLTLFERLIkEYPERSRTLNVQYRMNQKIM 439
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   445 RFPNKEFYGGRIKDAENVK--------ESIYQKRFLKGNMFDSFSFINV-GRGKEEFGDGHSPK--NMVEVAVISEIISN 513
Cdd:TIGR00376 440 EFPSREFYNGKLTAHESVAnillrdlpKVEATESEDDLETGIPLLFIDTsGCELFELKEADSTSkyNPGEAELVSEIIQA 519
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   514 LykvsceRRMKV---SVGVVSPYKGQMRAIQEKIGDKYSSLSgqqftlnVRSVDGFQGGEEDIIIISTVRSNGNGKVGFL 590
Cdd:TIGR00376 520 L------VKMGVpanDIGVITPYDAQVDLLRQLLEHRHIDIE-------VSSVDGFQGREKEVIIISFVRSNRKGEVGFL 586
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 15242273   591 NNRQRANVALTRARHCLWVIGNETTLALSGSiWATLISESRTRG 634
Cdd:TIGR00376 587 KDLRRLNVALTRARRKLIVIGDSRTLSNHKF-YKRLIEWCKQHG 629
 
Name Accession Description Interval E-value
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
415-612 1.43e-70

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: 227.82  E-value: 1.43e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   415 FGRSLFERLVLLG-HNKHLLDVQYRMHPSISRFPNKEFYGGRIKDAENVKESIYQKRFLKGNMFDSFSFINVGRGKEEFG 493
Cdd:pfam13087   1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDDFHLPDPLGPLVFIDVDGSEEEES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   494 D-GHSPKNMVEVAVISEIISNLYKVSCERRmkVSVGVVSPYKGQMRAIQEKIGDKYSSLSGqqftLNVRSVDGFQGGEED 572
Cdd:pfam13087  81 DgGTSYSNEAEAELVVQLVEKLIKSGPEEP--SDIGVITPYRAQVRLIRKLLKRKLGGKLE----IEVNTVDGFQGREKD 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 15242273   573 IIIISTVRSNGNGKVGFLNNRQRANVALTRARHCLWVIGN 612
Cdd:pfam13087 155 VIIFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGN 194
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
275-621 1.75e-59

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 214.61  E-value: 1.75e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 275 ASRQTLQRIRYFLRENSSRVDFEEGNFRFDCFKRLSDDCLKALRLLPKRFEIPDMLENEdirkfCLQNADIILCTASGAA 354
Cdd:COG1112 472 AAALLALALLESLLEELIEEHPEELEKLIAELREAARLRRALRRELKKRRELRKLLWDA-----LLELAPVVGMTPASVA 546
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 355 EMNVERTGNVELLVVDEAAQLKECESVAALQLPglRHAILIGDEFQLPAMV---HNEMCEKAKFGRSLFERLV-LLGHNK 430
Cdd:COG1112 547 RLLPLGEGSFDLVIIDEASQATLAEALGALARA--KRVVLVGDPKQLPPVVfgeEAEEVAEEGLDESLLDRLLaRLPERG 624
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 431 HLLDVQYRMHPSISRFPNKEFYGGRIKDAENVKEsiyqkRFLKGNmFDSFSFINVGRGKEEFGDGHSpkNMVEVAVISEI 510
Cdd:COG1112 625 VMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKA-----RRLADP-DSPLVFIDVDGVYERRGGSRT--NPEEAEAVVEL 696
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 511 ISNLYKVSCERRmkvSVGVVSPYKGQMRAIQEKIGDKYSSLSGQqftLNVRSVDGFQGGEEDIIIISTVRSNGN---GKV 587
Cdd:COG1112 697 VRELLEDGPDGE---SIGVITPYRAQVALIRELLREALGDGLEP---VFVGTVDRFQGDERDVIIFSLVYSNDEdvpRNF 770
                       330       340       350
                ....*....|....*....|....*....|....*
gi 15242273 588 GFLN-NRQRANVALTRARHCLWVIGNETTLALSGS 621
Cdd:COG1112 771 GFLNgGPRRLNVAVSRARRKLIVVGSRELLDSDPS 805
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
439-628 4.38e-53

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: 180.51  E-value: 4.38e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 439 MHPSISRFPNKEFYGGRIKDAENVKESIYqkRFLKGNMFDSFSFINVGRGKEEFGDGHSPKNMVEVAVISEIISNLYKVS 518
Cdd:cd18808   1 MHPEISEFPSKLFYEGKLKAGVSVAARLN--PPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 519 CERRmkvSVGVVSPYKGQMRAIQEKIGDKYSSLSGqqftLNVRSVDGFQGGEEDIIIISTVRSNG-NGKVGFLNNRQRAN 597
Cdd:cd18808  79 VKPS---SIGVITPYRAQVALIRELLRKRGGLLED----VEVGTVDNFQGREKDVIILSLVRSNEsGGSIGFLSDPRRLN 151
                       170       180       190
                ....*....|....*....|....*....|.
gi 15242273 598 VALTRARHCLWVIGNETTLALSGsIWATLIS 628
Cdd:cd18808 152 VALTRAKRGLIIVGNPDTLSKDP-LWKKLLE 181
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
56-634 5.43e-45

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: 170.38  E-value: 5.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273    56 TKLNSSQEDAILGCLETRNCThknsvkLIWGPPRTGKTKTVATLLFALLKLRCKTVVCAPTNTAIVQVTSRLlslfkenS 135
Cdd:TIGR00376 156 PNLNESQKEAVLFALSSKDLF------LIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERL-------A 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   136 TAENATYRLGNiilsgnrdrmginkndhvlldvflDERIGKLGKLfspfsgwmqrlESLIQFLENPEgKYERhVYELEE- 214
Cdd:TIGR00376 223 LCDQKIVRLGH------------------------PARLLKSNKQ-----------HSLDYLIENHP-KYQI-VADIREk 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   215 ----VERMNEEdereevvvniptfgefvQKNFNSLSE---EVKTCIVDLYthlpkvylpyEDVKKMIASRQTLQRIRYFL 287
Cdd:TIGR00376 266 idelIEERNKK-----------------TKPSPQKRRglsDIKILRKALK----------KREARGIESLKIASMAEWIE 318
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   288 RENSSrvdfeegnfrfdcfKRLsddclkaLRLLPKrfeipdmlENEDIRKFCLQNADIILCTASGAAEMNVErtgnVELL 367
Cdd:TIGR00376 319 TNKSI--------------DRL-------LKLLPE--------SEERIMNEILAESDATNSMAGSEILNGQY----FDVA 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   368 VVDEAAQLKEcesvAALQLPGLRHA--ILIGDEFQLPAMVHNEmcEKAKFGRSLFERLV-LLGHNKHLLDVQYRMHPSIS 444
Cdd:TIGR00376 366 VIDEASQAME----PSCLIPLLKARklILAGDHKQLPPTILSH--DAEELSLTLFERLIkEYPERSRTLNVQYRMNQKIM 439
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   445 RFPNKEFYGGRIKDAENVK--------ESIYQKRFLKGNMFDSFSFINV-GRGKEEFGDGHSPK--NMVEVAVISEIISN 513
Cdd:TIGR00376 440 EFPSREFYNGKLTAHESVAnillrdlpKVEATESEDDLETGIPLLFIDTsGCELFELKEADSTSkyNPGEAELVSEIIQA 519
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   514 LykvsceRRMKV---SVGVVSPYKGQMRAIQEKIGDKYSSLSgqqftlnVRSVDGFQGGEEDIIIISTVRSNGNGKVGFL 590
Cdd:TIGR00376 520 L------VKMGVpanDIGVITPYDAQVDLLRQLLEHRHIDIE-------VSSVDGFQGREKEVIIISFVRSNRKGEVGFL 586
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 15242273   591 NNRQRANVALTRARHCLWVIGNETTLALSGSiWATLISESRTRG 634
Cdd:TIGR00376 587 KDLRRLNVALTRARRKLIVIGDSRTLSNHKF-YKRLIEWCKQHG 629
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
333-438 1.42e-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: 96.51  E-value: 1.42e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 333 EDIRKFCLQNADIILCTASGAAEMNVERTGN-VELLVVDEAAQLKECESVAALQLpGLRHAILIGDEFQLPAMVHNEMCE 411
Cdd:cd18042 113 QELRASILNEADIVCTTLSSSGSDLLESLPRgFDTVIIDEAAQAVELSTLIPLRL-GCKRLILVGDPKQLPATVFSKVAQ 191
                        90       100
                ....*....|....*....|....*..
gi 15242273 412 KAKFGRSLFERLVLLGHNKHLLDVQYR 438
Cdd:cd18042 192 KLGYDRSLFERLQLAGYPVLMLTTQYR 218
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
61-408 4.05e-20

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: 90.10  E-value: 4.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273    61 SQEDAILGCLETRNCThknsvkLIWGPPRTGKTKTVATLLFALLKLRCKTV-------VCAPTNTAIVQVTSRLLSlfke 133
Cdd:pfam13086   1 SQREAIRSALSSSHFT------LIQGPPGTGKTTTIVELIRQLLSYPATSAaagprilVCAPSNAAVDNILERLLR---- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   134 nstaENATYRLgNIILSGNRDRMGINkndhvLLDVFLDERIGKLGKlfspfSGWMQRLESLIQFLENPEGKYERHVYELE 213
Cdd:pfam13086  71 ----KGQKYGP-KIVRIGHPAAISEA-----VLPVSLDYLVESKLN-----NEEDAQIVKDISKELEKLAKALRAFEKEI 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   214 EVERmneedereevvvniptfgefVQKNFNslseevktcivdlythlpkvylpyEDVKKMIASRQTLQRIRYFLRENSSR 293
Cdd:pfam13086 136 IVEK--------------------LLKSRN------------------------KDKSKLEQERRKLRSERKELRKELRR 171
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   294 VdfeegnfrfdcfkrlsddclkalrllpkrfeipdmlENEDIRKFcLQNADIILCTASGAAEMNVERTGNVELLVVDEAA 373
Cdd:pfam13086 172 R------------------------------------EQSLEREI-LDEAQIVCSTLSGAGSRLLSSLANFDVVIIDEAA 214
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 15242273   374 QLKECESVAALQLpGLRHAILIGDEFQLPAMVHNE 408
Cdd:pfam13086 215 QALEPSTLIPLLR-GPKKVVLVGDPKQLPPTVISK 248
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
55-119 6.32e-05

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: 46.12  E-value: 6.32e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242273  55 STKLNSSQEDAILGCLETRNCThknsvkLIWGPPRTGKTKTVATLLFALLKLRCKTVVCAPTNTA 119
Cdd:COG0507 122 GITLSDEQREAVALALTTRRVS------VLTGGAGTGKTTTLRALLAALEALGLRVALAAPTGKA 180
recD PRK10875
exodeoxyribonuclease V subunit alpha;
76-127 5.10e-04

exodeoxyribonuclease V subunit alpha;


Pssm-ID: 236783 [Multi-domain]  Cd Length: 615  Bit Score: 43.39  E-value: 5.10e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15242273   76 THKNSVklIWGPPRTGKTKTVATLLFALLKL----RCKTVVCAPTNTAIVQVTSRL 127
Cdd:PRK10875 166 TRRISV--ISGGPGTGKTTTVAKLLAALIQLadgeRCRIRLAAPTGKAAARLTESL 219
 
Name Accession Description Interval E-value
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
415-612 1.43e-70

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: 227.82  E-value: 1.43e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   415 FGRSLFERLVLLG-HNKHLLDVQYRMHPSISRFPNKEFYGGRIKDAENVKESIYQKRFLKGNMFDSFSFINVGRGKEEFG 493
Cdd:pfam13087   1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDDFHLPDPLGPLVFIDVDGSEEEES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   494 D-GHSPKNMVEVAVISEIISNLYKVSCERRmkVSVGVVSPYKGQMRAIQEKIGDKYSSLSGqqftLNVRSVDGFQGGEED 572
Cdd:pfam13087  81 DgGTSYSNEAEAELVVQLVEKLIKSGPEEP--SDIGVITPYRAQVRLIRKLLKRKLGGKLE----IEVNTVDGFQGREKD 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 15242273   573 IIIISTVRSNGNGKVGFLNNRQRANVALTRARHCLWVIGN 612
Cdd:pfam13087 155 VIIFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGN 194
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
275-621 1.75e-59

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 214.61  E-value: 1.75e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 275 ASRQTLQRIRYFLRENSSRVDFEEGNFRFDCFKRLSDDCLKALRLLPKRFEIPDMLENEdirkfCLQNADIILCTASGAA 354
Cdd:COG1112 472 AAALLALALLESLLEELIEEHPEELEKLIAELREAARLRRALRRELKKRRELRKLLWDA-----LLELAPVVGMTPASVA 546
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 355 EMNVERTGNVELLVVDEAAQLKECESVAALQLPglRHAILIGDEFQLPAMV---HNEMCEKAKFGRSLFERLV-LLGHNK 430
Cdd:COG1112 547 RLLPLGEGSFDLVIIDEASQATLAEALGALARA--KRVVLVGDPKQLPPVVfgeEAEEVAEEGLDESLLDRLLaRLPERG 624
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 431 HLLDVQYRMHPSISRFPNKEFYGGRIKDAENVKEsiyqkRFLKGNmFDSFSFINVGRGKEEFGDGHSpkNMVEVAVISEI 510
Cdd:COG1112 625 VMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKA-----RRLADP-DSPLVFIDVDGVYERRGGSRT--NPEEAEAVVEL 696
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 511 ISNLYKVSCERRmkvSVGVVSPYKGQMRAIQEKIGDKYSSLSGQqftLNVRSVDGFQGGEEDIIIISTVRSNGN---GKV 587
Cdd:COG1112 697 VRELLEDGPDGE---SIGVITPYRAQVALIRELLREALGDGLEP---VFVGTVDRFQGDERDVIIFSLVYSNDEdvpRNF 770
                       330       340       350
                ....*....|....*....|....*....|....*
gi 15242273 588 GFLN-NRQRANVALTRARHCLWVIGNETTLALSGS 621
Cdd:COG1112 771 GFLNgGPRRLNVAVSRARRKLIVVGSRELLDSDPS 805
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
439-628 4.38e-53

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: 180.51  E-value: 4.38e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 439 MHPSISRFPNKEFYGGRIKDAENVKESIYqkRFLKGNMFDSFSFINVGRGKEEFGDGHSPKNMVEVAVISEIISNLYKVS 518
Cdd:cd18808   1 MHPEISEFPSKLFYEGKLKAGVSVAARLN--PPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 519 CERRmkvSVGVVSPYKGQMRAIQEKIGDKYSSLSGqqftLNVRSVDGFQGGEEDIIIISTVRSNG-NGKVGFLNNRQRAN 597
Cdd:cd18808  79 VKPS---SIGVITPYRAQVALIRELLRKRGGLLED----VEVGTVDNFQGREKDVIILSLVRSNEsGGSIGFLSDPRRLN 151
                       170       180       190
                ....*....|....*....|....*....|.
gi 15242273 598 VALTRARHCLWVIGNETTLALSGsIWATLIS 628
Cdd:cd18808 152 VALTRAKRGLIIVGNPDTLSKDP-LWKKLLE 181
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
56-634 5.43e-45

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: 170.38  E-value: 5.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273    56 TKLNSSQEDAILGCLETRNCThknsvkLIWGPPRTGKTKTVATLLFALLKLRCKTVVCAPTNTAIVQVTSRLlslfkenS 135
Cdd:TIGR00376 156 PNLNESQKEAVLFALSSKDLF------LIHGPPGTGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERL-------A 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   136 TAENATYRLGNiilsgnrdrmginkndhvlldvflDERIGKLGKLfspfsgwmqrlESLIQFLENPEgKYERhVYELEE- 214
Cdd:TIGR00376 223 LCDQKIVRLGH------------------------PARLLKSNKQ-----------HSLDYLIENHP-KYQI-VADIREk 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   215 ----VERMNEEdereevvvniptfgefvQKNFNSLSE---EVKTCIVDLYthlpkvylpyEDVKKMIASRQTLQRIRYFL 287
Cdd:TIGR00376 266 idelIEERNKK-----------------TKPSPQKRRglsDIKILRKALK----------KREARGIESLKIASMAEWIE 318
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   288 RENSSrvdfeegnfrfdcfKRLsddclkaLRLLPKrfeipdmlENEDIRKFCLQNADIILCTASGAAEMNVErtgnVELL 367
Cdd:TIGR00376 319 TNKSI--------------DRL-------LKLLPE--------SEERIMNEILAESDATNSMAGSEILNGQY----FDVA 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   368 VVDEAAQLKEcesvAALQLPGLRHA--ILIGDEFQLPAMVHNEmcEKAKFGRSLFERLV-LLGHNKHLLDVQYRMHPSIS 444
Cdd:TIGR00376 366 VIDEASQAME----PSCLIPLLKARklILAGDHKQLPPTILSH--DAEELSLTLFERLIkEYPERSRTLNVQYRMNQKIM 439
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   445 RFPNKEFYGGRIKDAENVK--------ESIYQKRFLKGNMFDSFSFINV-GRGKEEFGDGHSPK--NMVEVAVISEIISN 513
Cdd:TIGR00376 440 EFPSREFYNGKLTAHESVAnillrdlpKVEATESEDDLETGIPLLFIDTsGCELFELKEADSTSkyNPGEAELVSEIIQA 519
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   514 LykvsceRRMKV---SVGVVSPYKGQMRAIQEKIGDKYSSLSgqqftlnVRSVDGFQGGEEDIIIISTVRSNGNGKVGFL 590
Cdd:TIGR00376 520 L------VKMGVpanDIGVITPYDAQVDLLRQLLEHRHIDIE-------VSSVDGFQGREKEVIIISFVRSNRKGEVGFL 586
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 15242273   591 NNRQRANVALTRARHCLWVIGNETTLALSGSiWATLISESRTRG 634
Cdd:TIGR00376 587 KDLRRLNVALTRARRKLIVIGDSRTLSNHKF-YKRLIEWCKQHG 629
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
333-438 1.42e-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: 96.51  E-value: 1.42e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 333 EDIRKFCLQNADIILCTASGAAEMNVERTGN-VELLVVDEAAQLKECESVAALQLpGLRHAILIGDEFQLPAMVHNEMCE 411
Cdd:cd18042 113 QELRASILNEADIVCTTLSSSGSDLLESLPRgFDTVIIDEAAQAVELSTLIPLRL-GCKRLILVGDPKQLPATVFSKVAQ 191
                        90       100
                ....*....|....*....|....*..
gi 15242273 412 KAKFGRSLFERLVLLGHNKHLLDVQYR 438
Cdd:cd18042 192 KLGYDRSLFERLQLAGYPVLMLTTQYR 218
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
57-438 6.81e-21

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: 91.92  E-value: 6.81e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273  57 KLNSSQEDAILGCLetrncthKNSVKLIWGPPRTGKTKTVATLLFALLKLRCKTV-VCAPTNTAIVQVTSRLlslfkens 135
Cdd:cd18039   1 ELNHSQVDAVKTAL-------QRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGPVlVCAPSNVAVDQLTEKI-------- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 136 taenatyrlgniilsgnrDRMGINkndhvlldvflderigklgklfspfsgwmqrlesliqflenpegkyerhVYELEEV 215
Cdd:cd18039  66 ------------------HQTGLK-------------------------------------------------VVRLCAK 78
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 216 ERmneedereevvvniptfgefvqknfnslsEEVKTCIVDLYTHlpkvylpyEDVKKMIaSRQTLQRIRYFLRENSSRVD 295
Cdd:cd18039  79 SR-----------------------------EAVESPVSFLALH--------NQVRNLD-SAEKLELLKLLKLETGELSS 120
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 296 FEEGNFRfdcfkrlsddclkALRLlpkrfeipdMLENEdirkfCLQNADIILCTASGAAEMNVERtGNVELLVVDEAAQL 375
Cdd:cd18039 121 ADEKRYR-------------KLKR---------KAERE-----LLRNADVICCTCVGAGDPRLSK-MKFRTVLIDEATQA 172
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242273 376 KECESVAALQLpGLRHAILIGDEFQLPAMVHNEMCEKAKFGRSLFERLVLLGHNKHLLDVQYR 438
Cdd:cd18039 173 TEPECLIPLVH-GAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVQLGIRPIRLQVQYR 234
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
61-408 4.05e-20

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: 90.10  E-value: 4.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273    61 SQEDAILGCLETRNCThknsvkLIWGPPRTGKTKTVATLLFALLKLRCKTV-------VCAPTNTAIVQVTSRLLSlfke 133
Cdd:pfam13086   1 SQREAIRSALSSSHFT------LIQGPPGTGKTTTIVELIRQLLSYPATSAaagprilVCAPSNAAVDNILERLLR---- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   134 nstaENATYRLgNIILSGNRDRMGINkndhvLLDVFLDERIGKLGKlfspfSGWMQRLESLIQFLENPEGKYERHVYELE 213
Cdd:pfam13086  71 ----KGQKYGP-KIVRIGHPAAISEA-----VLPVSLDYLVESKLN-----NEEDAQIVKDISKELEKLAKALRAFEKEI 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   214 EVERmneedereevvvniptfgefVQKNFNslseevktcivdlythlpkvylpyEDVKKMIASRQTLQRIRYFLRENSSR 293
Cdd:pfam13086 136 IVEK--------------------LLKSRN------------------------KDKSKLEQERRKLRSERKELRKELRR 171
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273   294 VdfeegnfrfdcfkrlsddclkalrllpkrfeipdmlENEDIRKFcLQNADIILCTASGAAEMNVERTGNVELLVVDEAA 373
Cdd:pfam13086 172 R------------------------------------EQSLEREI-LDEAQIVCSTLSGAGSRLLSSLANFDVVIIDEAA 214
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 15242273   374 QLKECESVAALQLpGLRHAILIGDEFQLPAMVHNE 408
Cdd:pfam13086 215 QALEPSTLIPLLR-GPKKVVLVGDPKQLPPTVISK 248
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
333-437 3.20e-17

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: 79.90  E-value: 3.20e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 333 EDIRKFCLQN-----ADIILCTASGAAEMN--VERTgNVELLVVDEAAQLKECESVAALQlPGLRHAILIGDEFQL-P-A 403
Cdd:cd17936  67 EGLLDFGPTKivrlgARVIGMTTTGAAKYRelLQAL-GPKVVIVEEAAEVLEAHILAALT-PSTEHLILIGDHKQLrPkV 144
                        90       100       110
                ....*....|....*....|....*....|....
gi 15242273 404 MVHNEMCEKAKFGRSLFERLVLLGHNKHLLDVQY 437
Cdd:cd17936 145 NVYELTAKKYNLDVSLFERLVKNGLPFVTLNVQR 178
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
315-438 3.04e-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: 76.41  E-value: 3.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 315 KALRLLPKRFEIP-DMLENEDI----------RKFCLQNADIILCTASGAAEMNVERTGNVELLVVDEAAQLKECES-VA 382
Cdd:cd18040 139 QQIKAFEARFERTqEKITEEDIktykiliweaRFEELETVDVILCTCSEAASQKMRTHANVKQCIVDECGMCTEPESlIP 218
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15242273 383 ALQLPGLRHAILIGDEFQLPAMVHNEMCEKAKFGRSLFERLvllgHNK-HLLDVQYR 438
Cdd:cd18040 219 IVSAPRAEQVVLIGDHKQLRPVVQNKEAQKLGLGRSLFERY----AEKaCMLDTQYR 271
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
346-438 2.62e-14

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: 69.57  E-value: 2.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 346 ILCTA-SGAAemnVErtgNVELLVVDEAAQLkeCESVAALQLPGLRHAILIGDEFQLPAMVHNE----MCEKAKFGRSLF 420
Cdd:cd17934  32 VLVTAqSNVA---VD---NVDVVIIDEASQI--TEPELLIALIRAKKVVLVGDPKQLPPVVQEDhaalLGLSFILSLLLL 103
                        90
                ....*....|....*...
gi 15242273 421 ERLVLLGHNKHLLDVQYR 438
Cdd:cd17934 104 FRLLLPGSPKVMLDTQYR 121
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
308-438 6.23e-14

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: 70.72  E-value: 6.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 308 RLSDDCLKALRL-LPKRfeipdMLENedIRKFCLQ---NADIILCTASGAAEMNVERTGNVELLVVDEAAQLKEcesvAA 383
Cdd:cd18044  64 RLVALKVKVVRIgHPAR-----LLES--VLDHSLDalvAAQVVLATNTGAGSRQLLPNELFDVVVIDEAAQALE----AS 132
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15242273 384 LQLPGLRH--AILIGDEFQLPAMVHNEMCEKAKFGRSLFERLVLL--GHNKHLLDVQYR 438
Cdd:cd18044 133 CWIPLLKArrCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLygESVVRMLTVQYR 191
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
343-445 5.63e-13

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: 68.22  E-value: 5.63e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 343 ADIILCTASGAAemnVERTGNVEL------LVVDEAAQLKECESVAALQLP-------GLRHAILIGDEFQLPAMVHNEM 409
Cdd:cd17935  87 AKIIAMTCTHAA---LKRGELVELgfkydnILMEEAAQILEIETFIPLLLQnpedgpnRLKRLIMIGDHHQLPPVIKNMA 163
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15242273 410 CEK-AKFGRSLFERLVLLGHNKHLLDVQYRMHPSISR 445
Cdd:cd17935 164 FQKySNMEQSLFTRLVRLGVPTVDLDAQGRARASISS 200
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
57-130 4.30e-10

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: 59.55  E-value: 4.30e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15242273  57 KLNSSQEDAILGCLETRNcthknsVKLIWGPPRTGKTKTVATLLFALLKLRCKTVVCAPTNTAIVQVTSRLLSL 130
Cdd:cd18044   1 NLNDSQKEAVKFALSQKD------VALIHGPPGTGKTTTVVEIILQAVKRGEKVLACAPSNIAVDNLVERLVAL 68
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
58-163 6.78e-09

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: 56.86  E-value: 6.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273  58 LNSSQEDAILgclETRNCTHKNSVKLIWGPPRTGKTKTVATLLFALLKLRCKTV--VCAPTNTAIVQVTSRLLSLFKENS 135
Cdd:cd18038   2 LNDEQKLAVR---NIVTGTSRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARilVCAPSNSAADLLAERLLNALVTKR 78
                        90       100
                ....*....|....*....|....*...
gi 15242273 136 taenATYRlgniILSGNRDRMGINKNDH 163
Cdd:cd18038  79 ----EILR----LNAPSRDRASVPPELL 98
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
83-120 1.32e-07

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: 50.70  E-value: 1.32e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 15242273  83 LIWGPPRTGKTKTVATLLFALLKLRC-KTV-VCAPTNTAI 120
Cdd:cd17934   3 LIQGPPGTGKTTTIAAIVLQLLKGLRgKRVlVTAQSNVAV 42
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
322-426 1.70e-07

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: 52.62  E-value: 1.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 322 KRFEIPDMlenEDIRKFclqnaDIILCTASGAAEMNVERTGNVEL--LVVDEAAQLKECESVAALQLPGLRHA--ILIGD 397
Cdd:cd18038 107 GTFRLPSL---EELKKY-----RIVVCTLMTAGRLVQAGVPNGHFthIFIDEAGQATEPEALIPLSELASKNTqiVLAGD 178
                        90       100
                ....*....|....*....|....*....
gi 15242273 398 EFQLPAMVHNEMCEKAKFGRSLFERLVLL 426
Cdd:cd18038 179 PKQLGPVVRSPLARKYGLGKSLLERLMER 207
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
507-605 2.56e-07

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: 48.97  E-value: 2.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 507 ISEIISNLYKVscerrmkvsvGVVSPYKGQMRAIQEKIgdKYSSLSGQQFTL-NVRSVDGFQGGEEDIIIISTVRSNgng 585
Cdd:cd18786   3 IVNAANGLYKG----------VVLTPYHRDRAYLNQYL--QGLSLDEFDLQLvGAITIDSSQGLTFDVVTLYLPTAN--- 67
                        90       100
                ....*....|....*....|
gi 15242273 586 kvgfLNNRQRANVALTRARH 605
Cdd:cd18786  68 ----SLTPRRLYVALTRARK 83
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
341-437 7.74e-07

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: 48.25  E-value: 7.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 341 QNADIILCTASGAAemnVERTGNVellVVDEAAQLKECE-SVAALQLPGLRHAILIGDEFQLPAMVHNEMCEKAKFGRSL 419
Cdd:cd17914  30 EPGRILLVTPTNKA---AAQLDNI---LVDEAAQILEPEtSRLIDLALDQGRVILVGDHDQLGPVWRGAVLAKICNEQSL 103
                        90
                ....*....|....*...
gi 15242273 420 FERLVLLGHNKHLLDVQY 437
Cdd:cd17914 104 FTRLVRLGVSLIRLQVQY 121
CoV_Nsp13-helicase cd21718
helicase domain of coronavirus non-structural protein 13; This model represents the helicase ...
313-613 1.37e-06

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: 50.99  E-value: 1.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 313 CLKALRLLP----KRFeIPDMLENEDIRKFCLQN--ADIILCTASGAAEMNVErtgnveLLVVDEAAQLKECESVAALQL 386
Cdd:cd21718  68 CEKASKWLPndkcSRI-VPQRARVECFDGFKVNNtnAQYIFSTINALPECSAD------IVVVDEVSMCTNYDLSVVNAR 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 387 PGLRHAILIGDEFQLPA---MVHNEMCEKAKFGRsLFERLVLLGHNKhLLDVQYRMHPSISRFPNKEFYGGRIKdAENVK 463
Cdd:cd21718 141 LKYKHIVYVGDPAQLPAprtLLTEGSLEPKDYNV-VTRLMVGSGPDV-FLSKCYRCPKEIVDTVSKLVYDNKLK-AIKPK 217
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 464 ESIYQKRFLKGNmfdsfsfinVGRgkeefgDGHSPKNMVEVAVISEIIsnlykvsCERRMKVSVGVVSPYKGQmraiqek 543
Cdd:cd21718 218 SRQCFKTFGKGD---------VRH------DNGSAINRPQLEFVKRFL-------DRNPRWRKAVFISPYNAM------- 268
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 544 iGDKYSSLSGqqftLNVRSVDGFQGGEEDIIIISTVRSNGNGKvgflnNRQRANVALTRARHCLWVIGNE 613
Cdd:cd21718 269 -NNRASRLLG----LSTQTVDSSQGSEYDYVIFCQTTDTAHAL-----NINRFNVAITRAKHGILVIMRD 328
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
317-438 1.48e-06

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: 49.54  E-value: 1.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 317 LRLLPKRFEI----PDMLENEDIRKFC-----------------LQNADIILCTASGAAeMNVERTGNVELLVVDEAAQL 375
Cdd:cd18041  63 LKLKKFGVNFlrlgRLKKIHPDVQEFTleailkscksveeleskYESVSVVATTCLGIN-HPIFRRRTFDYCIVDEASQI 141
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242273 376 KEcesvaALQLPGLRHA---ILIGDEFQLPAMVHNEMCEKAKFGRSLFERLvllgHNKHL-----LDVQYR 438
Cdd:cd18041 142 TL-----PICLGPLRLAkkfVLVGDHYQLPPLVKSREARELGMDESLFKRL----SEAHPdavvqLTIQYR 203
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
83-157 1.85e-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: 47.48  E-value: 1.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273  83 LIWGPPRTGKTKTVATLLFALLKL----RCKTVVCAPTNTAIVQVTSRLLSLFKENSTAENATY-----RLGNIILSGNR 153
Cdd:cd17914   3 LIQGPPGTGKTRVLVKIVAALMQNkngePGRILLVTPTNKAAAQLDNILVDEAAQILEPETSRLidlalDQGRVILVGDH 82

                ....
gi 15242273 154 DRMG 157
Cdd:cd17914  83 DQLG 86
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
57-128 3.58e-06

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: 48.52  E-value: 3.58e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15242273  57 KLNSSQEDAILGCL--ETRNCTHknsvkLIWGPPRTGKTKT-VATLL---FALLKLRckTVVCAPTNTAIVQVTSRLL 128
Cdd:cd18078   1 DLNELQKEAVKRILggECRPLPY-----ILFGPPGTGKTVTiIEAILqvvYNLPRSR--ILVCAPSNSAADLVTSRLH 71
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
57-147 5.37e-06

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: 47.62  E-value: 5.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273  57 KLNSSQEDAILGCLETRNCThknsvkLIWGPPRTGKTKTVATLLFALLKLRCKTVVCAPTNTAIVQVTSRLLSlFKENst 136
Cdd:cd18041   1 GLNKDQRQAIKKVLNAKDYA------LILGMPGTGKTTTIAALVRILVALGKSVLLTSYTHSAVDNILLKLKK-FGVN-- 71
                        90
                ....*....|.
gi 15242273 137 aenaTYRLGNI 147
Cdd:cd18041  72 ----FLRLGRL 78
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
367-423 4.36e-05

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: 45.17  E-value: 4.36e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15242273 367 LVVDEAAQLKECESVAALQLPGLRHAI-LIGDEFQLPAMVHNEMCEKAKFGRSLFERL 423
Cdd:cd18077 150 ILLDEAAQAMECEAIMPLALATKSTRIvLAGDHMQLSPEVYSEFARERNLHISLLERL 207
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
55-119 6.32e-05

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: 46.12  E-value: 6.32e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15242273  55 STKLNSSQEDAILGCLETRNCThknsvkLIWGPPRTGKTKTVATLLFALLKLRCKTVVCAPTNTA 119
Cdd:COG0507 122 GITLSDEQREAVALALTTRRVS------VLTGGAGTGKTTTLRALLAALEALGLRVALAAPTGKA 180
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
59-120 1.93e-04

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: 41.80  E-value: 1.93e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15242273  59 NSSQEDAILGCLetrncTHKNSVklIWGPPRTGKTKTVATLLFALLKlRCKTV-VCAPTNTAI 120
Cdd:cd18043   1 DSSQEAAIISAR-----NGKNVV--IQGPPGTGKSQTIANIIANALA-RGKRVlFVSEKKAAL 55
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
62-116 3.48e-04

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: 41.39  E-value: 3.48e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15242273  62 QEDAILGCLetrncthKNSVKLIWGPPRTGKTKTVATLLFALLKLRCKTVVCAPT 116
Cdd:cd17933   2 QKAAVRLVL-------RNRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVLAAPT 49
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
79-138 4.37e-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: 41.23  E-value: 4.37e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242273  79 NSVKLIWGPPRTGKTKTVA-TLLFALLKLRCKTVVCAPTNTAIVQVTSRLLSLFKENSTAE 138
Cdd:cd00046   1 GENVLITAPTGSGKTLAALlAALLLLLKKGKKVLVLVPTKALALQTAERLRELFGPGIRVA 61
recD PRK10875
exodeoxyribonuclease V subunit alpha;
76-127 5.10e-04

exodeoxyribonuclease V subunit alpha;


Pssm-ID: 236783 [Multi-domain]  Cd Length: 615  Bit Score: 43.39  E-value: 5.10e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15242273   76 THKNSVklIWGPPRTGKTKTVATLLFALLKL----RCKTVVCAPTNTAIVQVTSRL 127
Cdd:PRK10875 166 TRRISV--ISGGPGTGKTTTVAKLLAALIQLadgeRCRIRLAAPTGKAAARLTESL 219
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
58-134 7.76e-04

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: 40.99  E-value: 7.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273  58 LNSSQEDAILGCLetrncthKNSVKLIWGPPRTGKTKTVATLLFALLKLRCKT-----VVCAPTNTAIVQVTSRLLSLFK 132
Cdd:cd17936   2 LDPSQLEALKHAL-------TSELALIQGPPGTGKTFLGVKLVRALLQNQDLSitgpiLVVCYTNHALDQFLEGLLDFGP 74

                ..
gi 15242273 133 EN 134
Cdd:cd17936  75 TK 76
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
325-425 3.64e-03

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: 39.66  E-value: 3.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242273 325 EIPDMLENEDIRKfcLQNADIIL--CTASGAAEMNVERTGNVELLVVDEAAQLKECESVAALQLPGLRHA--ILIGDEFQ 400
Cdd:cd18078  98 RKLYCRLGEDLSK--ASRHRIVIstCSTAGLLYQMGLPVGHFTHVFVDEAGQATEPESLIPLGLISSRDGqiILAGDPMQ 175
                        90       100
                ....*....|....*....|....*
gi 15242273 401 LPAMVHNEMCEKAKFGRSLFERLVL 425
Cdd:cd18078 176 LGPVIKSRLASAYGLGVSFLERLMN 200
 
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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