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Conserved domains on  [gi|758988465|ref|XP_011393161|]
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DNA-binding protein SMUBP-2 [Neurospora crassa OR74A]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 1007248)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; similar to Saccharomyces cerevisiae DNA polymerase alpha-associated DNA helicase A that acts as DNA polymerase alpha-associated DNA helicase which may be involved in DNA replication

EC:  3.6.4.12
Gene Ontology:  GO:0003678|GO:0003677|GO:0016887|GO:0005524
PubMed:  16935882|1552844

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
TIGR00376 super family cl36628
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
 23-728 2.92e-171

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: 505.89  E-value: 2.92e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465   23 ELAAEIAENSELIGLHTPTALQRAGLALTNLVVNaQRTGYGGKTVLELGPDSATVTitssssssssgqkgggydgpelpe 102
Cdd:TIGR00376   2 ERDAEISAMMNEIRRLSLKQRERRGRAILNLQGK-IRGGLLGFLLVRFGRRKAIAT------------------------ 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  103 hGIRTGDIVVVSEQPAGSAKKREVreLEKKGAKGVVTrvgrgvvgvALDEDkgeenvvgtGGLGGSGRVWMVKLADDVTY 182
Cdd:TIGR00376  57 -EISVGDIVLVSRGNPLQSDLTGV--VTRVGKRFITV---------ALEES---------VPQWSLKRVRIDLYANDVTF 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  183 RRMNGTMEKLQKMseseHSMFIRVLFGQSSPSPVPadltndpEVGNIDWVDPTLNDSQKDAIRFALASREIALIHGPPGv 262
Cdd:TIGR00376 116 KRMKEALRALTEN----HSRLLEFLLGREAPSKAS-------EIHDFQFFDPNLNESQKEAVLFALSSKDLFLIHGPPG- 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  263 clyvpspqsvaymsnpplqTGKTHTLIELILQLLRRDLRILVCGPSNISVDNIVERLSPHKLPILRLGHPARLLPSVLSH 342
Cdd:TIGR00376 184 -------------------TGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLGHPARLLKSNKQH 244

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  343 SLDILTTTSDAGAIVKDVRAEMDA-KQASIRKTRNGRERRAIYAELKELRKEYRERERRCVSDLVGRSKVVLATLHG--- 418
Cdd:TIGR00376 245 SLDYLIENHPKYQIVADIREKIDElIEERNKKTKPSPQKRRGLSDIKILRKALKKREARGIESLKIASMAEWIETNKsid 324

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  419 ---------------------------AGGYQLKNEEFDVVIIDEASQALEAQCWVPLLWAKKAVLAGDHLQLPPTIKSl 471
Cdd:TIGR00376 325 rllkllpeseerimneilaesdatnsmAGSEILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAGDHKQLPPTILS- 403

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  472 nsraattkekKEGQTLETTLFDRLLTLHgPSIKRMLTTQYRMHEKIMRFPSDELYESKLVAAEHVRERLLKDLPyeGVEA 551
Cdd:TIGR00376 404 ----------HDAEELSLTLFERLIKEY-PERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLP--KVEA 470

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  552 -----NDDTTEPLIFIDTQGGDFPEKNEEELdgngstdkkkvirslhgESKSNEMEAALVRQHVRGLIKAGVRPDDIAVV 626
Cdd:TIGR00376 471 tesedDLETGIPLLFIDTSGCELFELKEADS-----------------TSKYNPGEAELVSEIIQALVKMGVPANDIGVI 533

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  627 TPYNAQLSILAPL-KDEFPGIELGSVDGFQGREKEAVIVSLVRSNDEGEVGFLGEKRRLNVAMTRPKRSLTVIGDSETVk 705
Cdd:TIGR00376 534 TPYDAQVDLLRQLlEHRHIDIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGDSRTL- 612

                         730       740
                  ....*....|....*....|...
gi 758988465  706 KGSTFLKRWMEFLEENADLRYPD 728
Cdd:TIGR00376 613 SNHKFYKRLIEWCKQHGEVREAF 635
 
Name Accession Description Interval E-value
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
 23-728 2.92e-171

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: 505.89  E-value: 2.92e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465   23 ELAAEIAENSELIGLHTPTALQRAGLALTNLVVNaQRTGYGGKTVLELGPDSATVTitssssssssgqkgggydgpelpe 102
Cdd:TIGR00376   2 ERDAEISAMMNEIRRLSLKQRERRGRAILNLQGK-IRGGLLGFLLVRFGRRKAIAT------------------------ 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  103 hGIRTGDIVVVSEQPAGSAKKREVreLEKKGAKGVVTrvgrgvvgvALDEDkgeenvvgtGGLGGSGRVWMVKLADDVTY 182
Cdd:TIGR00376  57 -EISVGDIVLVSRGNPLQSDLTGV--VTRVGKRFITV---------ALEES---------VPQWSLKRVRIDLYANDVTF 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  183 RRMNGTMEKLQKMseseHSMFIRVLFGQSSPSPVPadltndpEVGNIDWVDPTLNDSQKDAIRFALASREIALIHGPPGv 262
Cdd:TIGR00376 116 KRMKEALRALTEN----HSRLLEFLLGREAPSKAS-------EIHDFQFFDPNLNESQKEAVLFALSSKDLFLIHGPPG- 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  263 clyvpspqsvaymsnpplqTGKTHTLIELILQLLRRDLRILVCGPSNISVDNIVERLSPHKLPILRLGHPARLLPSVLSH 342
Cdd:TIGR00376 184 -------------------TGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLGHPARLLKSNKQH 244

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  343 SLDILTTTSDAGAIVKDVRAEMDA-KQASIRKTRNGRERRAIYAELKELRKEYRERERRCVSDLVGRSKVVLATLHG--- 418
Cdd:TIGR00376 245 SLDYLIENHPKYQIVADIREKIDElIEERNKKTKPSPQKRRGLSDIKILRKALKKREARGIESLKIASMAEWIETNKsid 324

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  419 ---------------------------AGGYQLKNEEFDVVIIDEASQALEAQCWVPLLWAKKAVLAGDHLQLPPTIKSl 471
Cdd:TIGR00376 325 rllkllpeseerimneilaesdatnsmAGSEILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAGDHKQLPPTILS- 403

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  472 nsraattkekKEGQTLETTLFDRLLTLHgPSIKRMLTTQYRMHEKIMRFPSDELYESKLVAAEHVRERLLKDLPyeGVEA 551
Cdd:TIGR00376 404 ----------HDAEELSLTLFERLIKEY-PERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLP--KVEA 470

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  552 -----NDDTTEPLIFIDTQGGDFPEKNEEELdgngstdkkkvirslhgESKSNEMEAALVRQHVRGLIKAGVRPDDIAVV 626
Cdd:TIGR00376 471 tesedDLETGIPLLFIDTSGCELFELKEADS-----------------TSKYNPGEAELVSEIIQALVKMGVPANDIGVI 533

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  627 TPYNAQLSILAPL-KDEFPGIELGSVDGFQGREKEAVIVSLVRSNDEGEVGFLGEKRRLNVAMTRPKRSLTVIGDSETVk 705
Cdd:TIGR00376 534 TPYDAQVDLLRQLlEHRHIDIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGDSRTL- 612

                         730       740
                  ....*....|....*....|...
gi 758988465  706 KGSTFLKRWMEFLEENADLRYPD 728
Cdd:TIGR00376 613 SNHKFYKRLIEWCKQHGEVREAF 635
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
 236-512 7.10e-98

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: 300.30  E-value: 7.10e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 236 LNDSQKDAIRFALASREIALIHGPPGvclyvpspqsvaymsnpplqTGKTHTLIELILQLLRRDLRILVCGPSNISVDNI 315
Cdd:cd18044    2 LNDSQKEAVKFALSQKDVALIHGPPG--------------------TGKTTTVVEIILQAVKRGEKVLACAPSNIAVDNL 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 316 VERLSPHKLPILRLGHPARLLPSVLSHSLDILTttsdagaivkdvraemdakqasirktrngrerraiyaelkelrkeyr 395
Cdd:cd18044   62 VERLVALKVKVVRIGHPARLLESVLDHSLDALV----------------------------------------------- 94

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 396 ererrcvsdlvgRSKVVLATLHGAGGYQLK-NEEFDVVIIDEASQALEAQCWVPLLWAKKAVLAGDHLQLPPTIKSlnsr 474
Cdd:cd18044   95 ------------AAQVVLATNTGAGSRQLLpNELFDVVVIDEAAQALEASCWIPLLKARRCILAGDHKQLPPTILS---- 158

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 758988465 475 aattkEKKEGQTLETTLFDRLLTLHGPSIKRMLTTQYR 512
Cdd:cd18044  159 -----DKAARGGLGVTLFERLVNLYGESVVRMLTVQYR 191
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 487-702 1.33e-77

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: 247.46  E-value: 1.33e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  487 LETTLFDRLLTLHgPSIKRMLTTQYRMHEKIMRFPSDELYESKLVAAEHVRERllkdlPYEGVEANDDTTEPLIFIDTQG 566
Cdd:pfam13087   1 LDRSLFERLQELG-PSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAER-----PLPDDFHLPDPLGPLVFIDVDG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  567 GdfpekneEELDGNGSTdkkkvirslhgeSKSNEMEAALVRQHVRGLIKAGVRPD-DIAVVTPYNAQLSI----LAPLKD 641
Cdd:pfam13087  75 S-------EEEESDGGT------------SYSNEAEAELVVQLVEKLIKSGPEEPsDIGVITPYRAQVRLirklLKRKLG 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 758988465  642 EFPGIELGSVDGFQGREKEAVIVSLVRSNDEGEVGFLGEKRRLNVAMTRPKRSLTVIGDSE 702
Cdd:pfam13087 136 GKLEIEVNTVDGFQGREKDVIIFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNAK 196
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
190-721 1.99e-76

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 262.76  E-value: 1.99e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 190 EKLQKMSESEHSMFIRVLFGQSSPSPVPADLTNDPEVGNIDWVDPTLNDSQKDAIRFALASREIALIHGPPGVCLYVPSP 269
Cdd:COG1112  322 LAARLAAALAALLLLLLLEELALLAALLLLLELALLRLLAALLLALALLLLLALEELLLLALLRLLAEGLALLLLLLLAA 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 270 QSVAYMSNPPLQTGKTHTLIELILQLLRRDLRILVCGPSNISVDNIVERLSPHKLPILRLGHPARLLPSVLSHSLDILTT 349
Cdd:COG1112  402 LLRLARALLLLALLLAAAAAALAALLLLALALLAALLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALL 481

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 350 TSDAGAIVKDVRAEMDAKQASIRKTRNGRERraiyaeLKELRKEYRERERRCVSDLVGRSKVVLATLHGAGGY-QLKNEE 428
Cdd:COG1112  482 ESLLEELIEEHPEELEKLIAELREAARLRRA------LRRELKKRRELRKLLWDALLELAPVVGMTPASVARLlPLGEGS 555

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 429 FDVVIIDEASQALEAQCWVPLLWAKKAVLAGDHLQLPPTIKSlnsraaTTKEKKEGQTLETTLFDRLLTLHgPSIKRMLT 508
Cdd:COG1112  556 FDLVIIDEASQATLAEALGALARAKRVVLVGDPKQLPPVVFG------EEAEEVAEEGLDESLLDRLLARL-PERGVMLR 628

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 509 TQYRMHEKIMRFPSDELYESKLVAAEHVRERLLkdlpyegveanDDTTEPLIFIDTQGgdfpekneeeldgngstdkkkv 588
Cdd:COG1112  629 EHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRL-----------ADPDSPLVFIDVDG---------------------- 675

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 589 IRSLHGESKSNEMEAALVRQHVRGLIKAGVRPDDIAVVTPYNAQLS-----ILAPLKDEFPGIELGSVDGFQGREKEAVI 663
Cdd:COG1112  676 VYERRGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVAlirelLREALGDGLEPVFVGTVDRFQGDERDVII 755

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 758988465 664 VSLVRSNDE---GEVGFL-GEKRRLNVAMTRPKRSLTVIGDSETVK--KGSTFLKRWMEFLEEN 721
Cdd:COG1112  756 FSLVYSNDEdvpRNFGFLnGGPRRLNVAVSRARRKLIVVGSRELLDsdPSTPALKRLLEYLERA 819
 
Name Accession Description Interval E-value
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
 23-728 2.92e-171

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: 505.89  E-value: 2.92e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465   23 ELAAEIAENSELIGLHTPTALQRAGLALTNLVVNaQRTGYGGKTVLELGPDSATVTitssssssssgqkgggydgpelpe 102
Cdd:TIGR00376   2 ERDAEISAMMNEIRRLSLKQRERRGRAILNLQGK-IRGGLLGFLLVRFGRRKAIAT------------------------ 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  103 hGIRTGDIVVVSEQPAGSAKKREVreLEKKGAKGVVTrvgrgvvgvALDEDkgeenvvgtGGLGGSGRVWMVKLADDVTY 182
Cdd:TIGR00376  57 -EISVGDIVLVSRGNPLQSDLTGV--VTRVGKRFITV---------ALEES---------VPQWSLKRVRIDLYANDVTF 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  183 RRMNGTMEKLQKMseseHSMFIRVLFGQSSPSPVPadltndpEVGNIDWVDPTLNDSQKDAIRFALASREIALIHGPPGv 262
Cdd:TIGR00376 116 KRMKEALRALTEN----HSRLLEFLLGREAPSKAS-------EIHDFQFFDPNLNESQKEAVLFALSSKDLFLIHGPPG- 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  263 clyvpspqsvaymsnpplqTGKTHTLIELILQLLRRDLRILVCGPSNISVDNIVERLSPHKLPILRLGHPARLLPSVLSH 342
Cdd:TIGR00376 184 -------------------TGKTRTVVELIRQLVKRGLRVLVTAPSNIAVDNLLERLALCDQKIVRLGHPARLLKSNKQH 244

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  343 SLDILTTTSDAGAIVKDVRAEMDA-KQASIRKTRNGRERRAIYAELKELRKEYRERERRCVSDLVGRSKVVLATLHG--- 418
Cdd:TIGR00376 245 SLDYLIENHPKYQIVADIREKIDElIEERNKKTKPSPQKRRGLSDIKILRKALKKREARGIESLKIASMAEWIETNKsid 324

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  419 ---------------------------AGGYQLKNEEFDVVIIDEASQALEAQCWVPLLWAKKAVLAGDHLQLPPTIKSl 471
Cdd:TIGR00376 325 rllkllpeseerimneilaesdatnsmAGSEILNGQYFDVAVIDEASQAMEPSCLIPLLKARKLILAGDHKQLPPTILS- 403

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  472 nsraattkekKEGQTLETTLFDRLLTLHgPSIKRMLTTQYRMHEKIMRFPSDELYESKLVAAEHVRERLLKDLPyeGVEA 551
Cdd:TIGR00376 404 ----------HDAEELSLTLFERLIKEY-PERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLP--KVEA 470

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  552 -----NDDTTEPLIFIDTQGGDFPEKNEEELdgngstdkkkvirslhgESKSNEMEAALVRQHVRGLIKAGVRPDDIAVV 626
Cdd:TIGR00376 471 tesedDLETGIPLLFIDTSGCELFELKEADS-----------------TSKYNPGEAELVSEIIQALVKMGVPANDIGVI 533

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  627 TPYNAQLSILAPL-KDEFPGIELGSVDGFQGREKEAVIVSLVRSNDEGEVGFLGEKRRLNVAMTRPKRSLTVIGDSETVk 705
Cdd:TIGR00376 534 TPYDAQVDLLRQLlEHRHIDIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIGDSRTL- 612

                         730       740
                  ....*....|....*....|...
gi 758988465  706 KGSTFLKRWMEFLEENADLRYPD 728
Cdd:TIGR00376 613 SNHKFYKRLIEWCKQHGEVREAF 635
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
 236-512 7.10e-98

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: 300.30  E-value: 7.10e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 236 LNDSQKDAIRFALASREIALIHGPPGvclyvpspqsvaymsnpplqTGKTHTLIELILQLLRRDLRILVCGPSNISVDNI 315
Cdd:cd18044    2 LNDSQKEAVKFALSQKDVALIHGPPG--------------------TGKTTTVVEIILQAVKRGEKVLACAPSNIAVDNL 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 316 VERLSPHKLPILRLGHPARLLPSVLSHSLDILTttsdagaivkdvraemdakqasirktrngrerraiyaelkelrkeyr 395
Cdd:cd18044   62 VERLVALKVKVVRIGHPARLLESVLDHSLDALV----------------------------------------------- 94

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 396 ererrcvsdlvgRSKVVLATLHGAGGYQLK-NEEFDVVIIDEASQALEAQCWVPLLWAKKAVLAGDHLQLPPTIKSlnsr 474
Cdd:cd18044   95 ------------AAQVVLATNTGAGSRQLLpNELFDVVVIDEAAQALEASCWIPLLKARRCILAGDHKQLPPTILS---- 158

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 758988465 475 aattkEKKEGQTLETTLFDRLLTLHGPSIKRMLTTQYR 512
Cdd:cd18044  159 -----DKAARGGLGVTLFERLVNLYGESVVRMLTVQYR 191
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 487-702 1.33e-77

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: 247.46  E-value: 1.33e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  487 LETTLFDRLLTLHgPSIKRMLTTQYRMHEKIMRFPSDELYESKLVAAEHVRERllkdlPYEGVEANDDTTEPLIFIDTQG 566
Cdd:pfam13087   1 LDRSLFERLQELG-PSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAER-----PLPDDFHLPDPLGPLVFIDVDG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  567 GdfpekneEELDGNGSTdkkkvirslhgeSKSNEMEAALVRQHVRGLIKAGVRPD-DIAVVTPYNAQLSI----LAPLKD 641
Cdd:pfam13087  75 S-------EEEESDGGT------------SYSNEAEAELVVQLVEKLIKSGPEEPsDIGVITPYRAQVRLirklLKRKLG 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 758988465  642 EFPGIELGSVDGFQGREKEAVIVSLVRSNDEGEVGFLGEKRRLNVAMTRPKRSLTVIGDSE 702
Cdd:pfam13087 136 GKLEIEVNTVDGFQGREKDVIIFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNAK 196
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
190-721 1.99e-76

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 262.76  E-value: 1.99e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 190 EKLQKMSESEHSMFIRVLFGQSSPSPVPADLTNDPEVGNIDWVDPTLNDSQKDAIRFALASREIALIHGPPGVCLYVPSP 269
Cdd:COG1112  322 LAARLAAALAALLLLLLLEELALLAALLLLLELALLRLLAALLLALALLLLLALEELLLLALLRLLAEGLALLLLLLLAA 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 270 QSVAYMSNPPLQTGKTHTLIELILQLLRRDLRILVCGPSNISVDNIVERLSPHKLPILRLGHPARLLPSVLSHSLDILTT 349
Cdd:COG1112  402 LLRLARALLLLALLLAAAAAALAALLLLALALLAALLALLLLLAAALAALLALLLLLLLALAALLLLLAAAAALLALALL 481

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 350 TSDAGAIVKDVRAEMDAKQASIRKTRNGRERraiyaeLKELRKEYRERERRCVSDLVGRSKVVLATLHGAGGY-QLKNEE 428
Cdd:COG1112  482 ESLLEELIEEHPEELEKLIAELREAARLRRA------LRRELKKRRELRKLLWDALLELAPVVGMTPASVARLlPLGEGS 555

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 429 FDVVIIDEASQALEAQCWVPLLWAKKAVLAGDHLQLPPTIKSlnsraaTTKEKKEGQTLETTLFDRLLTLHgPSIKRMLT 508
Cdd:COG1112  556 FDLVIIDEASQATLAEALGALARAKRVVLVGDPKQLPPVVFG------EEAEEVAEEGLDESLLDRLLARL-PERGVMLR 628

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 509 TQYRMHEKIMRFPSDELYESKLVAAEHVRERLLkdlpyegveanDDTTEPLIFIDTQGgdfpekneeeldgngstdkkkv 588
Cdd:COG1112  629 EHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRL-----------ADPDSPLVFIDVDG---------------------- 675

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 589 IRSLHGESKSNEMEAALVRQHVRGLIKAGVRPDDIAVVTPYNAQLS-----ILAPLKDEFPGIELGSVDGFQGREKEAVI 663
Cdd:COG1112  676 VYERRGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVAlirelLREALGDGLEPVFVGTVDRFQGDERDVII 755

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 758988465 664 VSLVRSNDE---GEVGFL-GEKRRLNVAMTRPKRSLTVIGDSETVK--KGSTFLKRWMEFLEEN 721
Cdd:COG1112  756 FSLVYSNDEdvpRNFGFLnGGPRRLNVAVSRARRKLIVVGSRELLDsdPSTPALKRLLEYLERA 819
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 239-470 6.51e-63

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: 210.28  E-value: 6.51e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  239 SQKDAIRFALASREIALIHGPPGvclyvpspqsvaymsnpplqTGKTHTLIELILQLLRRDL-------RILVCGPSNIS 311
Cdd:pfam13086   1 SQREAIRSALSSSHFTLIQGPPG--------------------TGKTTTIVELIRQLLSYPAtsaaagpRILVCAPSNAA 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  312 VDNIVERLSP----HKLPILRLGHPARLLPSVLSHSLDILT----TTSDAGAIVKDVRAE------------------MD 365
Cdd:pfam13086  61 VDNILERLLRkgqkYGPKIVRIGHPAAISEAVLPVSLDYLVesklNNEEDAQIVKDISKEleklakalrafekeiiveKL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465  366 AKQASIRKTRNGRERRAIYAELKELRKEYRERERRCVSDLVGRSKVVLATLHGAGGYQLKN-EEFDVVIIDEASQALEAQ 444
Cdd:pfam13086 141 LKSRNKDKSKLEQERRKLRSERKELRKELRRREQSLEREILDEAQIVCSTLSGAGSRLLSSlANFDVVIIDEAAQALEPS 220

                         250       260
                  ....*....|....*....|....*..
gi 758988465  445 CWVPLLWA-KKAVLAGDHLQLPPTIKS 470
Cdd:pfam13086 221 TLIPLLRGpKKVVLVGDPKQLPPTVIS 247
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 513-719 8.59e-59

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: 197.07  E-value: 8.59e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 513 MHEKIMRFPSDELYESKLVAAEHVRERllkdlpyEGVEANDDTTEPLIFIDTQGGDfpeknEEELDGNgstdkkkvirsl 592
Cdd:cd18808    1 MHPEISEFPSKLFYEGKLKAGVSVAAR-------LNPPPLPGPSKPLVFVDVSGGE-----EREESGT------------ 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 593 hgeSKSNEMEAALVRQHVRGLIKAGVRPDDIAVVTPYNAQL----SILAPLKDEFPGIELGSVDGFQGREKEAVIVSLVR 668
Cdd:cd18808   57 ---SKSNEAEAELVVELVKYLLKSGVKPSSIGVITPYRAQValirELLRKRGGLLEDVEVGTVDNFQGREKDVIILSLVR 133

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 758988465 669 SNDEGE-VGFLGEKRRLNVAMTRPKRSLTVIGDSETVKKgSTFLKRWMEFLE 719
Cdd:cd18808  134 SNESGGsIGFLSDPRRLNVALTRAKRGLIIVGNPDTLSK-DPLWKKLLEYLE 184
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
 236-512 2.53e-40

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: 147.00  E-value: 2.53e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 236 LNDSQKDAIRFALASREIALIHGPPGvclyvpspqsvaymsnpplqTGKTHTLIELILQLLRRDLRILVCGPSNISVDNI 315
Cdd:cd18041    2 LNKDQRQAIKKVLNAKDYALILGMPG--------------------TGKTTTIAALVRILVALGKSVLLTSYTHSAVDNI 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 316 VERLSPHKLPILRLGHPARLLPSVLSHSLDILTTTSDagaivkdvraemdakqasirktrngrerraIYAELKelrkeyr 395
Cdd:cd18041   62 LLKLKKFGVNFLRLGRLKKIHPDVQEFTLEAILKSCK------------------------------SVEELE------- 104

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 396 ererrcvsDLVGRSKVVLATLHGAGGYQLKNEEFDVVIIDEASQALEAQCWVPLLWAKKAVLAGDHLQLPPTIKSLNSRa 475
Cdd:cd18041  105 --------SKYESVSVVATTCLGINHPIFRRRTFDYCIVDEASQITLPICLGPLRLAKKFVLVGDHYQLPPLVKSREAR- 175

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 758988465 476 attkekKEGqtLETTLFDRLLTLHgPSIKRMLTTQYR 512
Cdd:cd18041  176 ------ELG--MDESLFKRLSEAH-PDAVVQLTIQYR 203
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
 236-512 2.30e-34

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: 130.41  E-value: 2.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 236 LNDSQKDAIRFAL-ASREIALIHGPPGvclyvpspqsvaymsnpplqTGKTHTLIELILQLLRRDL-------------- 300
Cdd:cd18042    1 LNESQLEAIASALqNSPGITLIQGPPG--------------------TGKTKTIVGILSVLLAGKYrkyyekvkkklrkl 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 301 -----------RILVCGPSNISVDNIVERlsphklpilrlghparllpsvlshsldiltttsdagaIVKDVRAEMDAKQA 369
Cdd:cd18042   61 qrnlnnkkkknRILVCAPSNAAVDEIVLR-------------------------------------LLSEGFLDGDGRSY 103

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 370 SIRKTRNGRE--RRAIyaelkelrkeyrererrcvsdlVGRSKVVLATLHGAGGYQLKN--EEFDVVIIDEASQALEAQC 445
Cdd:cd18042  104 KPNVVRVGRQelRASI----------------------LNEADIVCTTLSSSGSDLLESlpRGFDTVIIDEAAQAVELST 161

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758988465 446 WVPL-LWAKKAVLAGDHLQLPPTIKSLNSRAAttkekkegqTLETTLFDRLLtLHGPSIKrMLTTQYR 512
Cdd:cd18042  162 LIPLrLGCKRLILVGDPKQLPATVFSKVAQKL---------GYDRSLFERLQ-LAGYPVL-MLTTQYR 218
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
 236-512 2.85e-33

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: 128.13  E-value: 2.85e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 236 LNDSQKDAIRFALaSREIALIHGPPGvclyvpspqsvaymsnpplqTGKTHTLIELILQLLRRDL-RILVCGPSNISVDN 314
Cdd:cd18039    2 LNHSQVDAVKTAL-QRPLSLIQGPPG--------------------TGKTVTSATIVYHLVKQGNgPVLVCAPSNVAVDQ 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 315 IVERLSPHKLPILRLGHPAR-LLPSVLSH-SLDI----LTTTSDAGAIVKDVRAEMDAKQASIRKTRNGRERRAiyaelk 388
Cdd:cd18039   61 LTEKIHQTGLKVVRLCAKSReAVESPVSFlALHNqvrnLDSAEKLELLKLLKLETGELSSADEKRYRKLKRKAE------ 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 389 elrkeyrererrcvSDLVGRSKVVLATLHGAGGYQLKNEEFDVVIIDEASQALEAQCWVPL-LWAKKAVLAGDHLQLPPT 467
Cdd:cd18039  135 --------------RELLRNADVICCTCVGAGDPRLSKMKFRTVLIDEATQATEPECLIPLvHGAKQVILVGDHCQLGPV 200

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 758988465 468 IksLNSRAAttkekKEGqtLETTLFDRLLTL-HGPSikrMLTTQYR 512
Cdd:cd18039  201 V--MCKKAA-----KAG--LSQSLFERLVQLgIRPI---RLQVQYR 234
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
 236-498 1.86e-30

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: 119.65  E-value: 1.86e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 236 LNDSQKDAIRFALASREIA---LIHGPPGvclyvpspqsvaymsnpplqTGKTHTLIELILQLLRR--DLRILVCGPSNI 310
Cdd:cd18038    2 LNDEQKLAVRNIVTGTSRPppyIIFGPPG--------------------TGKTVTLVEAILQVLRQppEARILVCAPSNS 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 311 SVDNIVERLSPHKLP---ILRLGHPARLLPSVLSHSLDIltttsdagaivkdvraemdakqasirkTRNGRERRAIYAEL 387
Cdd:cd18038   62 AADLLAERLLNALVTkreILRLNAPSRDRASVPPELLPY---------------------------CNSKAEGTFRLPSL 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 388 KelrkeyrererrcvsDLVgRSKVVLATLHGAG---GYQLKNEEFDVVIIDEASQALEAQCWVPLLWAKKA----VLAGD 460
Cdd:cd18038  115 E---------------ELK-KYRIVVCTLMTAGrlvQAGVPNGHFTHIFIDEAGQATEPEALIPLSELASKntqiVLAGD 178

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 758988465 461 HLQLPPTIKSlnSRAAttkekkeGQTLETTLFDRLLTL 498
Cdd:cd18038  179 PKQLGPVVRS--PLAR-------KYGLGKSLLERLMER 207
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
 253-512 6.43e-25

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: 100.00  E-value: 6.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 253 IALIHGPPGvclyvpspqsvaymsnpplqTGKTHTLIELILQLLR--RDLRILVCGPSNISVDNIverlsphklpilrlg 330
Cdd:cd17934    1 ISLIQGPPG--------------------TGKTTTIAAIVLQLLKglRGKRVLVTAQSNVAVDNV--------------- 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 331 hparllpsvlshsldiltttsdagaivkdvraemdakqasirktrngrerraiyaelkelrkeyrererrcvsdlvgrsk 410
Cdd:cd17934      --------------------------------------------------------------------------------

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 411 vvlatlhgaggyqlkneefDVVIIDEASQALEAQCWVPLLWAKKAVLAGDHLQLPPTIKSlnsraatTKEKKEGQTLETT 490
Cdd:cd17934   46 -------------------DVVIIDEASQITEPELLIALIRAKKVVLVGDPKQLPPVVQE-------DHAALLGLSFILS 99

                        250       260
                 ....*....|....*....|..
gi 758988465 491 LFDRLLTLHGPSIKRMLTTQYR 512
Cdd:cd17934  100 LLLLFRLLLPGSPKVMLDTQYR 121
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
 236-531 5.27e-20

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: 89.74  E-value: 5.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 236 LNDSQKDAIRFALA--SREIA-LIHGPPGvclyvpspqsvaymsnpplqTGKTHTLIELILQLLRR--DLRILVCGPSNI 310
Cdd:cd18078    2 LNELQKEAVKRILGgeCRPLPyILFGPPG--------------------TGKTVTIIEAILQVVYNlpRSRILVCAPSNS 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 311 SVDNIVERLSPHKlpILRLGHPARLlpsvlshsldiltttsdagaiVKDVRAEMDAKQASIRKTRNGRERRAIyaelkel 390
Cdd:cd18078   62 AADLVTSRLHESK--VLKPGDMVRL---------------------NAVNRFESTVIDARKLYCRLGEDLSKA------- 111

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 391 rkeyrererrcvsdlvGRSKVVLATLHGAGGYQ---LKNEEFDVVIIDEASQALEAQCWVPL-LWAKKA---VLAGDHLQ 463
Cdd:cd18078  112 ----------------SRHRIVISTCSTAGLLYqmgLPVGHFTHVFVDEAGQATEPESLIPLgLISSRDgqiILAGDPMQ 175

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 758988465 464 LPPTIKSLNSRAAttkekkegqTLETTLFDRLltlhgpsikrMLTTQYRMHEKimRFPSDELYESKLV 531
Cdd:cd18078  176 LGPVIKSRLASAY---------GLGVSFLERL----------MNRPLYLRDPN--RFGESGGYNPLLV 222
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
 235-511 3.49e-15

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: 74.12  E-value: 3.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 235 TLNDSQKDAIRFALaSREIALIHGPPGvclyvpspqsvaymsnpplqTGKTHT---LIELILQLLR--RDLRILVCGPSN 309
Cdd:cd17936    1 TLDPSQLEALKHAL-TSELALIQGPPG--------------------TGKTFLgvkLVRALLQNQDlsITGPILVVCYTN 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 310 ISVDNIVERLSPHKLP-ILRLGHparllpSVLshsldILTTTsdaGAivkdvraemdakqasirktrngrerrAIYAELk 388
Cdd:cd17936   60 HALDQFLEGLLDFGPTkIVRLGA------RVI-----GMTTT---GA--------------------------AKYREL- 98

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 389 elrkeyrererrcvsdlvgrskvvlatlhgaggyqLKNEEFDVVIIDEASQALEAQ---CWVPllWAKKAVLAGDHLQLP 465
Cdd:cd17936   99 -----------------------------------LQALGPKVVIVEEAAEVLEAHilaALTP--STEHLILIGDHKQLR 141

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 758988465 466 PtikSLNSRAATTKEKKegqtLETTLFDRLLTLHGPSIkrMLTTQY 511
Cdd:cd17936  142 P---KVNVYELTAKKYN----LDVSLFERLVKNGLPFV--TLNVQR 178
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
 236-512 4.67e-12

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: 67.16  E-value: 4.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 236 LNDSQKDAIRFALaSREIALIHGPPGvclyvpspqsvaymsnpplqTGKTHTLIELILQLLRRDLR-------------I 302
Cdd:cd18040    2 LNPSQNHAVRTAL-TKPFTLIQGPPG--------------------TGKTVTGVHIAYWFAKQNREiqsvsgegdggpcV 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 303 LVCGPSNISVDNIVERLSPHK-LPILRL-GHPARLL----PSVLSHSLDILTTTSDAGAIVKDVRAEMDAKQASirkTRN 376
Cdd:cd18040   61 LYCGPSNKSVDVVAELLLKVPgLKILRVySEQIETTeypiPNEPRHPNKKSERESKPNSELSSITLHHRIRQPS---NPH 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 377 GRERRAIYAELKELRKEYRERERRCVSDLVGRSK--------VVLATLHGAGGYQLKnEEFDV--VIIDEASQALEAQCW 446
Cdd:cd18040  138 SQQIKAFEARFERTQEKITEEDIKTYKILIWEARfeeletvdVILCTCSEAASQKMR-THANVkqCIVDECGMCTEPESL 216

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 758988465 447 VPLLWA---KKAVLAGDHLQLPPTIKSLNSRaattkekKEGqtLETTLFDRLltlhgPSIKRMLTTQYR 512
Cdd:cd18040  217 IPIVSApraEQVVLIGDHKQLRPVVQNKEAQ-------KLG--LGRSLFERY-----AEKACMLDTQYR 271
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
 235-512 5.17e-10

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: 60.19  E-value: 5.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 235 TLNDSQKDAIRFALASREIALihgPPGVCLyvpspqsvaymsnPPLQTGKTHTLIELILQLLRR-DLRILVCGPSNISVD 313
Cdd:cd18077    1 RLNAKQKEAVLAITTPLSIQL---PPVLLI-------------GPFGTGKTFTLAQAVKHILQQpETRILICTHSNSAAD 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 314 -NIVERLSPHKLPILRLGHPARLL----------PSVLSHSLdiltttsdagaivkdvraeMDAkqasirktrNGRERRA 382
Cdd:cd18077   65 lYIKEYLHPYVETGNPRARPLRVYyrnrwvktvhPVVQKYCL-------------------IDE---------HGTFRMP 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 383 IYAElkelrkeyrererrcvsdlVGRSKVVLATLHGAGGY-QLKNEE--FDVVIIDEASQALEAQCWVPLLWAKKA---V 456
Cdd:cd18077  117 TRED-------------------VMRHRVVVVTLSTSQYLcQLDLEPgfFTHILLDEAAQAMECEAIMPLALATKStriV 177

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 758988465 457 LAGDHLQLPPTIKSLNSRaattkEKKEGQTLETTLFDRLLTLHGPSIkrMLTTQYR 512
Cdd:cd18077  178 LAGDHMQLSPEVYSEFAR-----ERNLHISLLERLYEHYPSEHPCRI--LLCENYR 226
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
 428-529 7.00e-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: 59.36  E-value: 7.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 428 EFDVVIIDEASQALEAQCWVPLLWA---------KKAVLAGDHLQLPPTIKSLNSRAATtkekkegqTLETTLFDRLLTL 498
Cdd:cd17935  110 KYDNILMEEAAQILEIETFIPLLLQnpedgpnrlKRLIMIGDHHQLPPVIKNMAFQKYS--------NMEQSLFTRLVRL 181

                         90       100       110
                 ....*....|....*....|....*....|.
gi 758988465 499 HGPSIKrmLTTQYRMHEKIMrfpsdELYESK 529
Cdd:cd17935  182 GVPTVD--LDAQGRARASIS-----SLYNWR 205
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
 236-495 7.29e-10

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: 59.90  E-value: 7.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 236 LNDSQKDAIRF----ALASREIA--LIHGPPGvclyvpspqsvaymsnpplqTGKTHTLIELILQLLRR-DLRILVCGPS 308
Cdd:cd18076    2 GNNKQQLAFNFiagkPSEARFVPplLIYGPFG--------------------TGKTFTLAMAALEVIREpGTKVLICTHT 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 309 NISVD-NIVERLSPHKLPILRLGHPARLLPSvlSHSLDIL-TTTSDAGAIVKDvraemdaKQASIRKTRngrerraiyae 386
Cdd:cd18076   62 NSAADiYIREYFHPYVDKGHPEARPLRIKAT--DRPNAITdPDTITYCCLTKD-------RQCFRLPTR----------- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 758988465 387 lkelrkeyrererrcvsDLVGRSKVVLAT------LHGAGGYqlkneeFDVVIIDEASQALEAQCWVPLLWA---KKAVL 457
Cdd:cd18076  122 -----------------DELDFHNIVITTtamafnLHVLSGF------FTHIFIDEAAQMLECEALIPLSYAgpkTRVVL 178

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 758988465 458 AGDHLQLPPTIKSLNsraattkekkEGQTLETTLFDRL 495
Cdd:cd18076  179 AGDHMQMTPKLFSVA----------DYNRANHTLLNRL 206
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
 406-468 4.38e-09

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: 55.28  E-value: 4.38e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 758988465 406 VGRSKVVLATLHGAGGY-QLKNEEFDVVIIDEASQALEAQCwVPLLW-AKKAVLAGDHLQLPPTI 468
Cdd:cd18043   57 VVRFPCWIMSPLSVSQYlPLNRNLFDLVIFDEASQIPIEEA-LPALFrGKQVVVVGDDKQLPPSI 120
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
 428-469 3.34e-04

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: 40.93  E-value: 3.34e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 758988465 428 EFDVVIIDEASQALEAQCWVP---LLWAKKAVLAGDHLQLPPTIK 469
Cdd:cd17914   46 QLDNILVDEAAQILEPETSRLidlALDQGRVILVGDHDQLGPVWR 90
 
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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