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Conserved domains on  [gi|332189722|gb|AEE27843|]
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P-loop containing nucleoside triphosphate hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
 396-622 2.81e-108

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: 335.36  E-value: 2.81e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  396 ALNAEQICSIEMVLGCK-GAPPYVIHGPPGTGKTMTLVEAIVQLYTTQRNARVLVCAPSNSAADHILEKLLCLEGVRikd 474
Cdd:cd18038     1 ELNDEQKLAVRNIVTGTsRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLLAERLLNALVTK--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  475 NEIFRLNAATRSYEEIKPEIIRFCF-FDELIFKCPPLKALTRYKLVVSTYMSASLLNAEGVNRGHFTHILLDEAGQASEP 553
Cdd:cd18038    78 REILRLNAPSRDRASVPPELLPYCNsKAEGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQATEP 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332189722  554 ENMIAVSNLCLTETVVVLAGDPRQLGPVIYSRDAESLGLGKSYLERLFECDYYC---EGDENYVTKLVKNYR 622
Cdd:cd18038   158 EALIPLSELASKNTQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMERPLYYkdgEYNPSYITKLLKNYR 229
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 623-812 4.71e-67

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: 222.49  E-value: 4.71e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  623 CHPEILDLPSKLFYDGELVASkeDTDSVLASLNFLPNKEFPMVFYGIQGCDEREGNNPSWFNRIEISKVIETIKRLTAND 702
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAG--VSVAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  703 cVQEEDIGVITPYRQQVMKIKEVLDRLDM--TEVKVGSVEQFQGQEKQVIIISTVRSTIKHNEfdraycLGFLSNPRRFN 780
Cdd:cd18808    79 -VKPSSIGVITPYRAQVALIRELLRKRGGllEDVEVGTVDNFQGREKDVIILSLVRSNESGGS------IGFLSDPRRLN 151

                         170       180       190
                  ....*....|....*....|....*....|..
gi 332189722  781 VAITRAISLLVIIGNPHIICKDMNWNKLLWRC 812
Cdd:cd18808   152 VALTRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
dermokine super family cl42387
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 815-962 9.25e-06

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


The actual alignment was detected with superfamily member cd21118:

Pssm-ID: 455732 [Multi-domain]  Cd Length: 495  Bit Score: 49.61  E-value: 9.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  815 NNAYQGCGLPEQEEFVEEPFKQEGSSNG-----PQYPPEAEWNNSGELNNGGANENGEWSDGWNNNGGTKEKNEWSDGWN 889
Cdd:cd21118   196 NNQNSGCTNPPPSGSHESFSNSGGSSSSgssgsQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGS 275

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332189722  890 SNGGGTkkkDEWSDGWDNNGGTNGINQEGSSNAPqdpqeaEWN----DSGEVKNGGTKEKDVRSDGWNNNGGKNEKE 962
Cdd:cd21118   276 GSGGSS---SGGSNGWGGSSSSGGSGGSGGGNKP------ECNnpgnDVRMAGGGGSQGSKESSGSHGSNGGNGQAE 343
 
Name Accession Description Interval E-value
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
 396-622 2.81e-108

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: 335.36  E-value: 2.81e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  396 ALNAEQICSIEMVLGCK-GAPPYVIHGPPGTGKTMTLVEAIVQLYTTQRNARVLVCAPSNSAADHILEKLLCLEGVRikd 474
Cdd:cd18038     1 ELNDEQKLAVRNIVTGTsRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLLAERLLNALVTK--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  475 NEIFRLNAATRSYEEIKPEIIRFCF-FDELIFKCPPLKALTRYKLVVSTYMSASLLNAEGVNRGHFTHILLDEAGQASEP 553
Cdd:cd18038    78 REILRLNAPSRDRASVPPELLPYCNsKAEGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQATEP 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332189722  554 ENMIAVSNLCLTETVVVLAGDPRQLGPVIYSRDAESLGLGKSYLERLFECDYYC---EGDENYVTKLVKNYR 622
Cdd:cd18038   158 EALIPLSELASKNTQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMERPLYYkdgEYNPSYITKLLKNYR 229
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 623-812 4.71e-67

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: 222.49  E-value: 4.71e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  623 CHPEILDLPSKLFYDGELVASkeDTDSVLASLNFLPNKEFPMVFYGIQGCDEREGNNPSWFNRIEISKVIETIKRLTAND 702
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAG--VSVAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  703 cVQEEDIGVITPYRQQVMKIKEVLDRLDM--TEVKVGSVEQFQGQEKQVIIISTVRSTIKHNEfdraycLGFLSNPRRFN 780
Cdd:cd18808    79 -VKPSSIGVITPYRAQVALIRELLRKRGGllEDVEVGTVDNFQGREKDVIILSLVRSNESGGS------IGFLSDPRRLN 151

                         170       180       190
                  ....*....|....*....|....*....|..
gi 332189722  781 VAITRAISLLVIIGNPHIICKDMNWNKLLWRC 812
Cdd:cd18808   152 VALTRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 592-796 3.08e-66

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: 220.88  E-value: 3.08e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   592 LGKSYLERLFECDYYCegdenyVTKLVKNYRCHPEILDLPSKLFYDGELVASKEDTDSVLASLNFLPNKEFPMVFYGIQG 671
Cdd:pfam13087    1 LDRSLFERLQELGPSA------VVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDDFHLPDPLGPLVFIDVDG 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   672 CDEREGNN-PSWFNRIEISKVIETIKRLTANDCVQEEDIGVITPYRQQVMKIKEVLDRLDMT--EVKVGSVEQFQGQEKQ 748
Cdd:pfam13087   75 SEEEESDGgTSYSNEAEAELVVQLVEKLIKSGPEEPSDIGVITPYRAQVRLIRKLLKRKLGGklEIEVNTVDGFQGREKD 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 332189722   749 VIIISTVRSTIKHNefdraycLGFLSNPRRFNVAITRAISLLVIIGNP 796
Cdd:pfam13087  155 VIIFSCVRSNEKGG-------IGFLSDPRRLNVALTRAKRGLIIVGNA 195
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
 350-835 2.14e-63

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: 227.01  E-value: 2.14e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   350 TYNRI--NTRRLYQAVDAAEmldpNFLFPSLHSgKRMIKTKPFVPISPALNAEQICSIEMVLGCKGAppYVIHGPPGTGK 427
Cdd:TIGR00376  114 TFKRMkeALRALTENHSRLL----EFLLGREAP-SKASEIHDFQFFDPNLNESQKEAVLFALSSKDL--FLIHGPPGTGK 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   428 TMTLVEAIVQLytTQRNARVLVCAPSNSAADHILEKLLCLEG--VRI--------------------------------- 472
Cdd:TIGR00376  187 TRTVVELIRQL--VKRGLRVLVTAPSNIAVDNLLERLALCDQkiVRLghparllksnkqhsldylienhpkyqivadire 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   473 -----------------------KDNEIFRLNAATRSYEEIKPEIIRFCF--------FDELIFKCPPLKALTRYKLVVS 521
Cdd:TIGR00376  265 kidelieernkktkpspqkrrglSDIKILRKALKKREARGIESLKIASMAewietnksIDRLLKLLPESEERIMNEILAE 344

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   522 TYMSASLLNAEGVNRGHFTHILLDEAGQASEPENMIAVsnlcLTETVVVLAGDPRQLGPVIYSRDAEslGLGKSYLERLF 601
Cdd:TIGR00376  345 SDATNSMAGSEILNGQYFDVAVIDEASQAMEPSCLIPL----LKARKLILAGDHKQLPPTILSHDAE--ELSLTLFERLI 418

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   602 EcdYYCEgdenYVTKLVKNYRCHPEILDLPSKLFYDGELVASKEDTDSVLASL---------NFLPNKEfPMVFYGIQGC 672
Cdd:TIGR00376  419 K--EYPE----RSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLpkveateseDDLETGI-PLLFIDTSGC 491

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   673 D---EREGNNPSWFNRIEISKVIETIKRLTANDcVQEEDIGVITPYRQQVMKIKEVLDrLDMTEVKVGSVEQFQGQEKQV 749
Cdd:TIGR00376  492 ElfeLKEADSTSKYNPGEAELVSEIIQALVKMG-VPANDIGVITPYDAQVDLLRQLLE-HRHIDIEVSSVDGFQGREKEV 569

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   750 IIISTVRStikhnefDRAYCLGFLSNPRRFNVAITRAISLLVIIGNPHIICKDMNWNKLLWRCvdnnayqgcglpEQEEF 829
Cdd:TIGR00376  570 IIISFVRS-------NRKGEVGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWC------------KQHGE 630


                   ....*.
gi 332189722   830 VEEPFK 835
Cdd:TIGR00376  631 VREAFK 636
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
431-799 4.43e-61

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 223.85  E-value: 4.43e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  431 LVEAIVQLYTTQRNARVLVCAPSNSAADHILEKLLCLEGVRIKDnEIFRLNAATRSYEEIKPEIIRFCFFDELIFKcppl 510
Cdd:COG1112   455 LLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEK-LIAELREAARLRRALRRELKKRRELRKLLWD---- 529

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  511 KALTRYKLVVSTymSASLLNAEGVNRGHFTHILLDEAGQASEPENMIAvsnLCLTETVVVlAGDPRQLGPVIYSRDAESL 590
Cdd:COG1112   530 ALLELAPVVGMT--PASVARLLPLGEGSFDLVIIDEASQATLAEALGA---LARAKRVVL-VGDPKQLPPVVFGEEAEEV 603

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  591 ---GLGKSYLERLFEcdyyceGDENYVTKLVKNYRCHPEILDLPSKLFYDGELVASKEDTDSVLaslnflPNKEFPMVFY 667
Cdd:COG1112   604 aeeGLDESLLDRLLA------RLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRL------ADPDSPLVFI 671

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  668 GIQGCDEREGNnpSWFNRIEISKVIETIKRLtANDCVQEEDIGVITPYRQQVMKIKEVLDRLDMTE---VKVGSVEQFQG 744
Cdd:COG1112   672 DVDGVYERRGG--SRTNPEEAEAVVELVREL-LEDGPDGESIGVITPYRAQVALIRELLREALGDGlepVFVGTVDRFQG 748

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 332189722  745 QEKQVIIISTVRStiKHNEFDRAycLGFLS-NPRRFNVAITRAISLLVIIGNPHII 799
Cdd:COG1112   749 DERDVIIFSLVYS--NDEDVPRN--FGFLNgGPRRLNVAVSRARRKLIVVGSRELL 800
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 419-585 1.64e-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: 92.02  E-value: 1.64e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   419 IHGPPGTGKTMTLVEAIVQLYTTQRNA-----RVLVCAPSNSAADHILEKLL-CLEG-----VRI--------------- 472
Cdd:pfam13086   18 IQGPPGTGKTTTIVELIRQLLSYPATSaaagpRILVCAPSNAAVDNILERLLrKGQKygpkiVRIghpaaiseavlpvsl 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   473 ---------------KDNEIFRLNAATRSYEEIKPEIIRFCFFDELIFKCPPLKALTRYKL------------------- 518
Cdd:pfam13086   98 dylvesklnneedaqIVKDISKELEKLAKALRAFEKEIIVEKLLKSRNKDKSKLEQERRKLrserkelrkelrrreqsle 177

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332189722   519 ---------VVSTYMSA---SLLNAEGvnrghFTHILLDEAGQASEPENMIAVSNLClteTVVVLAGDPRQLGPVIYSR 585
Cdd:pfam13086  178 reildeaqiVCSTLSGAgsrLLSSLAN-----FDVVIIDEAAQALEPSTLIPLLRGP---KKVVLVGDPKQLPPTVISK 248
DEXDc smart00487
DEAD-like helicases superfamily;
418-547 5.32e-07

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 51.34  E-value: 5.32e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722    418 VIHGPPGTGKTMTLVEAIVQLYTTQRNARVLVCAPSNSAADHILEKLLclegvriKDNEIFRLNAATRSYEEIKPEIIRF 497
Cdd:smart00487   28 ILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELK-------KLGPSLGLKVVGLYGGDSKREQLRK 100

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 332189722    498 CffdelifkcpplkALTRYKLVVSTYMSA-SLLNAEGVNRGHFTHILLDEA 547
Cdd:smart00487  101 L-------------ESGKTDILVTTPGRLlDLLENDKLSLSNVDLVILDEA 138
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 815-962 9.25e-06

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 49.61  E-value: 9.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  815 NNAYQGCGLPEQEEFVEEPFKQEGSSNG-----PQYPPEAEWNNSGELNNGGANENGEWSDGWNNNGGTKEKNEWSDGWN 889
Cdd:cd21118   196 NNQNSGCTNPPPSGSHESFSNSGGSSSSgssgsQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGS 275

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332189722  890 SNGGGTkkkDEWSDGWDNNGGTNGINQEGSSNAPqdpqeaEWN----DSGEVKNGGTKEKDVRSDGWNNNGGKNEKE 962
Cdd:cd21118   276 GSGGSS---SGGSNGWGGSSSSGGSGGSGGGNKP------ECNnpgnDVRMAGGGGSQGSKESSGSHGSNGGNGQAE 343
recD PRK10875
exodeoxyribonuclease V subunit alpha;
418-464 4.26e-03

exodeoxyribonuclease V subunit alpha;


Pssm-ID: 236783 [Multi-domain]  Cd Length: 615  Bit Score: 41.08  E-value: 4.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 332189722  418 VIHGPPGTGKTMT---LVEAIVQLYTTQRnARVLVCAPSNSAADHILEKL 464
Cdd:PRK10875  171 VISGGPGTGKTTTvakLLAALIQLADGER-CRIRLAAPTGKAAARLTESL 219
 
Name Accession Description Interval E-value
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
 396-622 2.81e-108

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: 335.36  E-value: 2.81e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  396 ALNAEQICSIEMVLGCK-GAPPYVIHGPPGTGKTMTLVEAIVQLYTTQRNARVLVCAPSNSAADHILEKLLCLEGVRikd 474
Cdd:cd18038     1 ELNDEQKLAVRNIVTGTsRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEARILVCAPSNSAADLLAERLLNALVTK--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  475 NEIFRLNAATRSYEEIKPEIIRFCF-FDELIFKCPPLKALTRYKLVVSTYMSASLLNAEGVNRGHFTHILLDEAGQASEP 553
Cdd:cd18038    78 REILRLNAPSRDRASVPPELLPYCNsKAEGTFRLPSLEELKKYRIVVCTLMTAGRLVQAGVPNGHFTHIFIDEAGQATEP 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332189722  554 ENMIAVSNLCLTETVVVLAGDPRQLGPVIYSRDAESLGLGKSYLERLFECDYYC---EGDENYVTKLVKNYR 622
Cdd:cd18038   158 EALIPLSELASKNTQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERLMERPLYYkdgEYNPSYITKLLKNYR 229
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
 623-812 4.71e-67

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: 222.49  E-value: 4.71e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  623 CHPEILDLPSKLFYDGELVASkeDTDSVLASLNFLPNKEFPMVFYGIQGCDEREGNNPSWFNRIEISKVIETIKRLTAND 702
Cdd:cd18808     1 MHPEISEFPSKLFYEGKLKAG--VSVAARLNPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  703 cVQEEDIGVITPYRQQVMKIKEVLDRLDM--TEVKVGSVEQFQGQEKQVIIISTVRSTIKHNEfdraycLGFLSNPRRFN 780
Cdd:cd18808    79 -VKPSSIGVITPYRAQVALIRELLRKRGGllEDVEVGTVDNFQGREKDVIILSLVRSNESGGS------IGFLSDPRRLN 151

                         170       180       190
                  ....*....|....*....|....*....|..
gi 332189722  781 VAITRAISLLVIIGNPHIICKDMNWNKLLWRC 812
Cdd:cd18808   152 VALTRAKRGLIIVGNPDTLSKDPLWKKLLEYL 183
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 592-796 3.08e-66

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: 220.88  E-value: 3.08e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   592 LGKSYLERLFECDYYCegdenyVTKLVKNYRCHPEILDLPSKLFYDGELVASKEDTDSVLASLNFLPNKEFPMVFYGIQG 671
Cdd:pfam13087    1 LDRSLFERLQELGPSA------VVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDDFHLPDPLGPLVFIDVDG 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   672 CDEREGNN-PSWFNRIEISKVIETIKRLTANDCVQEEDIGVITPYRQQVMKIKEVLDRLDMT--EVKVGSVEQFQGQEKQ 748
Cdd:pfam13087   75 SEEEESDGgTSYSNEAEAELVVQLVEKLIKSGPEEPSDIGVITPYRAQVRLIRKLLKRKLGGklEIEVNTVDGFQGREKD 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 332189722   749 VIIISTVRSTIKHNefdraycLGFLSNPRRFNVAITRAISLLVIIGNP 796
Cdd:pfam13087  155 VIIFSCVRSNEKGG-------IGFLSDPRRLNVALTRAKRGLIIVGNA 195
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
 397-622 6.60e-66

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: 221.09  E-value: 6.60e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  397 LNAEQICSIEMVLGCKGAP-PYVIHGPPGTGKTMTLVEAIVQLYTTQRNARVLVCAPSNSAADHILEKLLclEGVRIKDN 475
Cdd:cd18078     2 LNELQKEAVKRILGGECRPlPYILFGPPGTGKTVTIIEAILQVVYNLPRSRILVCAPSNSAADLVTSRLH--ESKVLKPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  476 EIFRLNAATRSYEEIKPEIIRFCFfdelifKCPPLKALTRYKLVVSTYMSASLLNAEGVNRGHFTHILLDEAGQASEPEN 555
Cdd:cd18078    80 DMVRLNAVNRFESTVIDARKLYCR------LGEDLSKASRHRIVISTCSTAGLLYQMGLPVGHFTHVFVDEAGQATEPES 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332189722  556 MIAVSNLCLTETVVVLAGDPRQLGPVIYSRDAESLGLGKSYLERLFECDYYCEGDENY----------VTKLVKNYR 622
Cdd:cd18078   154 LIPLGLISSRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLMNRPLYLRDPNRFgesggynpllVTKLVDNYR 230
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
 350-835 2.14e-63

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: 227.01  E-value: 2.14e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   350 TYNRI--NTRRLYQAVDAAEmldpNFLFPSLHSgKRMIKTKPFVPISPALNAEQICSIEMVLGCKGAppYVIHGPPGTGK 427
Cdd:TIGR00376  114 TFKRMkeALRALTENHSRLL----EFLLGREAP-SKASEIHDFQFFDPNLNESQKEAVLFALSSKDL--FLIHGPPGTGK 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   428 TMTLVEAIVQLytTQRNARVLVCAPSNSAADHILEKLLCLEG--VRI--------------------------------- 472
Cdd:TIGR00376  187 TRTVVELIRQL--VKRGLRVLVTAPSNIAVDNLLERLALCDQkiVRLghparllksnkqhsldylienhpkyqivadire 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   473 -----------------------KDNEIFRLNAATRSYEEIKPEIIRFCF--------FDELIFKCPPLKALTRYKLVVS 521
Cdd:TIGR00376  265 kidelieernkktkpspqkrrglSDIKILRKALKKREARGIESLKIASMAewietnksIDRLLKLLPESEERIMNEILAE 344

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   522 TYMSASLLNAEGVNRGHFTHILLDEAGQASEPENMIAVsnlcLTETVVVLAGDPRQLGPVIYSRDAEslGLGKSYLERLF 601
Cdd:TIGR00376  345 SDATNSMAGSEILNGQYFDVAVIDEASQAMEPSCLIPL----LKARKLILAGDHKQLPPTILSHDAE--ELSLTLFERLI 418

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   602 EcdYYCEgdenYVTKLVKNYRCHPEILDLPSKLFYDGELVASKEDTDSVLASL---------NFLPNKEfPMVFYGIQGC 672
Cdd:TIGR00376  419 K--EYPE----RSRTLNVQYRMNQKIMEFPSREFYNGKLTAHESVANILLRDLpkveateseDDLETGI-PLLFIDTSGC 491

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   673 D---EREGNNPSWFNRIEISKVIETIKRLTANDcVQEEDIGVITPYRQQVMKIKEVLDrLDMTEVKVGSVEQFQGQEKQV 749
Cdd:TIGR00376  492 ElfeLKEADSTSKYNPGEAELVSEIIQALVKMG-VPANDIGVITPYDAQVDLLRQLLE-HRHIDIEVSSVDGFQGREKEV 569

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   750 IIISTVRStikhnefDRAYCLGFLSNPRRFNVAITRAISLLVIIGNPHIICKDMNWNKLLWRCvdnnayqgcglpEQEEF 829
Cdd:TIGR00376  570 IIISFVRS-------NRKGEVGFLKDLRRLNVALTRARRKLIVIGDSRTLSNHKFYKRLIEWC------------KQHGE 630


                   ....*.
gi 332189722   830 VEEPFK 835
Cdd:TIGR00376  631 VREAFK 636
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
431-799 4.43e-61

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 223.85  E-value: 4.43e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  431 LVEAIVQLYTTQRNARVLVCAPSNSAADHILEKLLCLEGVRIKDnEIFRLNAATRSYEEIKPEIIRFCFFDELIFKcppl 510
Cdd:COG1112   455 LLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEK-LIAELREAARLRRALRRELKKRRELRKLLWD---- 529

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  511 KALTRYKLVVSTymSASLLNAEGVNRGHFTHILLDEAGQASEPENMIAvsnLCLTETVVVlAGDPRQLGPVIYSRDAESL 590
Cdd:COG1112   530 ALLELAPVVGMT--PASVARLLPLGEGSFDLVIIDEASQATLAEALGA---LARAKRVVL-VGDPKQLPPVVFGEEAEEV 603

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  591 ---GLGKSYLERLFEcdyyceGDENYVTKLVKNYRCHPEILDLPSKLFYDGELVASKEDTDSVLaslnflPNKEFPMVFY 667
Cdd:COG1112   604 aeeGLDESLLDRLLA------RLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRL------ADPDSPLVFI 671

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  668 GIQGCDEREGNnpSWFNRIEISKVIETIKRLtANDCVQEEDIGVITPYRQQVMKIKEVLDRLDMTE---VKVGSVEQFQG 744
Cdd:COG1112   672 DVDGVYERRGG--SRTNPEEAEAVVELVREL-LEDGPDGESIGVITPYRAQVALIRELLREALGDGlepVFVGTVDRFQG 748

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 332189722  745 QEKQVIIISTVRStiKHNEFDRAycLGFLS-NPRRFNVAITRAISLLVIIGNPHII 799
Cdd:COG1112   749 DERDVIIFSLVYS--NDEDVPRN--FGFLNgGPRRLNVAVSRARRKLIVVGSRELL 800
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
 397-600 6.85e-36

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: 134.66  E-value: 6.85e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  397 LNAEQICSIEMVLGCKgaPPYVIHGPPGTGKTMTLVEAIVQLytTQRNARVLVCAPSNSAADHILEKLLCLeGVRikdne 476
Cdd:cd18044     2 LNDSQKEAVKFALSQK--DVALIHGPPGTGKTTTVVEIILQA--VKRGEKVLACAPSNIAVDNLVERLVAL-KVK----- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  477 IFRLNAATRsyeeIKPEIIRFCffdelifkcppLKALTRYKLVVSTYMSASllnAEGVNRG-HFTHILLDEAGQASEPEN 555
Cdd:cd18044    72 VVRIGHPAR----LLESVLDHS-----------LDALVAAQVVLATNTGAG---SRQLLPNeLFDVVVIDEAAQALEASC 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 332189722  556 MIAVsnlcLTETVVVLAGDPRQLGPVIYSRDAESLGLGKSYLERL 600
Cdd:cd18044   134 WIPL----LKARRCILAGDHKQLPPTILSDKAARGGLGVTLFERL 174
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
 397-622 2.58e-35

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: 134.15  E-value: 2.58e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  397 LNAEQ---ICSIEMVLGcKGAPPYVIHGPPGTGKTMTLVEAIVQLyTTQRNARVLVCAPSNSAAD-HILEKLLCLEGVRI 472
Cdd:cd18077     2 LNAKQkeaVLAITTPLS-IQLPPVLLIGPFGTGKTFTLAQAVKHI-LQQPETRILICTHSNSAADlYIKEYLHPYVETGN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  473 KDNEIFRLNAATRSYEEIKPEIIRFCFFDEL-IFKCPPLKALTRYKLVVSTYMSASLLNAEGVNRGHFTHILLDEAGQAS 551
Cdd:cd18077    80 PRARPLRVYYRNRWVKTVHPVVQKYCLIDEHgTFRMPTREDVMRHRVVVVTLSTSQYLCQLDLEPGFFTHILLDEAAQAM 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332189722  552 EPENMIAVSnLCLTETVVVLAGDPRQLGPVIYSRDAESLGLGKSYLERLFE---CDYYCEgdenyvTKLVKNYR 622
Cdd:cd18077   160 ECEAIMPLA-LATKSTRIVLAGDHMQLSPEVYSEFARERNLHISLLERLYEhypSEHPCR------ILLCENYR 226
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
 397-600 8.77e-29

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: 115.42  E-value: 8.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  397 LNAEQICSIEMVLGckgAPPYVIHGPPGTGKTMTLVeAIVQLYTTQRNARVLVCAPSNSAADHILEKLlCLEGVRIkdne 476
Cdd:cd18039     2 LNHSQVDAVKTALQ---RPLSLIQGPPGTGKTVTSA-TIVYHLVKQGNGPVLVCAPSNVAVDQLTEKI-HQTGLKV---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  477 iFRLNAATRS---------------YEEIKPEIIRFCFFDELIFKCPPLKALTRYKLVVSTYMSASLLNAEGV------- 534
Cdd:cd18039    73 -VRLCAKSREavespvsflalhnqvRNLDSAEKLELLKLLKLETGELSSADEKRYRKLKRKAERELLRNADVIcctcvga 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332189722  535 -----NRGHFTHILLDEAGQASEPENMIAVSNLClteTVVVLAGDPRQLGPVIYSRDAESLGLGKSYLERL 600
Cdd:cd18039   152 gdprlSKMKFRTVLIDEATQATEPECLIPLVHGA---KQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERL 219
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
 397-622 3.44e-27

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: 110.02  E-value: 3.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  397 LNAEQICSIEMVLGCKGappYV-IHGPPGTGKTMTLVEAIVQLYTtqRNARVLVCAPSNSAADHILEKLLClegvriKDN 475
Cdd:cd18041     2 LNKDQRQAIKKVLNAKD---YAlILGMPGTGKTTTIAALVRILVA--LGKSVLLTSYTHSAVDNILLKLKK------FGV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  476 EIFRLNAATRsyeeIKPEIIRFCfFDELIFKCPPLKALTRY----KLVVSTYMSaslLNAEGVNRGHFTHILLDEAGQAS 551
Cdd:cd18041    71 NFLRLGRLKK----IHPDVQEFT-LEAILKSCKSVEELESKyesvSVVATTCLG---INHPIFRRRTFDYCIVDEASQIT 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332189722  552 EPENMIAVSnLCLTetvVVLAGDPRQLGPVIYSRDAESLGLGKSYLERLfecdyyCEGDENYVTKLVKNYR 622
Cdd:cd18041   143 LPICLGPLR-LAKK---FVLVGDHYQLPPLVKSREARELGMDESLFKRL------SEAHPDAVVQLTIQYR 203
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
 396-603 4.29e-24

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: 101.89  E-value: 4.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  396 ALNAEQICSIEMVLG----CKGAPPYVIHGPPGTGKTMTLVEAIVQLyTTQRNARVLVCAPSNSAAD-HILEKLLCLEGV 470
Cdd:cd18076     1 AGNNKQQLAFNFIAGkpseARFVPPLLIYGPFGTGKTFTLAMAALEV-IREPGTKVLICTHTNSAADiYIREYFHPYVDK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  471 RIKDNEIFRLNAATRSYEEIKPEIIRFCFF--DELIFKCPPLKALTRYKLVVSTYMSASLLNaegVNRGHFTHILLDEAG 548
Cdd:cd18076    80 GHPEARPLRIKATDRPNAITDPDTITYCCLtkDRQCFRLPTRDELDFHNIVITTTAMAFNLH---VLSGFFTHIFIDEAA 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 332189722  549 QASEPENMIAVSnLCLTETVVVLAGDPRQLGPVIYSRDaESLGLGKSYLERLFEC 603
Cdd:cd18076   157 QMLECEALIPLS-YAGPKTRVVLAGDHMQMTPKLFSVA-DYNRANHTLLNRLFHY 209
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
 397-605 6.52e-24

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: 101.14  E-value: 6.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  397 LNAEQICSIEMVLgcKGAPPYV-IHGPPGTGKTMTLVEAIVQLYTTQRNA-----------------------RVLVCAP 452
Cdd:cd18042     1 LNESQLEAIASAL--QNSPGITlIQGPPGTGKTKTIVGILSVLLAGKYRKyyekvkkklrklqrnlnnkkkknRILVCAP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  453 SNSAADHILEKLLcLEGVRIKDNEIFRLNAATRSYEEIKPEIIRfcffdelifkcpplKAltryKLVVSTYMSA--SLLN 530
Cdd:cd18042    79 SNAAVDEIVLRLL-SEGFLDGDGRSYKPNVVRVGRQELRASILN--------------EA----DIVCTTLSSSgsDLLE 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332189722  531 AEGvnrGHFTHILLDEAGQASEPENMIAVSNLCLTetvVVLAGDPRQLGPVIYSRDAESLGLGKSYLERLFECDY 605
Cdd:cd18042   140 SLP---RGFDTVIIDEAAQAVELSTLIPLRLGCKR---LILVGDPKQLPATVFSKVAQKLGYDRSLFERLQLAGY 208
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 419-585 1.64e-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: 92.02  E-value: 1.64e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   419 IHGPPGTGKTMTLVEAIVQLYTTQRNA-----RVLVCAPSNSAADHILEKLL-CLEG-----VRI--------------- 472
Cdd:pfam13086   18 IQGPPGTGKTTTIVELIRQLLSYPATSaaagpRILVCAPSNAAVDNILERLLrKGQKygpkiVRIghpaaiseavlpvsl 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   473 ---------------KDNEIFRLNAATRSYEEIKPEIIRFCFFDELIFKCPPLKALTRYKL------------------- 518
Cdd:pfam13086   98 dylvesklnneedaqIVKDISKELEKLAKALRAFEKEIIVEKLLKSRNKDKSKLEQERRKLrserkelrkelrrreqsle 177

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332189722   519 ---------VVSTYMSA---SLLNAEGvnrghFTHILLDEAGQASEPENMIAVSNLClteTVVVLAGDPRQLGPVIYSR 585
Cdd:pfam13086  178 reildeaqiVCSTLSGAgsrLLSSLAN-----FDVVIIDEAAQALEPSTLIPLLRGP---KKVVLVGDPKQLPPTVISK 248
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
 418-622 6.50e-20

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: 86.13  E-value: 6.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  418 VIHGPPGTGKTMTLVEAIVQLYTTQRNARVLVCAPSNSAADHIlekllclegvrikdneifrlnaatrsyeeikpeiirf 497
Cdd:cd17934     3 LIQGPPGTGKTTTIAAIVLQLLKGLRGKRVLVTAQSNVAVDNV------------------------------------- 45

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  498 cffdelifkcpplkaltryklvvstymsasllnaegvnrghfTHILLDEAGQASEPENMIAVSNLclteTVVVLAGDPRQ 577
Cdd:cd17934    46 ------------------------------------------DVVIIDEASQITEPELLIALIRA----KKVVLVGDPKQ 79

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 332189722  578 LGPVIYSRDAESLGLGKSYLERLFECDYYCEGDenyVTKLVKNYR 622
Cdd:cd17934    80 LPPVVQEDHAALLGLSFILSLLLLFRLLLPGSP---KVMLDTQYR 121
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
 397-602 5.81e-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: 5.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  397 LNAEQICSIEMVLGCkgaPPYVIHGPPGTGKTMTLVEAIVQLYTTQRNAR-----------VLVCAPSNSAAD---HILE 462
Cdd:cd18040     2 LNPSQNHAVRTALTK---PFTLIQGPPGTGKTVTGVHIAYWFAKQNREIQsvsgegdggpcVLYCGPSNKSVDvvaELLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  463 KLLCLEGVRIKDNEIFRL---------NAATRSYEEIKPE----------IIR---------FCFFDELIfkcpplkALT 514
Cdd:cd18040    79 KVPGLKILRVYSEQIETTeypipneprHPNKKSERESKPNselssitlhhRIRqpsnphsqqIKAFEARF-------ERT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  515 RYKLV---VSTYMSasLLNAEGVNRGHFTHILL----------------------DEAGQASEPENMIAVSNLCLTETVV 569
Cdd:cd18040   152 QEKITeedIKTYKI--LIWEARFEELETVDVILctcseaasqkmrthanvkqcivDECGMCTEPESLIPIVSAPRAEQVV 229

                         250       260       270
                  ....*....|....*....|....*....|...
gi 332189722  570 vLAGDPRQLGPVIYSRDAESLGLGKSYLERLFE 602
Cdd:cd18040   230 -LIGDHKQLRPVVQNKEAQKLGLGRSLFERYAE 261
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
 397-602 3.89e-11

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: 62.95  E-value: 3.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  397 LNAEQICSIEMVLGCKGAppyVIHGPPGTGKTMT---LVEAIVQLYTTQRNARVLVCAPSNSAADHILEKLLclegvRIK 473
Cdd:cd17936     2 LDPSQLEALKHALTSELA---LIQGPPGTGKTFLgvkLVRALLQNQDLSITGPILVVCYTNHALDQFLEGLL-----DFG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  474 DNEIFRLNAatrsyeeikpEIIrfcffdelifkcpplkALTryklvvSTY--MSASLLNAEGvnrghFTHILLDEAGQAS 551
Cdd:cd17936    74 PTKIVRLGA----------RVI----------------GMT------TTGaaKYRELLQALG-----PKVVIVEEAAEVL 116

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 332189722  552 EPeNMIAvsnlCLTETV--VVLAGDPRQLGPVI--YSRDAESLGLGKSYLERLFE 602
Cdd:cd17936   117 EA-HILA----ALTPSTehLILIGDHKQLRPKVnvYELTAKKYNLDVSLFERLVK 166
CoV_Nsp13-helicase cd21718
helicase domain of coronavirus non-structural protein 13; This model represents the helicase ...
 419-792 4.06e-10

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: 62.55  E-value: 4.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  419 IHGPPGTGKTmTLVEAIVQLYTtqrNARVLVCAPSNSAADHILEKLL-------------------CLEGVRIKDNEIFR 479
Cdd:cd21718    30 VQGPPGTGKS-HFAIGLALYYP---GARIVYTACSHAAVDALCEKASkwlpndkcsrivpqrarveCFDGFKVNNTNAQY 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  480 LNAATRSYEEIKPEIIrfcFFDELifkcpplKALTRYKLvvstymsaSLLNAegvnRGHFTHIlldeagqasepenmiav 559
Cdd:cd21718   106 IFSTINALPECSADIV---VVDEV-------SMCTNYDL--------SVVNA----RLKYKHI----------------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  560 snlcltetvvVLAGDPRQLgpviysrDAESLGLGKSYLErlfecdyycEGDENYVTKLVKN----------YRCHPEILD 629
Cdd:cd21718   147 ----------VYVGDPAQL-------PAPRTLLTEGSLE---------PKDYNVVTRLMVGsgpdvflskcYRCPKEIVD 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  630 LPSKLFYDGELVASKEDTDSVlaslnflpnkeFPMVFYGIQGCDeregnNPSWFNRIEISKVIETIKRLTANDcvqeeDI 709
Cdd:cd21718   201 TVSKLVYDNKLKAIKPKSRQC-----------FKTFGKGDVRHD-----NGSAINRPQLEFVKRFLDRNPRWR-----KA 259

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  710 GVITPYRQQVMKIKEVLDrldmteVKVGSVEQFQGQEKQVIIIsTVRSTIKHNefdrayclgflSNPRRFNVAITRA-IS 788
Cdd:cd21718   260 VFISPYNAMNNRASRLLG------LSTQTVDSSQGSEYDYVIF-CQTTDTAHA-----------LNINRFNVAITRAkHG 321


                  ....
gi 332189722  789 LLVI 792
Cdd:cd21718   322 ILVI 325
betaCoV_Nsp13-helicase cd21722
helicase domain of betacoronavirus non-structural protein 13; This model represents the ...
 419-786 5.00e-09

helicase domain of betacoronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from betacoronavirus, 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: 409655 [Multi-domain]  Cd Length: 340  Bit Score: 59.04  E-value: 5.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  419 IHGPPGTGKTMTLVEAIVQLYTtqrnARVLVCAPSNSAADHILEKLLclegvrikdnEIFRLNAATRsyeeIKPEIIRFC 498
Cdd:cd21722    30 VQGPPGTGKSHLAIGLAVYYPT----ARVVYTACSHAAVDALCEKAF----------KFLNINKCSR----IIPAKARVE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  499 FFDEliFKCPPlkalTRYKLVVSTymsaslLNA--EGVnrghfTHILL-DEAGQASEPEnmIAVSNLCLTETVVVLAGDP 575
Cdd:cd21722    92 CYDK--FKVND----TSRQYVFST------INAlpETV-----TDILVvDEVSMCTNYD--LSVINARVRAKHIVYIGDP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  576 RQLgpviysrDAESLGLGKSYLE-RLFecdyycegdeNYVTKLVKN----------YRCHPEILDLPSKLFYDGELVASK 644
Cdd:cd21722   153 AQL-------PAPRTLLTKGTLEpEYF----------NSVTRLMCClgpdiflgtcYRCPKEIVDTVSALVYDNKLKAKK 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  645 EDTDSVlaslnflpnkeFPMVFYGIQGCDeregnNPSWFNRIEISKVIETIKRLTA-NDCVqeedigVITPYRQQVMKIK 723
Cdd:cd21722   216 DNSGQC-----------FKVYYKGSVTHD-----SSSAINRPQIYLVKKFLKANPAwSKAV------FISPYNSQNAVAR 273

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332189722  724 EVLDrldmteVKVGSVEQFQGQEKQVIIISTVRSTIKHNefdrayclgflsNPRRFNVAITRA 786
Cdd:cd21722   274 RVLG------LQTQTVDSSQGSEYDYVIYCQTAETAHSV------------NVNRFNVAITRA 318
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 390-581 1.05e-08

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: 58.83  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  390 FVPISPALNAEQICSIEMVLgcKGAPPYVIHGPPGTGKTmTLVEAIVQLYtTQRNARVLVCAPSNSAADHiLEKLLCLEG 469
Cdd:COG0507   118 EPRAGITLSDEQREAVALAL--TTRRVSVLTGGAGTGKT-TTLRALLAAL-EALGLRVALAAPTGKAAKR-LSESTGIEA 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  470 V-------RIKDNEIFRLNAAtrsyeeikpeiirfcffdelifkcpplKALTRYKLVVstymsasllnaegvnrghfthi 542
Cdd:COG0507   193 RtihrllgLRPDSGRFRHNRD---------------------------NPLTPADLLV---------------------- 223

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 332189722  543 lLDEAGQASEPenMIA--VSNLCLTETVVVLAGDPRQLGPV 581
Cdd:COG0507   224 -VDEASMVDTR--LMAalLEALPRAGARLILVGDPDQLPSV 261
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 396-581 1.72e-08

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


Pssm-ID: 433343 [Multi-domain]  Cd Length: 191  Bit Score: 55.26  E-value: 1.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   396 ALNAEQICSIEMVLGcKGAPPYVIHGPPGTGKTmTLVEAIVQLYtTQRNARVLVCAPSNSAADhilekllclegvrikdn 475
Cdd:pfam13604    1 TLNAEQAAAVRALLT-SGDRVAVLVGPAGTGKT-TALKALREAW-EAAGYRVIGLAPTGRAAK----------------- 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   476 eifRLNAATrsyeeikpeiirfcffdelifkcpPLKALTRYKLVVSTYMSASLLNAEGVnrghfthiLLDEAGQASEPEn 555
Cdd:pfam13604   61 ---VLGEEL------------------------GIPADTIAKLLHRLGGRAGLDPGTLL--------IVDEAGMVGTRQ- 104

                          170       180
                   ....*....|....*....|....*..
gi 332189722   556 MIAVSNLCLTE-TVVVLAGDPRQLGPV 581
Cdd:pfam13604  105 MARLLKLAEDAgARVILVGDPRQLPSV 131
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
 418-582 2.40e-08

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: 55.51  E-value: 2.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  418 VIHGPPGTGKTMTLVEAIVQLYTTQRNARVLVCAPSNSAADHILEKllcLEGVRIKDNEIFRLNAATRsyeeikpeiirf 497
Cdd:cd17935    24 MVVGPPGTGKTDVAVQIISNLYHNFPNQRTLIVTHSNQALNQLFEK---IMALDIDERHLLRLGHGAK------------ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  498 cffdelifkcpplkaltrykLVVSTYMSASLLNAEGVNRG-HFTHILLDEAGQASEPENMIAVSnLCLTETV------VV 570
Cdd:cd17935    89 --------------------IIAMTCTHAALKRGELVELGfKYDNILMEEAAQILEIETFIPLL-LQNPEDGpnrlkrLI 147

                         170
                  ....*....|..
gi 332189722  571 LAGDPRQLGPVI 582
Cdd:cd17935   148 MIGDHHQLPPVI 159
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
 708-794 4.01e-08

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: 51.67  E-value: 4.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  708 DIGVITPYRQQVMKIKEVL-----DRLDMTEVKVGSVEQFQGQEKQVIIISTVRStikhnefdrayclgFLSNPRRFNVA 782
Cdd:cd18786    12 KGVVLTPYHRDRAYLNQYLqglslDEFDLQLVGAITIDSSQGLTFDVVTLYLPTA--------------NSLTPRRLYVA 77

                          90
                  ....*....|..
gi 332189722  783 ITRAISLLVIIG 794
Cdd:cd18786    78 LTRARKRLVIYD 89
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 400-581 7.47e-08

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: 52.56  E-value: 7.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  400 EQICSIEMVLGCKGAppyVIHGPPGTGKTmTLVEAIVQLYtTQRNARVLVCAPSNSAADHiLEKLLCLEGVRIKdneifr 479
Cdd:cd17933     1 EQKAAVRLVLRNRVS---VLTGGAGTGKT-TTLKALLAAL-EAEGKRVVLAAPTGKAAKR-LSESTGIEASTIH------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  480 lnaatrSYEEIKPEIIRFCFFDELIFKCpplkaltryKLVVstymsasllnaegvnrghfthilLDEAGqasepenMIAV 559
Cdd:cd17933    69 ------RLLGINPGGGGFYYNEENPLDA---------DLLI-----------------------VDEAS-------MVDT 103

                         170       180
                  ....*....|....*....|....*...
gi 332189722  560 SNLC-LTETV-----VVLAGDPRQLGPV 581
Cdd:cd17933   104 RLMAaLLSAIpagarLILVGDPDQLPSV 131
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
 418-583 1.07e-07

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: 51.43  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  418 VIHGPPGTGKTMTLVEAIVQLYTTQRnaRVLVCApsnsaadhilEKLLCLEGVRikdneifrlnaatrsyeeiKPEIIrf 497
Cdd:cd18043    18 VIQGPPGTGKSQTIANIIANALARGK--RVLFVS----------EKKAALDVVR-------------------FPCWI-- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  498 cffdelifkCPPLKAltryklvvstymsASLLNAegvNRGHFTHILLDEAGQASEPEnmiAVSNLCLTETVVVlAGDPRQ 577
Cdd:cd18043    65 ---------MSPLSV-------------SQYLPL---NRNLFDLVIFDEASQIPIEE---ALPALFRGKQVVV-VGDDKQ 115


                  ....*.
gi 332189722  578 LGPVIY 583
Cdd:cd18043   116 LPPSIL 121
DEXDc smart00487
DEAD-like helicases superfamily;
418-547 5.32e-07

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 51.34  E-value: 5.32e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722    418 VIHGPPGTGKTMTLVEAIVQLYTTQRNARVLVCAPSNSAADHILEKLLclegvriKDNEIFRLNAATRSYEEIKPEIIRF 497
Cdd:smart00487   28 ILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELK-------KLGPSLGLKVVGLYGGDSKREQLRK 100

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 332189722    498 CffdelifkcpplkALTRYKLVVSTYMSA-SLLNAEGVNRGHFTHILLDEA 547
Cdd:smart00487  101 L-------------ESGKTDILVTTPGRLlDLLENDKLSLSNVDLVILDEA 138
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 397-547 2.10e-06

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 48.46  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  397 LNAEQICSIEMVLGCKGAPPYVIHGPPGTGKTMTLVEAIVQLYttqrNARVLVCAPSnsaaDHILEKllclegvrIKDNe 476
Cdd:cd17926     1 LRPYQEEALEAWLAHKNNRRGILVLPTGSGKTLTALALIAYLK----ELRTLIVVPT----DALLDQ--------WKER- 63

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332189722  477 IFRLNAATRSYeeikpeiirfcffdelIFKCPPLKALTRYKLVVSTYMSASLLNAEGVNRGH-FTHILLDEA 547
Cdd:cd17926    64 FEDFLGDSSIG----------------LIGGGKKKDFDDANVVVATYQSLSNLAEEEKDLFDqFGLLIVDEA 119
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
 352-662 2.64e-06

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


Pssm-ID: 273631 [Multi-domain]  Cd Length: 582  Bit Score: 51.30  E-value: 2.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   352 NRINTRRLYQavDAAEMLdpNFLFPSLHSGKRMIKTKPFVPISPALNAEQICSIEMVLGCKGaPPYVIHGPPGTGKTMTL 431
Cdd:TIGR01447  102 GRLYLRRYWR--EEEKLA--AKLRTLLEARKRTAPSAILENLFPLLNEQNWRKTAVALALKS-NFSLITGGPGTGKTTTV 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   432 VEAIVQLYTTQRNA---RVLVCAPSNSAADHILEKLlclegvrikDNEIFRLNAAtrsyeeikpeiirfcffdELIFKCP 508
Cdd:TIGR01447  177 ARLLLALVKQSPKQgklRIALAAPTGKAAARLAESL---------RKAVKNLAAA------------------EALIAAL 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   509 PLKALTRYKLVVSTYMSASLLNAEGvNRGHFTHILLDEAgqasepeNMIAVSNLC-LTETV-----VVLAGDPRQLGPV- 581
Cdd:TIGR01447  230 PSEAVTIHRLLGIKPDTKRFRHHER-NPLPLDVLVVDEA-------SMVDLPLMAkLLKALppntkLILLGDKNQLPSVe 301

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   582 ---IYSR--DAESLGLGKSYLERLFECDYYCEGDENYVTKLVKNYRC-HPEILDLPSKLFYDGelvaskeDTDSVLASLN 655
Cdd:TIGR01447  302 agaVLGDlcELASIGKSILYALCKKINSKTRNPLSDNVCFLKTSHRFgKDSGIGQLAKAINSG-------DIEAVLNNLR 374


                   ....*..
gi 332189722   656 FLPNKEF 662
Cdd:TIGR01447  375 SGQLIEF 381
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
 418-458 4.64e-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: 46.71  E-value: 4.64e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 332189722  418 VIHGPPGTGKTMTLVEAIVQLYTTQR--NARVLVCAPSNSAAD 458
Cdd:cd17914     3 LIQGPPGTGKTRVLVKIVAALMQNKNgePGRILLVTPTNKAAA 45
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 815-962 9.25e-06

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 49.61  E-value: 9.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  815 NNAYQGCGLPEQEEFVEEPFKQEGSSNG-----PQYPPEAEWNNSGELNNGGANENGEWSDGWNNNGGTKEKNEWSDGWN 889
Cdd:cd21118   196 NNQNSGCTNPPPSGSHESFSNSGGSSSSgssgsQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGS 275

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332189722  890 SNGGGTkkkDEWSDGWDNNGGTNGINQEGSSNAPqdpqeaEWN----DSGEVKNGGTKEKDVRSDGWNNNGGKNEKE 962
Cdd:cd21118   276 GSGGSS---SGGSNGWGGSSSSGGSGGSGGGNKP------ECNnpgnDVRMAGGGGSQGSKESSGSHGSNGGNGQAE 343
SF1_C_UvrD cd18807
C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase ...
 687-794 2.82e-05

C-terminal helicase domain of UvrD family helicases; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. This family also includes ATP-dependent helicase/nuclease AddA and helicase/nuclease RecBCD subunit RecB, among others. UvrD family helicases 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: 350194 [Multi-domain]  Cd Length: 150  Bit Score: 45.30  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  687 EISKVIETIKRLTANDCVQEEDIGVITPYRQQVMKIKEVLdrldmtEVKVGSVEQFQGQE-KQVIIISTVRSTIKHNEFD 765
Cdd:cd18807    45 EAKAIADEIKRLIESGPVQYSDIAILVRTNRQARVIEEAL------RVTLMTIHASKGLEfPVVFIVGLGEGFIPSDASY 118

                          90       100       110
                  ....*....|....*....|....*....|..
gi 332189722  766 RAYCLGF--LSNPRR-FNVAITRAISLLVIIG 794
Cdd:cd18807   119 HAAKEDEerLEEERRlLYVALTRAKKELYLVG 150
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
412-547 7.53e-05

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 46.56  E-value: 7.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  412 KGAPPYVIHGPPGTGKTMTLVEAIVQLYttqRNARVLVCAPSnsaaDHILEKLLclegvrikdneifrlnaatRSYEEIK 491
Cdd:COG1061    98 RGGGRGLVVAPTGTGKTVLALALAAELL---RGKRVLVLVPR----RELLEQWA-------------------EELRRFL 151

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 332189722  492 PEIIRFCFFDELifkcpplkaltRYKLVVSTYMSASLLNAEGVNRGHFTHILLDEA 547
Cdd:COG1061   152 GDPLAGGGKKDS-----------DAPITVATYQSLARRAHLDELGDRFGLVIIDEA 196
AAA_19 pfam13245
AAA domain;
414-465 9.14e-05

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 43.36  E-value: 9.14e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 332189722   414 APPYVIHGPPGTGKTMTLVeAIVQLY--TTQRNARVLVCAPSNSAADHILEKLL 465
Cdd:pfam13245   11 SKVVLLTGGPGTGKTTTIR-HIVALLvaLGGVSFPILLAAPTGRAAKRLSERTG 63
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 416-503 1.20e-04

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 43.52  E-value: 1.20e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722    416 PYVIHGPPGTGKTmTLVEAIVQLYtTQRNARVLVCAPSNSAADHILEKLLCLEGVRIKDNEIF-RLNAATRSYEEIKPEI 494
Cdd:smart00382    4 VILIVGPPGSGKT-TLARALAREL-GPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGElRLRLALALARKLKPDV 81


                    ....*....
gi 332189722    495 IrfcFFDEL 503
Cdd:smart00382   82 L---ILDEI 87
DEXQc_UvrD cd17932
DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch ...
 398-588 2.98e-04

DEXQD-box helicase domain of UvrD; UvrD is a highly conserved helicase involved in mismatch repair, nucleotide excision repair, and recombinational repair. It plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species including Helicobacter pylori and Escherichia coli. UvrD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350690 [Multi-domain]  Cd Length: 189  Bit Score: 42.89  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  398 NAEQICSIEmvlgCKGAPPYVIHGPpGTGKTMTLVEAIVQLYTTQRNA--RVLVCAPSNSAADHILEKLlcleGVRIKDN 475
Cdd:cd17932     1 NPEQREAVT----HPDGPLLVLAGA-GSGKTRVLTHRIAYLILEGGVPpeRILAVTFTNKAAKEMRERL----RKLLGEQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  476 EIFRLNAATrsyeeikpeIIRFCF--------FDELIFKCppLKALTRYKLVVSTYmsasllnaegvnRGHFTHILLDEA 547
Cdd:cd17932    72 LASGVWIGT---------FHSFALrilrrygdFDDLLLYA--LELLEENPDVREKL------------QSRFRYILVDEY 128

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 332189722  548 GQASEPENMIaVSNLCLTETVVVLAGDPRQlgpVIYS-RDAE 588
Cdd:cd17932   129 QDTNPLQYEL-LKLLAGDGKNLFVVGDDDQ---SIYGfRGAD 166
RecB COG1074
3#-5# helicase subunit RecB of the DNA repair enzyme RecBCD (exonuclease V) [Replication, ...
 480-730 1.00e-03

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


Pssm-ID: 440692 [Multi-domain]  Cd Length: 866  Bit Score: 43.03  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  480 LNAATRSYEEIKpEIIRFCFFDELIFKCppLKALT-------RYKLvvstymsasllnaegvnRGHFTHILLDEA----- 547
Cdd:COG1074   239 LAAVLARYERRK-RERGLLDFDDLLHRA--LRLLRdedapwvAERL-----------------RERYRHILVDEFqdtsp 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  548 -----------GQASEPENMIAVsnlcltetvvvlaGDPRQlgpVIYS-RDAEsLGLgksYLERlfeCDYYCEGDENYVT 615
Cdd:COG1074   299 lqweilrrlagEALADGRTLFLV-------------GDPKQ---SIYRfRGAD-PEL---FLEA---RRALEGRVDGERL 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  616 KLVKNYRCHPEILD--------LPSKLFYDGELVASKEDTDSVLASLNFLPnkefpmvfygiqgCDEREGNNPSWfNRIE 687
Cdd:COG1074   356 TLTTNFRSTPEVVDavnalfaqLMGAGFGEIPYEPVEALRPGAYPAVELWP-------------LEPDDVSEEDA-RERE 421

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 332189722  688 ISKVIETIKRLTANDC--------VQEEDIGVITPYRQQVMKIKEVLDRLD 730
Cdd:COG1074   422 ARAVAARIRRLLAEGTtvegggrpVRPGDIAVLVRTRSEAAAIARALKAAG 472
alphaCoV_Nsp13-helicase cd21723
helicase domain of alphacoronavirus non-structural protein 13; This model represents the ...
 419-786 1.36e-03

helicase domain of alphacoronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from alphacoronavirus, including Porcine epidemic diarrhea virus and Human coronavirus (CoV) NL63. 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: 409656 [Multi-domain]  Cd Length: 340  Bit Score: 42.03  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  419 IHGPPGTGKTMTLVEaiVQLYTTqrNARVLVCAPSNSAADHileklLClegvrIKDNEIFRLNAATRsyeeIKPEIIRFC 498
Cdd:cd21723    30 IQGPPGSGKSHCVIG--LGLYYP--GARIVFTACSHAAVDS-----LC-----VKAATAYSVDKCSR----IIPARARVE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  499 FFDEliFKCPPLKAltryKLVVSTYMSASLLNAEGVnrghfthiLLDEAGQASEPEnmIAVSNLCLTETVVVLAGDPRQL 578
Cdd:cd21723    92 CYDG--FKPNNTSA----QYIFSTVNALPECNADIV--------VVDEVSMCTNYD--LSVINQRVSYKHIVYVGDPQQL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  579 gpviysrDAESLGLGKSYLErlfecdyycEGDENYVTK----------LVKNYRCHPEILDLPSKLFYDGELVASKEDTd 648
Cdd:cd21723   156 -------PAPRTMITRGVLE---------PKDYNVVTQrmcalgpdvfLHKCYRCPAEIVNTVSELVYENKFKPVHPES- 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  649 svlaslnflpNKEFPMVFYGIQGCDeregnNPSWFNRieisKVIETIKRLTANDCVQEEDIgVITPYRQQVMKIKEVLDr 728
Cdd:cd21723   219 ----------KQCFKIFCKGNVQVD-----NGSSINR----RQLDVVKMFLAKNPKWSKAV-FISPYNSQNYVASRVLG- 277

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 332189722  729 ldmteVKVGSVEQFQGQEKQVIIIsTVRSTIKHnefdrayclgfLSNPRRFNVAITRA 786
Cdd:cd21723   278 -----LQIQTVDSSQGSEYDYVIY-TQTSDTAH-----------ACNVNRFNVAITRA 318
AAA_22 pfam13401
AAA domain;
413-465 1.54e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.63  E-value: 1.54e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 332189722   413 GAPPYVIHGPPGTGKTMTLvEAIVQLYTTQRNARVLVCAPSNSAADHILEKLL 465
Cdd:pfam13401    4 GAGILVLTGESGTGKTTLL-RRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALL 55
ResIII pfam04851
Type III restriction enzyme, res subunit;
412-547 1.67e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 40.35  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722   412 KGAPPYVIHGPPGTGKTMTLVEAIVQLYTTQRNARVLVCAPSNSaadhILEKLLclegvrikdneifrlnaatRSYEEIK 491
Cdd:pfam04851   21 NGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKD----LLEQAL-------------------EEFKKFL 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332189722   492 PEIIRFCFF---DELIFKcpplkaLTRYKLVVSTYMSASLLNAEGVNR---GHFTHILLDEA 547
Cdd:pfam04851   78 PNYVEIGEIisgDKKDES------VDDNKIVVTTIQSLYKALELASLEllpDFFDVIIIDEA 133
recD PRK10875
exodeoxyribonuclease V subunit alpha;
418-464 4.26e-03

exodeoxyribonuclease V subunit alpha;


Pssm-ID: 236783 [Multi-domain]  Cd Length: 615  Bit Score: 41.08  E-value: 4.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 332189722  418 VIHGPPGTGKTMT---LVEAIVQLYTTQRnARVLVCAPSNSAADHILEKL 464
Cdd:PRK10875  171 VISGGPGTGKTTTvakLLAALIQLADGER-CRIRLAAPTGKAAARLTESL 219
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 411-476 5.45e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 38.64  E-value: 5.45e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332189722   411 CKGAPPYV-IHGPPGTGKTmTLVEAIVQLYTTQRNARVLVCAPSNSAADHILEKLLCLEGVRIKDNE 476
Cdd:pfam13191   20 RSGRPPSVlLTGEAGTGKT-TLLRELLRALERDGGYFLRGKCDENLPYSPLLEALTREGLLRQLLDE 85
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 415-503 6.96e-03

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 38.28  E-value: 6.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332189722  415 PPYVIHGPPGTGKTmTLVEAIVQlYTTQRNARVLVcapSNSAADHILEKLLCLEGVRIKDNEIFRLNAAtrsyeeiKPEI 494
Cdd:cd00009    20 KNLLLYGPPGTGKT-TLARAIAN-ELFRPGAPFLY---LNASDLLEGLVVAELFGHFLVRLLFELAEKA-------KPGV 87


                  ....*....
gi 332189722  495 IrfcFFDEL 503
Cdd:cd00009    88 L---FIDEI 93
 
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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