NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18859757|ref|NP_572767|]
View 

Upf1 RNA helicase, isoform A [Drosophila melanogaster]

Protein Classification

UPF1 family DEAD/DEAH box RNA helicase( domain architecture ID 18245197)

UPF1 family DEAD/DEAH box containing ATP-dependent RNA helicase catalyzes the unwinding of RNA; similar to regulator of nonsense transcripts 1, an RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
451-684 1.49e-165

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: 489.45  E-value: 1.49e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  451 DLNRSQVYAVKHALQRPLSLIQGPPGTGKTVTSATIVYQLVKLHGGTVLVCAPSNTAVDQLTEKIHRTNLKVVRVCAKSR 530
Cdd:cd18039    1 ELNHSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVDQLTEKIHQTGLKVVRLCAKSR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  531 EAIDSPVSFLALHNQIRNMETNSELKKLQQLKDETGELSSADEKRYRNLKRAAENQLLEAADVICCTCVGAGDGRLSRVK 610
Cdd:cd18039   81 EAVESPVSFLALHNQVRNLDSAEKLELLKLLKLETGELSSADEKRYRKLKRKAERELLRNADVICCTCVGAGDPRLSKMK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859757  611 FTSILIDESMQSTEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAARAGLSQSLFERLVVLGIRPFRLEVQYR 684
Cdd:cd18039  161 FRTVLIDEATQATEPECLIPLVHGAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVQLGIRPIRLQVQYR 234
UPF1_Zn_bind pfam09416
RNA helicase (UPF2 interacting domain); UPF1 is an essential RNA helicase that detects mRNAs ...
98-249 3.33e-107

RNA helicase (UPF2 interacting domain); UPF1 is an essential RNA helicase that detects mRNAs containing premature stop codons and triggers their degradation. This domain contains 3 zinc binding motifs and forms interactions with another protein (UPF2) that is also involved nonsense-mediated mRNA decay (NMD).


:

Pssm-ID: 401391  Cd Length: 152  Bit Score: 332.68  E-value: 3.33e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757     98 HACKYCGIHDPATVVMCNNCRKWFCNGRGSTSGSHIINHLVRAKHREVTLHGEGPLGETILECYSCGVRNVFVLGFIPAK 177
Cdd:pfam09416    1 HACAYCGIHDPACVVKCLTCGKWFCNGRGNTSGSHIINHLVRSKHKEVSLHPDSPLGDTVLECYNCGSKNVFLLGFIPAK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18859757    178 ADSVVVLLCRQPCAAQNSLKDMNWDQEQWKPLIADRCFLAWLVKQPSEQGQLRARQISAAQINKLEELWKEN 249
Cdd:pfam09416   81 SDSVVVLLCRQPCAQAKSLKDMNWDTSQWQPLIEDRQFLPWLVKVPSEEEQLRARQITPAQINKLEELWKDN 152
TIGR00376 super family cl36628
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
355-880 3.27e-87

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


The actual alignment was detected with superfamily member TIGR00376:

Pssm-ID: 273041 [Multi-domain]  Cd Length: 636  Bit Score: 295.96  E-value: 3.27e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    355 GHVIKVPDNFgddVGLELKSSTnaPVKCTSNFTVDFIWKCTSFDRMTRALCKFAIDRNSVSNFIYSRLLGHGRADSNDEV 434
Cdd:TIGR00376   78 GVVTRVGKRF---ITVALEESV--PQWSLKRVRIDLYANDVTFKRMKEALRALTENHSRLLEFLLGREAPSKASEIHDFQ 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    435 LFRgpqpklfsaphlPDLNRSQVYAVKHAL-QRPLSLIQGPPGTGKTVTSATIVYQLVKlHGGTVLVCAPSNTAVDQLTE 513
Cdd:TIGR00376  153 FFD------------PNLNESQKEAVLFALsSKDLFLIHGPPGTGKTRTVVELIRQLVK-RGLRVLVTAPSNIAVDNLLE 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    514 KIHRTNLKVVRVCAKSR--------------EAIDSPVSFLALHNQIRNM--ETNSELKKLQQLK---DETGELSSADEK 574
Cdd:TIGR00376  220 RLALCDQKIVRLGHPARllksnkqhsldyliENHPKYQIVADIREKIDELieERNKKTKPSPQKRrglSDIKILRKALKK 299
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    575 R--------------------------YRNLKRAAENQLLEAADVICCTCVGAGDGRLSRVKFTSILIDESMQSTEPECM 628
Cdd:TIGR00376  300 ReargieslkiasmaewietnksidrlLKLLPESEERIMNEILAESDATNSMAGSEILNGQYFDVAVIDEASQAMEPSCL 379
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    629 VPVVlGAKQLILVGDHCQLGPVVMCKKAAraGLSQSLFERLVVL-GIRPFRLEVQYRMHPELSQFPSNFFYEGSLQNGVC 707
Cdd:TIGR00376  380 IPLL-KARKLILAGDHKQLPPTILSHDAE--ELSLTLFERLIKEyPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHES 456
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    708 AEDRRLkLDFPWPQPER---------PMFFLVTQGQE----EIAGSgTSFLNRTEAANVEKITTRFLKAGIKPEQIGIIT 774
Cdd:TIGR00376  457 VANILL-RDLPKVEATEseddletgiPLLFIDTSGCElfelKEADS-TSKYNPGEAELVSEIIQALVKMGVPANDIGVIT 534
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    775 PYEGQRAYLVQYMQYQgslhsrlYQEIEIASVDAFQGREKDIIIMSCVRSNERQGIGFLNDPRRLNVALTRAKFGIIIVG 854
Cdd:TIGR00376  535 PYDAQVDLLRQLLEHR-------HIDIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIG 607
                          570       580
                   ....*....|....*....|....*.
gi 18859757    855 NPKVLAKQQLWNHLLNFYKDRKVLVE 880
Cdd:TIGR00376  608 DSRTLSNHKFYKRLIEWCKQHGEVRE 633
1B_UPF1-like cd21407
1B domain of eukaryotic UPF1 RNA helicase and related proteins; Helicases catalyze ...
302-390 2.20e-49

1B domain of eukaryotic UPF1 RNA helicase and related proteins; 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. UPF1 belongs to helicase superfamily 1 (SF1). It participates in nonsense-mediated mRNA decay (NMD), a pathway which degrades transcripts with premature termination codons. UPF1 is a multidomain protein; it includes an N-terminal Cys/His rich zinc-binding domain (CH/ZBD), a regulatory 1B domain, and a SF1 helicase core. The 1B domain is involved in nucleic acid substrate binding; the 1B domain of the related Equine arteritis virus (EAV) Nsp10 undergoes large conformational change upon substrate binding, and together with the 1A and 2A domains of the helicase core form a channel that accommodates the single stranded nucleic acids.


:

Pssm-ID: 394815  Cd Length: 90  Bit Score: 169.63  E-value: 2.20e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  302 TQENIEVRWDVGLNKKTIAYFTLAKTD-SDMKLMHGDELRLHYVGELYNPWSEIGHVIKVPDNFGDDVGLELKSSTNAPV 380
Cdd:cd21407    1 TQENISVRWDVGLNKKRLAYFTLPKLDeSELRLMVGDELRLRYKGDLREPWEGVGHVIKIPDNYSEEVALELRSSKNAPT 80
                         90
                 ....*....|
gi 18859757  381 KCTSNFTVDF 390
Cdd:cd21407   81 EITTGFSVEF 90
 
Name Accession Description Interval E-value
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
451-684 1.49e-165

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: 489.45  E-value: 1.49e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  451 DLNRSQVYAVKHALQRPLSLIQGPPGTGKTVTSATIVYQLVKLHGGTVLVCAPSNTAVDQLTEKIHRTNLKVVRVCAKSR 530
Cdd:cd18039    1 ELNHSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVDQLTEKIHQTGLKVVRLCAKSR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  531 EAIDSPVSFLALHNQIRNMETNSELKKLQQLKDETGELSSADEKRYRNLKRAAENQLLEAADVICCTCVGAGDGRLSRVK 610
Cdd:cd18039   81 EAVESPVSFLALHNQVRNLDSAEKLELLKLLKLETGELSSADEKRYRKLKRKAERELLRNADVICCTCVGAGDPRLSKMK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859757  611 FTSILIDESMQSTEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAARAGLSQSLFERLVVLGIRPFRLEVQYR 684
Cdd:cd18039  161 FRTVLIDEATQATEPECLIPLVHGAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVQLGIRPIRLQVQYR 234
UPF1_Zn_bind pfam09416
RNA helicase (UPF2 interacting domain); UPF1 is an essential RNA helicase that detects mRNAs ...
98-249 3.33e-107

RNA helicase (UPF2 interacting domain); UPF1 is an essential RNA helicase that detects mRNAs containing premature stop codons and triggers their degradation. This domain contains 3 zinc binding motifs and forms interactions with another protein (UPF2) that is also involved nonsense-mediated mRNA decay (NMD).


Pssm-ID: 401391  Cd Length: 152  Bit Score: 332.68  E-value: 3.33e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757     98 HACKYCGIHDPATVVMCNNCRKWFCNGRGSTSGSHIINHLVRAKHREVTLHGEGPLGETILECYSCGVRNVFVLGFIPAK 177
Cdd:pfam09416    1 HACAYCGIHDPACVVKCLTCGKWFCNGRGNTSGSHIINHLVRSKHKEVSLHPDSPLGDTVLECYNCGSKNVFLLGFIPAK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18859757    178 ADSVVVLLCRQPCAAQNSLKDMNWDQEQWKPLIADRCFLAWLVKQPSEQGQLRARQISAAQINKLEELWKEN 249
Cdd:pfam09416   81 SDSVVVLLCRQPCAQAKSLKDMNWDTSQWQPLIEDRQFLPWLVKVPSEEEQLRARQITPAQINKLEELWKDN 152
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
355-880 3.27e-87

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: 295.96  E-value: 3.27e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    355 GHVIKVPDNFgddVGLELKSSTnaPVKCTSNFTVDFIWKCTSFDRMTRALCKFAIDRNSVSNFIYSRLLGHGRADSNDEV 434
Cdd:TIGR00376   78 GVVTRVGKRF---ITVALEESV--PQWSLKRVRIDLYANDVTFKRMKEALRALTENHSRLLEFLLGREAPSKASEIHDFQ 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    435 LFRgpqpklfsaphlPDLNRSQVYAVKHAL-QRPLSLIQGPPGTGKTVTSATIVYQLVKlHGGTVLVCAPSNTAVDQLTE 513
Cdd:TIGR00376  153 FFD------------PNLNESQKEAVLFALsSKDLFLIHGPPGTGKTRTVVELIRQLVK-RGLRVLVTAPSNIAVDNLLE 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    514 KIHRTNLKVVRVCAKSR--------------EAIDSPVSFLALHNQIRNM--ETNSELKKLQQLK---DETGELSSADEK 574
Cdd:TIGR00376  220 RLALCDQKIVRLGHPARllksnkqhsldyliENHPKYQIVADIREKIDELieERNKKTKPSPQKRrglSDIKILRKALKK 299
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    575 R--------------------------YRNLKRAAENQLLEAADVICCTCVGAGDGRLSRVKFTSILIDESMQSTEPECM 628
Cdd:TIGR00376  300 ReargieslkiasmaewietnksidrlLKLLPESEERIMNEILAESDATNSMAGSEILNGQYFDVAVIDEASQAMEPSCL 379
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    629 VPVVlGAKQLILVGDHCQLGPVVMCKKAAraGLSQSLFERLVVL-GIRPFRLEVQYRMHPELSQFPSNFFYEGSLQNGVC 707
Cdd:TIGR00376  380 IPLL-KARKLILAGDHKQLPPTILSHDAE--ELSLTLFERLIKEyPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHES 456
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    708 AEDRRLkLDFPWPQPER---------PMFFLVTQGQE----EIAGSgTSFLNRTEAANVEKITTRFLKAGIKPEQIGIIT 774
Cdd:TIGR00376  457 VANILL-RDLPKVEATEseddletgiPLLFIDTSGCElfelKEADS-TSKYNPGEAELVSEIIQALVKMGVPANDIGVIT 534
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    775 PYEGQRAYLVQYMQYQgslhsrlYQEIEIASVDAFQGREKDIIIMSCVRSNERQGIGFLNDPRRLNVALTRAKFGIIIVG 854
Cdd:TIGR00376  535 PYDAQVDLLRQLLEHR-------HIDIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIG 607
                          570       580
                   ....*....|....*....|....*.
gi 18859757    855 NPKVLAKQQLWNHLLNFYKDRKVLVE 880
Cdd:TIGR00376  608 DSRTLSNHKFYKRLIEWCKQHGEVRE 633
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
661-857 3.73e-79

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: 257.86  E-value: 3.73e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    661 LSQSLFERLVVLG-IRPFRLEVQYRMHPELSQFPSNFFYEGSLQNGVCAEDRRLKLDFPWPQPERPMFFL-VTQGQEEIA 738
Cdd:pfam13087    1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDDFHLPDPLGPLVFIdVDGSEEEES 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    739 GSGTSFLNRTEAANVEKITTRFLKAGI-KPEQIGIITPYEGQRAYLVQYMQYQGSLHSrlyqEIEIASVDAFQGREKDII 817
Cdd:pfam13087   81 DGGTSYSNEAEAELVVQLVEKLIKSGPeEPSDIGVITPYRAQVRLIRKLLKRKLGGKL----EIEVNTVDGFQGREKDVI 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 18859757    818 IMSCVRSNERQGIGFLNDPRRLNVALTRAKFGIIIVGNPK 857
Cdd:pfam13087  157 IFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNAK 196
ZBD_UPF1-like cd21400
Cys/His rich zinc-binding domain (CH/ZBD) of eukaryotic UPF1 RNA helicase and related proteins; ...
99-219 1.04e-78

Cys/His rich zinc-binding domain (CH/ZBD) of eukaryotic UPF1 RNA helicase and related proteins; 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. UPF1 belongs to helicase superfamily 1 (SF1). The CH/ZBD has 3 zinc-finger (ZnF1-3) motifs. UPF1 participates in nonsense-mediated mRNA decay (NMD), a pathway which degrades transcripts with premature termination codons. The N-terminal CH/ZBD of UPF1 interacts with UPF2, a factor also involved in NMD. UPF1 has an N-terminal CH/ZBD, a 1B domain, and a SF1 helicase core.


Pssm-ID: 439167  Cd Length: 120  Bit Score: 253.71  E-value: 1.04e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757   99 ACKYCGIHDPATVVMCNNCRKWFCNGRGSTSGSHIINHLVRAKHREVTLHGEGPLGETILECYSCGVRNVFVLGFIPAKA 178
Cdd:cd21400    1 ACAYCGIHDPACLVKCLTCGKWFCNGRGNTSGSHIVQHLVRSKHKEVSLHPDSPLGDTVLECYNCGSRNVFLLGFIPAKA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 18859757  179 DSVVVLLCRQPCAAQNSlKDMNWDQEQWKPLIADRCFLAWL 219
Cdd:cd21400   81 DSVVVLLCRQPCLSQSS-KDMNWDLSQWQPLIDDRQFLPWL 120
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
685-873 1.61e-78

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: 255.62  E-value: 1.61e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  685 MHPELSQFPSNFFYEGSLQNGVCAEDRRLklDFPWPQPERPMFFLVTQGQEEIAGSGTSFLNRTEAANVEKITTRFLKAG 764
Cdd:cd18808    1 MHPEISEFPSKLFYEGKLKAGVSVAARLN--PPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  765 IKPEQIGIITPYEGQRAYLVQYMQYQGSlhsrLYQEIEIASVDAFQGREKDIIIMSCVRSNERQG-IGFLNDPRRLNVAL 843
Cdd:cd18808   79 VKPSSIGVITPYRAQVALIRELLRKRGG----LLEDVEVGTVDNFQGREKDVIILSLVRSNESGGsIGFLSDPRRLNVAL 154
                        170       180       190
                 ....*....|....*....|....*....|
gi 18859757  844 TRAKFGIIIVGNPKVLAKQQLWNHLLNFYK 873
Cdd:cd18808  155 TRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
507-875 2.35e-68

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 246.96  E-value: 2.35e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  507 AVDQLTEKIHRTNLKVVRVCAKSREAIDSPVSFLALHNQIRNMETNSELKKLQQLKDETGELSSADEKRyRNLKRAAENQ 586
Cdd:COG1112  452 LALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAARLRRALRRELKKR-RELRKLLWDA 530
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  587 LLEAADVICCTCVGAGD-GRLSRVKFTSILIDESMQSTEPECMVPVVLgAKQLILVGDHCQLGPVVMC---KKAARAGLS 662
Cdd:COG1112  531 LLELAPVVGMTPASVARlLPLGEGSFDLVIIDEASQATLAEALGALAR-AKRVVLVGDPKQLPPVVFGeeaEEVAEEGLD 609
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  663 QSLFERLV-VLGIRPFRLEVQYRMHPELSQFPSNFFYEGSLQNGVCAEDRRLkldfpwPQPERPMFFLVTQGQEEIAGSG 741
Cdd:COG1112  610 ESLLDRLLaRLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRL------ADPDSPLVFIDVDGVYERRGGS 683
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  742 TSflNRTEAANVEKITTRFLKAGIKPEQIGIITPYEGQRAYLVQYMQYQGSLHSRlyqEIEIASVDAFQGREKDIIIMSC 821
Cdd:COG1112  684 RT--NPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRELLREALGDGLE---PVFVGTVDRFQGDERDVIIFSL 758
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18859757  822 VRSNER---QGIGFLN-DPRRLNVALTRAKFGIIIVGNPKVL---AKQQLWNHLLNFYKDR 875
Cdd:COG1112  759 VYSNDEdvpRNFGFLNgGPRRLNVAVSRARRKLIVVGSRELLdsdPSTPALKRLLEYLERA 819
1B_UPF1-like cd21407
1B domain of eukaryotic UPF1 RNA helicase and related proteins; Helicases catalyze ...
302-390 2.20e-49

1B domain of eukaryotic UPF1 RNA helicase and related proteins; 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. UPF1 belongs to helicase superfamily 1 (SF1). It participates in nonsense-mediated mRNA decay (NMD), a pathway which degrades transcripts with premature termination codons. UPF1 is a multidomain protein; it includes an N-terminal Cys/His rich zinc-binding domain (CH/ZBD), a regulatory 1B domain, and a SF1 helicase core. The 1B domain is involved in nucleic acid substrate binding; the 1B domain of the related Equine arteritis virus (EAV) Nsp10 undergoes large conformational change upon substrate binding, and together with the 1A and 2A domains of the helicase core form a channel that accommodates the single stranded nucleic acids.


Pssm-ID: 394815  Cd Length: 90  Bit Score: 169.63  E-value: 2.20e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  302 TQENIEVRWDVGLNKKTIAYFTLAKTD-SDMKLMHGDELRLHYVGELYNPWSEIGHVIKVPDNFGDDVGLELKSSTNAPV 380
Cdd:cd21407    1 TQENISVRWDVGLNKKRLAYFTLPKLDeSELRLMVGDELRLRYKGDLREPWEGVGHVIKIPDNYSEEVALELRSSKNAPT 80
                         90
                 ....*....|
gi 18859757  381 KCTSNFTVDF 390
Cdd:cd21407   81 EITTGFSVEF 90
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
455-652 1.43e-47

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: 170.60  E-value: 1.43e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    455 SQVYAVKHALQRP-LSLIQGPPGTGKTVTSATIVYQLVKLHGGT------VLVCAPSNTAVDQLTEKIHRT----NLKVV 523
Cdd:pfam13086    1 SQREAIRSALSSShFTLIQGPPGTGKTTTIVELIRQLLSYPATSaaagprILVCAPSNAAVDNILERLLRKgqkyGPKIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    524 RVC--AKSREAIdSPVSFLALHNQIRNMETNSEL-----KKLQQLKDETGELSSADE----------------------- 573
Cdd:pfam13086   81 RIGhpAAISEAV-LPVSLDYLVESKLNNEEDAQIvkdisKELEKLAKALRAFEKEIIvekllksrnkdkskleqerrklr 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    574 -------KRYRNLKRAAENQLLEAADVICCTCVGAGDGRLSR-VKFTSILIDESMQSTEPECMVPVVLGAKQLILVGDHC 645
Cdd:pfam13086  160 serkelrKELRRREQSLEREILDEAQIVCSTLSGAGSRLLSSlANFDVVIIDEAAQALEPSTLIPLLRGPKKVVLVGDPK 239

                   ....*..
gi 18859757    646 QLGPVVM 652
Cdd:pfam13086  240 QLPPTVI 246
UPF1_1B_dom pfam18141
RNA helicase UPF1, 1B domain; UPF1 (or regulator of nonsense transcripts 1 homolog) is an ...
302-391 2.59e-41

RNA helicase UPF1, 1B domain; UPF1 (or regulator of nonsense transcripts 1 homolog) is an essential RNA helicase that detects mRNAs containing premature stop codons and triggers their degradation. Together with UPF2 and UPF3, forms a surveillance complex, in which UPF2 acts as a bridge between UPF1 and UPF3. UPF2 and UPF3 are non-enzymatic components of the complex that stimulate the activity of UPF1. UPF1 has a N-terminal cysteine/histidine-rich zinc-binding domain (CH/ZBD), a regulatory 1B domain, followed by a helicase core that belongs to superfamily 1 (SF1). This entry represents 1B domain of UPF1 which has a regulatory role. It suffers conformational changes from an inhibitory state to a transition-state complex that modulate RNA binding.


Pssm-ID: 407973  Cd Length: 93  Bit Score: 146.69  E-value: 2.59e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    302 TQENIEVRWDVGLNKKTIAYFTLAKTDS-DMKLMHGDELRLHYVGELYNPWSEIGHVIKVPDNFGDDVGLELK-SSTNAP 379
Cdd:pfam18141    2 TQDDISVRWDVGLNKKHLAWFSLPKLDSgEMKLAVGDELRLRYTGSLAEPWEGVGHVVKIPDNSSEEVTLELRsSSNNPP 81
                           90
                   ....*....|..
gi 18859757    380 VKCTSNFTVDFI 391
Cdd:pfam18141   82 TDLTHGFTVEFV 93
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
421-650 2.80e-12

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: 70.78  E-value: 2.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  421 RLLGHGRADSNDEVLFRGPQPKLFSAPHLpDLNRSQVYAVKHAL-QRPLSLIQGPPGTGKTVTSATIVYQLVKLhGGTVL 499
Cdd:COG0507   95 RRLRRLARPALDEADVEAALAALEPRAGI-TLSDEQREAVALALtTRRVSVLTGGAGTGKTTTLRALLAALEAL-GLRVA 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  500 VCAPSNTAVDQLTEK-------IHRtnlkvvrvcaksreaidspvsFLALhnqirnmetnselkklqqlkdetgelsSAD 572
Cdd:COG0507  173 LAAPTGKAAKRLSEStgieartIHR---------------------LLGL---------------------------RPD 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  573 EKRYRNlkraAENQLLEAADVicctcvgagdgrlsrvkftsILIDESMqstepecMVPVVLGAK----------QLILVG 642
Cdd:COG0507  205 SGRFRH----NRDNPLTPADL--------------------LVVDEAS-------MVDTRLMAAllealpragaRLILVG 253

                 ....*...
gi 18859757  643 DHCQLGPV 650
Cdd:COG0507  254 DPDQLPSV 261
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
447-650 4.80e-09

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: 60.54  E-value: 4.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    447 PHLPDLNRsQVYAVKHALQRPLSLIQGPPGTGKTVTSA----TIVYQLVKLHGGTVLVCAPSNTAVDQLTEKIHRtnlKV 522
Cdd:TIGR01447  141 PLLNEQNW-RKTAVALALKSNFSLITGGPGTGKTTTVArlllALVKQSPKQGKLRIALAAPTGKAAARLAESLRK---AV 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    523 VRVCAKSREAIDSPVSFLALHnqirnmetnselkKLQQLKdetgelssADEKRYRNLKRaaeNQLleAADVicctcvgag 602
Cdd:TIGR01447  217 KNLAAAEALIAALPSEAVTIH-------------RLLGIK--------PDTKRFRHHER---NPL--PLDV--------- 261
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 18859757    603 dgrlsrvkftsILIDE-SMQSTEPEC-MVPVVLGAKQLILVGDHCQLGPV 650
Cdd:TIGR01447  262 -----------LVVDEaSMVDLPLMAkLLKALPPNTKLILLGDKNQLPSV 300
DEXDc smart00487
DEAD-like helicases superfamily;
456-517 2.85e-05

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 46.33  E-value: 2.85e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859757     456 QVYAVKHALQRPLS-LIQGPPGTGKTVTSAT-IVYQLVKLHGGTVLVCAPSNTAVDQLTEKIHR 517
Cdd:smart00487   13 QKEAIEALLSGLRDvILAAPTGSGKTLAALLpALEALKRGKGGRVLVLVPTRELAEQWAEELKK 76
recD PRK10875
exodeoxyribonuclease V subunit alpha;
427-513 3.30e-04

exodeoxyribonuclease V subunit alpha;


Pssm-ID: 236783 [Multi-domain]  Cd Length: 615  Bit Score: 44.93  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757   427 RADSNDEVLFRGPQPKLF-SAPHLPDLnrsQVYAVKHALQRPLSLIQGPPGTGKTVTSATIVYQLVKLHGGTVLV---CA 502
Cdd:PRK10875  130 HAIEVDEALLRQTLDALFgPVTDEVDW---QKVAAAVALTRRISVISGGPGTGKTTTVAKLLAALIQLADGERCRirlAA 206
                          90
                  ....*....|.
gi 18859757   503 PSNTAVDQLTE 513
Cdd:PRK10875  207 PTGKAAARLTE 217
 
Name Accession Description Interval E-value
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
451-684 1.49e-165

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: 489.45  E-value: 1.49e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  451 DLNRSQVYAVKHALQRPLSLIQGPPGTGKTVTSATIVYQLVKLHGGTVLVCAPSNTAVDQLTEKIHRTNLKVVRVCAKSR 530
Cdd:cd18039    1 ELNHSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVDQLTEKIHQTGLKVVRLCAKSR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  531 EAIDSPVSFLALHNQIRNMETNSELKKLQQLKDETGELSSADEKRYRNLKRAAENQLLEAADVICCTCVGAGDGRLSRVK 610
Cdd:cd18039   81 EAVESPVSFLALHNQVRNLDSAEKLELLKLLKLETGELSSADEKRYRKLKRKAERELLRNADVICCTCVGAGDPRLSKMK 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859757  611 FTSILIDESMQSTEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAARAGLSQSLFERLVVLGIRPFRLEVQYR 684
Cdd:cd18039  161 FRTVLIDEATQATEPECLIPLVHGAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVQLGIRPIRLQVQYR 234
UPF1_Zn_bind pfam09416
RNA helicase (UPF2 interacting domain); UPF1 is an essential RNA helicase that detects mRNAs ...
98-249 3.33e-107

RNA helicase (UPF2 interacting domain); UPF1 is an essential RNA helicase that detects mRNAs containing premature stop codons and triggers their degradation. This domain contains 3 zinc binding motifs and forms interactions with another protein (UPF2) that is also involved nonsense-mediated mRNA decay (NMD).


Pssm-ID: 401391  Cd Length: 152  Bit Score: 332.68  E-value: 3.33e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757     98 HACKYCGIHDPATVVMCNNCRKWFCNGRGSTSGSHIINHLVRAKHREVTLHGEGPLGETILECYSCGVRNVFVLGFIPAK 177
Cdd:pfam09416    1 HACAYCGIHDPACVVKCLTCGKWFCNGRGNTSGSHIINHLVRSKHKEVSLHPDSPLGDTVLECYNCGSKNVFLLGFIPAK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18859757    178 ADSVVVLLCRQPCAAQNSLKDMNWDQEQWKPLIADRCFLAWLVKQPSEQGQLRARQISAAQINKLEELWKEN 249
Cdd:pfam09416   81 SDSVVVLLCRQPCAQAKSLKDMNWDTSQWQPLIEDRQFLPWLVKVPSEEEQLRARQITPAQINKLEELWKDN 152
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
355-880 3.27e-87

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: 295.96  E-value: 3.27e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    355 GHVIKVPDNFgddVGLELKSSTnaPVKCTSNFTVDFIWKCTSFDRMTRALCKFAIDRNSVSNFIYSRLLGHGRADSNDEV 434
Cdd:TIGR00376   78 GVVTRVGKRF---ITVALEESV--PQWSLKRVRIDLYANDVTFKRMKEALRALTENHSRLLEFLLGREAPSKASEIHDFQ 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    435 LFRgpqpklfsaphlPDLNRSQVYAVKHAL-QRPLSLIQGPPGTGKTVTSATIVYQLVKlHGGTVLVCAPSNTAVDQLTE 513
Cdd:TIGR00376  153 FFD------------PNLNESQKEAVLFALsSKDLFLIHGPPGTGKTRTVVELIRQLVK-RGLRVLVTAPSNIAVDNLLE 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    514 KIHRTNLKVVRVCAKSR--------------EAIDSPVSFLALHNQIRNM--ETNSELKKLQQLK---DETGELSSADEK 574
Cdd:TIGR00376  220 RLALCDQKIVRLGHPARllksnkqhsldyliENHPKYQIVADIREKIDELieERNKKTKPSPQKRrglSDIKILRKALKK 299
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    575 R--------------------------YRNLKRAAENQLLEAADVICCTCVGAGDGRLSRVKFTSILIDESMQSTEPECM 628
Cdd:TIGR00376  300 ReargieslkiasmaewietnksidrlLKLLPESEERIMNEILAESDATNSMAGSEILNGQYFDVAVIDEASQAMEPSCL 379
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    629 VPVVlGAKQLILVGDHCQLGPVVMCKKAAraGLSQSLFERLVVL-GIRPFRLEVQYRMHPELSQFPSNFFYEGSLQNGVC 707
Cdd:TIGR00376  380 IPLL-KARKLILAGDHKQLPPTILSHDAE--ELSLTLFERLIKEyPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHES 456
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    708 AEDRRLkLDFPWPQPER---------PMFFLVTQGQE----EIAGSgTSFLNRTEAANVEKITTRFLKAGIKPEQIGIIT 774
Cdd:TIGR00376  457 VANILL-RDLPKVEATEseddletgiPLLFIDTSGCElfelKEADS-TSKYNPGEAELVSEIIQALVKMGVPANDIGVIT 534
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    775 PYEGQRAYLVQYMQYQgslhsrlYQEIEIASVDAFQGREKDIIIMSCVRSNERQGIGFLNDPRRLNVALTRAKFGIIIVG 854
Cdd:TIGR00376  535 PYDAQVDLLRQLLEHR-------HIDIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIG 607
                          570       580
                   ....*....|....*....|....*.
gi 18859757    855 NPKVLAKQQLWNHLLNFYKDRKVLVE 880
Cdd:TIGR00376  608 DSRTLSNHKFYKRLIEWCKQHGEVRE 633
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
661-857 3.73e-79

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: 257.86  E-value: 3.73e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    661 LSQSLFERLVVLG-IRPFRLEVQYRMHPELSQFPSNFFYEGSLQNGVCAEDRRLKLDFPWPQPERPMFFL-VTQGQEEIA 738
Cdd:pfam13087    1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPDDFHLPDPLGPLVFIdVDGSEEEES 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    739 GSGTSFLNRTEAANVEKITTRFLKAGI-KPEQIGIITPYEGQRAYLVQYMQYQGSLHSrlyqEIEIASVDAFQGREKDII 817
Cdd:pfam13087   81 DGGTSYSNEAEAELVVQLVEKLIKSGPeEPSDIGVITPYRAQVRLIRKLLKRKLGGKL----EIEVNTVDGFQGREKDVI 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 18859757    818 IMSCVRSNERQGIGFLNDPRRLNVALTRAKFGIIIVGNPK 857
Cdd:pfam13087  157 IFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNAK 196
ZBD_UPF1-like cd21400
Cys/His rich zinc-binding domain (CH/ZBD) of eukaryotic UPF1 RNA helicase and related proteins; ...
99-219 1.04e-78

Cys/His rich zinc-binding domain (CH/ZBD) of eukaryotic UPF1 RNA helicase and related proteins; 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. UPF1 belongs to helicase superfamily 1 (SF1). The CH/ZBD has 3 zinc-finger (ZnF1-3) motifs. UPF1 participates in nonsense-mediated mRNA decay (NMD), a pathway which degrades transcripts with premature termination codons. The N-terminal CH/ZBD of UPF1 interacts with UPF2, a factor also involved in NMD. UPF1 has an N-terminal CH/ZBD, a 1B domain, and a SF1 helicase core.


Pssm-ID: 439167  Cd Length: 120  Bit Score: 253.71  E-value: 1.04e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757   99 ACKYCGIHDPATVVMCNNCRKWFCNGRGSTSGSHIINHLVRAKHREVTLHGEGPLGETILECYSCGVRNVFVLGFIPAKA 178
Cdd:cd21400    1 ACAYCGIHDPACLVKCLTCGKWFCNGRGNTSGSHIVQHLVRSKHKEVSLHPDSPLGDTVLECYNCGSRNVFLLGFIPAKA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 18859757  179 DSVVVLLCRQPCAAQNSlKDMNWDQEQWKPLIADRCFLAWL 219
Cdd:cd21400   81 DSVVVLLCRQPCLSQSS-KDMNWDLSQWQPLIDDRQFLPWL 120
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
685-873 1.61e-78

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: 255.62  E-value: 1.61e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  685 MHPELSQFPSNFFYEGSLQNGVCAEDRRLklDFPWPQPERPMFFLVTQGQEEIAGSGTSFLNRTEAANVEKITTRFLKAG 764
Cdd:cd18808    1 MHPEISEFPSKLFYEGKLKAGVSVAARLN--PPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKSG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  765 IKPEQIGIITPYEGQRAYLVQYMQYQGSlhsrLYQEIEIASVDAFQGREKDIIIMSCVRSNERQG-IGFLNDPRRLNVAL 843
Cdd:cd18808   79 VKPSSIGVITPYRAQVALIRELLRKRGG----LLEDVEVGTVDNFQGREKDVIILSLVRSNESGGsIGFLSDPRRLNVAL 154
                        170       180       190
                 ....*....|....*....|....*....|
gi 18859757  844 TRAKFGIIIVGNPKVLAKQQLWNHLLNFYK 873
Cdd:cd18808  155 TRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
507-875 2.35e-68

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 246.96  E-value: 2.35e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  507 AVDQLTEKIHRTNLKVVRVCAKSREAIDSPVSFLALHNQIRNMETNSELKKLQQLKDETGELSSADEKRyRNLKRAAENQ 586
Cdd:COG1112  452 LALLLLLLLALAALLLLLAAAAALLALALLESLLEELIEEHPEELEKLIAELREAARLRRALRRELKKR-RELRKLLWDA 530
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  587 LLEAADVICCTCVGAGD-GRLSRVKFTSILIDESMQSTEPECMVPVVLgAKQLILVGDHCQLGPVVMC---KKAARAGLS 662
Cdd:COG1112  531 LLELAPVVGMTPASVARlLPLGEGSFDLVIIDEASQATLAEALGALAR-AKRVVLVGDPKQLPPVVFGeeaEEVAEEGLD 609
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  663 QSLFERLV-VLGIRPFRLEVQYRMHPELSQFPSNFFYEGSLQNGVCAEDRRLkldfpwPQPERPMFFLVTQGQEEIAGSG 741
Cdd:COG1112  610 ESLLDRLLaRLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSPKARRL------ADPDSPLVFIDVDGVYERRGGS 683
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  742 TSflNRTEAANVEKITTRFLKAGIKPEQIGIITPYEGQRAYLVQYMQYQGSLHSRlyqEIEIASVDAFQGREKDIIIMSC 821
Cdd:COG1112  684 RT--NPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRELLREALGDGLE---PVFVGTVDRFQGDERDVIIFSL 758
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18859757  822 VRSNER---QGIGFLN-DPRRLNVALTRAKFGIIIVGNPKVL---AKQQLWNHLLNFYKDR 875
Cdd:COG1112  759 VYSNDEdvpRNFGFLNgGPRRLNVAVSRARRKLIVVGSRELLdsdPSTPALKRLLEYLERA 819
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
452-684 1.51e-51

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: 179.73  E-value: 1.51e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  452 LNRSQVYAVKHAL-QRPLSLIQGPPGTGKTVTSATIVYQLVKlHGGTVLVCAPSNTAVDQLTEKIHRTNLKVVRVCAKSR 530
Cdd:cd18044    2 LNDSQKEAVKFALsQKDVALIHGPPGTGKTTTVVEIILQAVK-RGEKVLACAPSNIAVDNLVERLVALKVKVVRIGHPAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  531 EaidspvsflalhnqirnmetnseLKKLQQlkdetgelSSADEkryrnlkraaenqlLEAADVICCTCVGAGD-GRLSRV 609
Cdd:cd18044   81 L-----------------------LESVLD--------HSLDA--------------LVAAQVVLATNTGAGSrQLLPNE 115
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18859757  610 KFTSILIDESMQSTEPECMVPVvLGAKQLILVGDHCQLGPVVMCKKAARAGLSQSLFERLVVL---GIRPFrLEVQYR 684
Cdd:cd18044  116 LFDVVVIDEAAQALEASCWIPL-LKARRCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLygeSVVRM-LTVQYR 191
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
452-684 3.01e-50

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: 178.87  E-value: 3.01e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  452 LNRSQVYAVKHALQRPLSLIQGPPGTGKTVTSATIVYQLVKLH------------GGTVLVCAPSNTAVDQLTEKI-HRT 518
Cdd:cd18040    2 LNPSQNHAVRTALTKPFTLIQGPPGTGKTVTGVHIAYWFAKQNreiqsvsgegdgGPCVLYCGPSNKSVDVVAELLlKVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  519 NLKVVRVCAKSREAIDSPV---------------------SFLALHNQIRNMET--NSELKKLQQLKDETGE-LSSADEK 574
Cdd:cd18040   82 GLKILRVYSEQIETTEYPIpneprhpnkksereskpnselSSITLHHRIRQPSNphSQQIKAFEARFERTQEkITEEDIK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  575 RYRNLKRAAENQLLEAADVICCTCVGAGDGRLSR-VKFTSILIDESMQSTEPECMVPVVLG--AKQLILVGDHCQLGPVV 651
Cdd:cd18040  162 TYKILIWEARFEELETVDVILCTCSEAASQKMRThANVKQCIVDECGMCTEPESLIPIVSAprAEQVVLIGDHKQLRPVV 241
                        250       260       270
                 ....*....|....*....|....*....|...
gi 18859757  652 MCKKAARAGLSQSLFERLVVlgiRPFRLEVQYR 684
Cdd:cd18040  242 QNKEAQKLGLGRSLFERYAE---KACMLDTQYR 271
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
452-687 9.22e-50

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: 175.89  E-value: 9.22e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  452 LNRSQVYAVKHALQR----PLSLIQGPPGTGKTVTSATIVYQLVKLHGGT-VLVCAPSNTAVDQLTEKIHRTNLK---VV 523
Cdd:cd18038    2 LNDEQKLAVRNIVTGtsrpPPYIIFGPPGTGKTVTLVEAILQVLRQPPEArILVCAPSNSAADLLAERLLNALVTkreIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  524 RVCAKSREAIDSPVSFLALHNQIrnMETNSELKKLQQLKdetgelssadekRYRnlkraaenqlleaadVICCTCVGAGd 603
Cdd:cd18038   82 RLNAPSRDRASVPPELLPYCNSK--AEGTFRLPSLEELK------------KYR---------------IVVCTLMTAG- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  604 gRLSRVK-----FTSILIDESMQSTEPECMVPVVLGAK---QLILVGDHCQLGPVVMCKKAARAGLSQSLFERLvvlgir 675
Cdd:cd18038  132 -RLVQAGvpnghFTHIFIDEAGQATEPEALIPLSELASkntQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERL------ 204
                        250
                 ....*....|..
gi 18859757  676 pFRLEVQYRMHP 687
Cdd:cd18038  205 -MERPLYYKDGE 215
1B_UPF1-like cd21407
1B domain of eukaryotic UPF1 RNA helicase and related proteins; Helicases catalyze ...
302-390 2.20e-49

1B domain of eukaryotic UPF1 RNA helicase and related proteins; 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. UPF1 belongs to helicase superfamily 1 (SF1). It participates in nonsense-mediated mRNA decay (NMD), a pathway which degrades transcripts with premature termination codons. UPF1 is a multidomain protein; it includes an N-terminal Cys/His rich zinc-binding domain (CH/ZBD), a regulatory 1B domain, and a SF1 helicase core. The 1B domain is involved in nucleic acid substrate binding; the 1B domain of the related Equine arteritis virus (EAV) Nsp10 undergoes large conformational change upon substrate binding, and together with the 1A and 2A domains of the helicase core form a channel that accommodates the single stranded nucleic acids.


Pssm-ID: 394815  Cd Length: 90  Bit Score: 169.63  E-value: 2.20e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  302 TQENIEVRWDVGLNKKTIAYFTLAKTD-SDMKLMHGDELRLHYVGELYNPWSEIGHVIKVPDNFGDDVGLELKSSTNAPV 380
Cdd:cd21407    1 TQENISVRWDVGLNKKRLAYFTLPKLDeSELRLMVGDELRLRYKGDLREPWEGVGHVIKIPDNYSEEVALELRSSKNAPT 80
                         90
                 ....*....|
gi 18859757  381 KCTSNFTVDF 390
Cdd:cd21407   81 EITTGFSVEF 90
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
455-652 1.43e-47

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: 170.60  E-value: 1.43e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    455 SQVYAVKHALQRP-LSLIQGPPGTGKTVTSATIVYQLVKLHGGT------VLVCAPSNTAVDQLTEKIHRT----NLKVV 523
Cdd:pfam13086    1 SQREAIRSALSSShFTLIQGPPGTGKTTTIVELIRQLLSYPATSaaagprILVCAPSNAAVDNILERLLRKgqkyGPKIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    524 RVC--AKSREAIdSPVSFLALHNQIRNMETNSEL-----KKLQQLKDETGELSSADE----------------------- 573
Cdd:pfam13086   81 RIGhpAAISEAV-LPVSLDYLVESKLNNEEDAQIvkdisKELEKLAKALRAFEKEIIvekllksrnkdkskleqerrklr 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    574 -------KRYRNLKRAAENQLLEAADVICCTCVGAGDGRLSR-VKFTSILIDESMQSTEPECMVPVVLGAKQLILVGDHC 645
Cdd:pfam13086  160 serkelrKELRRREQSLEREILDEAQIVCSTLSGAGSRLLSSlANFDVVIIDEAAQALEPSTLIPLLRGPKKVVLVGDPK 239

                   ....*..
gi 18859757    646 QLGPVVM 652
Cdd:pfam13086  240 QLPPTVI 246
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
452-684 1.81e-41

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: 151.98  E-value: 1.81e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  452 LNRSQVYAVKHALQR--PLSLIQGPPGTGKTVTSATIVYQL----------VKLHGGT--------------VLVCAPSN 505
Cdd:cd18042    1 LNESQLEAIASALQNspGITLIQGPPGTGKTKTIVGILSVLlagkyrkyyeKVKKKLRklqrnlnnkkkknrILVCAPSN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  506 TAVDQLTEKI----------HRTNLKVVRVcaksreaidspvsflalhnqirnmetnselkklqqlkdetGelssadekr 575
Cdd:cd18042   81 AAVDEIVLRLlsegfldgdgRSYKPNVVRV----------------------------------------G--------- 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  576 yrnlKRAAENQLLEAADVICCTCVGAGDGRLSR--VKFTSILIDESMQSTEPECMVPVVLGAKQLILVGDHCQLGPVVMC 653
Cdd:cd18042  112 ----RQELRASILNEADIVCTTLSSSGSDLLESlpRGFDTVIIDEAAQAVELSTLIPLRLGCKRLILVGDPKQLPATVFS 187
                        250       260       270
                 ....*....|....*....|....*....|.
gi 18859757  654 KKAARAGLSQSLFERLVVLGIRPFRLEVQYR 684
Cdd:cd18042  188 KVAQKLGYDRSLFERLQLAGYPVLMLTTQYR 218
UPF1_1B_dom pfam18141
RNA helicase UPF1, 1B domain; UPF1 (or regulator of nonsense transcripts 1 homolog) is an ...
302-391 2.59e-41

RNA helicase UPF1, 1B domain; UPF1 (or regulator of nonsense transcripts 1 homolog) is an essential RNA helicase that detects mRNAs containing premature stop codons and triggers their degradation. Together with UPF2 and UPF3, forms a surveillance complex, in which UPF2 acts as a bridge between UPF1 and UPF3. UPF2 and UPF3 are non-enzymatic components of the complex that stimulate the activity of UPF1. UPF1 has a N-terminal cysteine/histidine-rich zinc-binding domain (CH/ZBD), a regulatory 1B domain, followed by a helicase core that belongs to superfamily 1 (SF1). This entry represents 1B domain of UPF1 which has a regulatory role. It suffers conformational changes from an inhibitory state to a transition-state complex that modulate RNA binding.


Pssm-ID: 407973  Cd Length: 93  Bit Score: 146.69  E-value: 2.59e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    302 TQENIEVRWDVGLNKKTIAYFTLAKTDS-DMKLMHGDELRLHYVGELYNPWSEIGHVIKVPDNFGDDVGLELK-SSTNAP 379
Cdd:pfam18141    2 TQDDISVRWDVGLNKKHLAWFSLPKLDSgEMKLAVGDELRLRYTGSLAEPWEGVGHVVKIPDNSSEEVTLELRsSSNNPP 81
                           90
                   ....*....|..
gi 18859757    380 VKCTSNFTVDFI 391
Cdd:pfam18141   82 TDLTHGFTVEFV 93
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
451-670 3.44e-36

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: 137.11  E-value: 3.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  451 DLNRSQVYAVKHALQ---RPLS-LIQGPPGTGKTVTSATIVYQLVKLHGGT-VLVCAPSNTAVDQLTEKIHRTNLKVVRV 525
Cdd:cd18078    1 DLNELQKEAVKRILGgecRPLPyILFGPPGTGKTVTIIEAILQVVYNLPRSrILVCAPSNSAADLVTSRLHESKVLKPGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  526 CAKsreaidspvsfLALHNqiRNMETNSELKKLQQLKDETGELSSadekRYRnlkraaenqlleaadVICCTCVGAG--- 602
Cdd:cd18078   81 MVR-----------LNAVN--RFESTVIDARKLYCRLGEDLSKAS----RHR---------------IVISTCSTAGlly 128
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18859757  603 DGRLSRVKFTSILIDESMQSTEPECMVPVVL---GAKQLILVGDHCQLGPVVMCKKAARAGLSQSLFERLV 670
Cdd:cd18078  129 QMGLPVGHFTHVFVDEAGQATEPESLIPLGLissRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLM 199
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
452-684 3.25e-35

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: 133.13  E-value: 3.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  452 LNRSQVYAVKHALQ-RPLSLIQGPPGTGKTVTSATIVYQLVKLhGGTVLVCAPSNTAVDQLTEKIHRTNLKVVRVCAKSR 530
Cdd:cd18041    2 LNKDQRQAIKKVLNaKDYALILGMPGTGKTTTIAALVRILVAL-GKSVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  531 eaIDSPVSFLALHNQIRNMETNSELKKLqqlkdetgelssadekryrnlkraaenqlLEAADVICCTCVGAGDGRLSRVK 610
Cdd:cd18041   81 --IHPDVQEFTLEAILKSCKSVEELESK-----------------------------YESVSVVATTCLGINHPIFRRRT 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  611 FTSILIDESMQSTEPECMVPVVLgAKQLILVGDHCQLGPVVMCKKAARAGLSQSLFERL-------VVlgirpfRLEVQY 683
Cdd:cd18041  130 FDYCIVDEASQITLPICLGPLRL-AKKFVLVGDHYQLPPLVKSREARELGMDESLFKRLseahpdaVV------QLTIQY 202

                 .
gi 18859757  684 R 684
Cdd:cd18041  203 R 203
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
468-684 3.97e-28

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: 110.02  E-value: 3.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  468 LSLIQGPPGTGKTVTSATIVYQLVK-LHGGTVLVCAPSNTAVDQLtekihrtnlkvvrvcaksreaidspvsflalhnqi 546
Cdd:cd17934    1 ISLIQGPPGTGKTTTIAAIVLQLLKgLRGKRVLVTAQSNVAVDNV----------------------------------- 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  547 rnmetnselkklqqlkdetgelssadekryrnlkraaenqlleaaDVIcctcvgagdgrlsrvkftsiLIDESMQSTEPE 626
Cdd:cd17934   46 ---------------------------------------------DVV--------------------IIDEASQITEPE 60
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18859757  627 CMVPVvLGAKQLILVGDHCQLGPVVMCKKAARAG----LSQSLFERLVVLGIRPFRLEVQYR 684
Cdd:cd17934   61 LLIAL-IRAKKVVLVGDPKQLPPVVQEDHAALLGlsfiLSLLLLFRLLLPGSPKVMLDTQYR 121
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
452-683 2.41e-27

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: 109.94  E-value: 2.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  452 LNRSQVYAVKHALQRPLSLIQGPPGTGKTVTSATIVYQLV----KLHGGTVLVCAPSNTAVDQLTEKIHRTNL-KVVRVc 526
Cdd:cd17936    2 LDPSQLEALKHALTSELALIQGPPGTGKTFLGVKLVRALLqnqdLSITGPILVVCYTNHALDQFLEGLLDFGPtKIVRL- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  527 aksreaidspvsflalhnqirnmetnselkklqqlkdetgelssadekryrnlkraaenqlleAADVICCTCVGAGDGR- 605
Cdd:cd17936   81 ---------------------------------------------------------------GARVIGMTTTGAAKYRe 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  606 -LSRVKFTSILIDESMQSTEPE---CMVPVVlgaKQLILVGDHCQLGPVVMCKKAARAG--LSQSLFERLVVLGIRPFRL 679
Cdd:cd17936   98 lLQALGPKVVIVEEAAEVLEAHilaALTPST---EHLILIGDHKQLRPKVNVYELTAKKynLDVSLFERLVKNGLPFVTL 174

                 ....
gi 18859757  680 EVQY 683
Cdd:cd17936  175 NVQR 178
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
468-683 5.58e-25

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: 101.02  E-value: 5.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  468 LSLIQGPPGTGKTVTSATIVYQLVKLHG---GTVLVCAPSNTAVDQLTEkihrtnlkvvrvcaksreaidspvsflalhn 544
Cdd:cd17914    1 LSLIQGPPGTGKTRVLVKIVAALMQNKNgepGRILLVTPTNKAAAQLDN------------------------------- 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  545 qirnmetnselkklqqlkdetgelssadekryrnlkraaenqlleaadvicctcvgagdgrlsrvkftsILIDESMQSTE 624
Cdd:cd17914   50 ---------------------------------------------------------------------ILVDEAAQILE 60
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18859757  625 PECM--VPVVLGAKQLILVGDHCQLGPVVMCKKAARAGLSQSLFERLVVLGIRPFRLEVQY 683
Cdd:cd17914   61 PETSrlIDLALDQGRVILVGDHDQLGPVWRGAVLAKICNEQSLFTRLVRLGVSLIRLQVQY 121
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
769-854 1.98e-22

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: 92.50  E-value: 1.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  769 QIGIITPYEGQRAYLVQYMQyQGSLHSRLYQEIEIASVDAFQGREKDIIIMSCVRSNErqgigflNDPRRLNVALTRAKF 848
Cdd:cd18786   12 KGVVLTPYHRDRAYLNQYLQ-GLSLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTANS-------LTPRRLYVALTRARK 83

                 ....*.
gi 18859757  849 GIIIVG 854
Cdd:cd18786   84 RLVIYD 89
1B_UPF1_nv_SF1_Hel-like cd21344
1B domain of eukaryotic UPF1 helicase, nidovirus SF1 helicases including coronavirus Nsp13 and ...
304-389 1.81e-21

1B domain of eukaryotic UPF1 helicase, nidovirus SF1 helicases including coronavirus Nsp13 and arterivirus Nsp10, and related proteins; 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. Members of this family belong to helicase superfamily 1 (SF1) and include nidoviral helicases such as Severe Acute Respiratory Syndrome coronavirus (SARS) non-structural protein 13 (SARS-Nsp13), Equine arteritis virus (EAV) Nsp10, and eukaryotic UPF1 RNA helicase. SARS-Nsp13 is a component of the viral RNA synthesis replication and transcription complex (RTC). UPF1 participates in nonsense-mediated mRNA decay (NMD), a pathway which degrades transcripts with premature termination codons. UPF1, EAV Nsp10 and SARS-Nsp13 are multidomain proteins with an N-terminal Cys/His rich zinc-binding domain (CH/ZBD), a 1B domain and a SF1 helicase core. The 1B domain is involved in nucleic acid substrate binding; the 1B domain of EAV Nsp10 undergoes large conformational change upon substrate binding, and together with the 1A and 2A domains of the helicase core form a channel that accommodates the single stranded nucleic acids.


Pssm-ID: 439170  Cd Length: 86  Bit Score: 89.68  E-value: 1.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  304 ENIEVRWDVGLNKKTIAYFTLAKTDSDMKLMHGDELRLHYVGELYNPWSEIGHVIKVPDNFGDDVGLELKSSTNAPVKCT 383
Cdd:cd21344    1 LIITVRWRLALNDFRGAYFSLEKGKSQCKPPLGDEIVLTYYGDTVPLWEGIGEVIDLPNTGNDDDALELKGSTTYPLTVT 80

                 ....*.
gi 18859757  384 SNFTVD 389
Cdd:cd21344   81 HIFVLT 86
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
453-691 1.53e-19

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: 88.25  E-value: 1.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  453 NRSQVYAVKHALQRPLSLIQGPPGTGKTVTSATIVYQLVKLHGG--TVLVcAPSNTAVDQLTEKIhrtnlkvvrvcaksr 530
Cdd:cd17935    7 TPTQIEAIRSGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNqrTLIV-THSNQALNQLFEKI--------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  531 EAIDspvsflalhnqirnmetnselkklqqlkdetgelssADEkryRNLKRaaenqLLEAADVICCTCVGAGDGRLSRV- 609
Cdd:cd17935   71 MALD------------------------------------IDE---RHLLR-----LGHGAKIIAMTCTHAALKRGELVe 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  610 ---KFTSILIDESMQSTEPECMVPVVL--------GAKQLILVGDHCQLGPVVmcKKAARAGLS---QSLFERLVVLGIR 675
Cdd:cd17935  107 lgfKYDNILMEEAAQILEIETFIPLLLqnpedgpnRLKRLIMIGDHHQLPPVI--KNMAFQKYSnmeQSLFTRLVRLGVP 184
                        250
                 ....*....|....*.
gi 18859757  676 PFRLEVQYRMHPELSQ 691
Cdd:cd17935  185 TVDLDAQGRARASISS 200
ZBD_UPF1_nv_SF1_Hel-like cd21343
Cys/His rich zinc-binding domain (CH/ZBD) of eukaryotic UPF1 helicase, nidovirus SF1 helicases ...
99-188 2.55e-14

Cys/His rich zinc-binding domain (CH/ZBD) of eukaryotic UPF1 helicase, nidovirus SF1 helicases including coronavirus Nsp13 and arterivirus Nsp10, and related proteins; 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. Members of this family belong to helicase superfamily 1 (SF1) and include nidoviral helicases such as Severe Acute Respiratory Syndrome coronavirus (SARS) non-structural protein 13 (SARS-Nsp13) and equine arteritis virus (EAV) Nsp10, as well as eukaryotic UPF1 helicase. The CH/ZBD has 3 zinc-finger (ZnF1-3) motifs. UPF1 participates in nonsense-mediated mRNA decay (NMD), a pathway which degrades transcripts with premature termination codons. The CH/ZBD of UPF1 interacts with UPF2, a factor also involved in NMD. SARS-Nsp13 is a component of the viral RNA synthesis replication and transcription complex (RTC). The SARS-Nsp13 CH/ZBD is indispensable for helicase activity and interacts with SARS-Nsp12, the RNA-dependent RNA polymerase. SARS-Nsp12 can enhance the helicase activity of SARS-Nsp13. UPF1, SARS-Nsp13 and EAV Nsp10 are multidomain proteins; their other domains include a 1B regulatory domain and a SF1 helicase core.


Pssm-ID: 439166  Cd Length: 70  Bit Score: 68.67  E-value: 2.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757   99 ACKYCGIHdpaTVVMCNNC--RKWFCNgrgstsgSHIINHLVRAKHREVTLHgegplgeTILECYSCGVRNVFVLGFipa 176
Cdd:cd21343    1 ACYVCGSH---TVVRCGTCirRPWFCN-------SCIYDHLIRTKHKEVLLA-------SPYVCAGCGESDITLLYF--- 60
                         90
                 ....*....|..
gi 18859757  177 kadSVVVLLCRQ 188
Cdd:cd21343   61 ---GGVSYRCVD 69
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
452-669 5.34e-13

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: 69.82  E-value: 5.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  452 LNRSQVYAVKhALQRPLS------LIQGPPGTGKTVTSATIVYQLVKLHGGTVLVCAPSNTAVD-QLTEKIHrtnlkvvr 524
Cdd:cd18077    2 LNAKQKEAVL-AITTPLSiqlppvLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADlYIKEYLH-------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  525 vcaKSREAIDSPVSFLALHNQIRNMETNSELKKLQQLKDETGelssadekryrNLKRAAENQLLEAADVICCTCVGAGDG 604
Cdd:cd18077   73 ---PYVETGNPRARPLRVYYRNRWVKTVHPVVQKYCLIDEHG-----------TFRMPTREDVMRHRVVVVTLSTSQYLC 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18859757  605 RLSRVK--FTSILIDESMQSTEPECMVPVVLGAK--QLILVGDHCQLGPVVMCKKAARAGLSQSLFERL 669
Cdd:cd18077  139 QLDLEPgfFTHILLDEAAQAMECEAIMPLALATKstRIVLAGDHMQLSPEVYSEFARERNLHISLLERL 207
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
453-652 1.32e-12

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: 65.68  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  453 NRSQVYAVKHALQRPLSLIQGPPGTGKTVTSATIVYQLVKlHGGTVLVCAPSNTAvdqltekihrtnLKVVRVcaksrea 532
Cdd:cd18043    1 DSSQEAAIISARNGKNVVIQGPPGTGKSQTIANIIANALA-RGKRVLFVSEKKAA------------LDVVRF------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  533 idsPVSFLALHNQIRNMETNselkklqqlkdetgelssadekryrnlkraaenqlleaadvicctcvgagdgrlsRVKFT 612
Cdd:cd18043   61 ---PCWIMSPLSVSQYLPLN-------------------------------------------------------RNLFD 82
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 18859757  613 SILIDESMQStEPECMVPVVLGAKQLILVGDHCQLGPVVM 652
Cdd:cd18043   83 LVIFDEASQI-PIEEALPALFRGKQVVVVGDDKQLPPSIL 121
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
421-650 2.80e-12

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: 70.78  E-value: 2.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  421 RLLGHGRADSNDEVLFRGPQPKLFSAPHLpDLNRSQVYAVKHAL-QRPLSLIQGPPGTGKTVTSATIVYQLVKLhGGTVL 499
Cdd:COG0507   95 RRLRRLARPALDEADVEAALAALEPRAGI-TLSDEQREAVALALtTRRVSVLTGGAGTGKTTTLRALLAALEAL-GLRVA 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  500 VCAPSNTAVDQLTEK-------IHRtnlkvvrvcaksreaidspvsFLALhnqirnmetnselkklqqlkdetgelsSAD 572
Cdd:COG0507  173 LAAPTGKAAKRLSEStgieartIHR---------------------LLGL---------------------------RPD 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  573 EKRYRNlkraAENQLLEAADVicctcvgagdgrlsrvkftsILIDESMqstepecMVPVVLGAK----------QLILVG 642
Cdd:COG0507  205 SGRFRH----NRDNPLTPADL--------------------LVVDEAS-------MVDTRLMAAllealpragaRLILVG 253

                 ....*...
gi 18859757  643 DHCQLGPV 650
Cdd:COG0507  254 DPDQLPSV 261
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
452-669 1.41e-11

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: 65.68  E-value: 1.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  452 LNRSQVYAVK-------HALQRPLSLIQGPPGTGKTVTSATIVYQLVKLHGGTVLVCAPSNTAVD-QLTEKIHRtnlkvv 523
Cdd:cd18076    2 GNNKQQLAFNfiagkpsEARFVPPLLIYGPFGTGKTFTLAMAALEVIREPGTKVLICTHTNSAADiYIREYFHP------ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  524 RVCAKSREAIdsPVSFLALHNQIRNMETNSelkklQQLKdetgeLSSADEKRYRNLKRAaenqLLEAADVICCTCVGAGD 603
Cdd:cd18076   76 YVDKGHPEAR--PLRIKATDRPNAITDPDT-----ITYC-----CLTKDRQCFRLPTRD----ELDFHNIVITTTAMAFN 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18859757  604 GRLSRVKFTSILIDESMQSTEPECMVPVVLGA--KQLILVGDHCQLGPVVMCKKAARAGlSQSLFERL 669
Cdd:cd18076  140 LHVLSGFFTHIFIDEAAQMLECEALIPLSYAGpkTRVVLAGDHMQMTPKLFSVADYNRA-NHTLLNRL 206
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
456-517 4.05e-11

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: 62.57  E-value: 4.05e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18859757  456 QVYAVKHALQRPLSLIQGPPGTGKTVTSATIVYQLVKlHGGTVLVCAPSNTAVDQLTEK-------IHR 517
Cdd:cd17933    2 QKAAVRLVLRNRVSVLTGGAGTGKTTTLKALLAALEA-EGKRVVLAAPTGKAAKRLSEStgieastIHR 69
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
447-650 4.80e-09

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: 60.54  E-value: 4.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    447 PHLPDLNRsQVYAVKHALQRPLSLIQGPPGTGKTVTSA----TIVYQLVKLHGGTVLVCAPSNTAVDQLTEKIHRtnlKV 522
Cdd:TIGR01447  141 PLLNEQNW-RKTAVALALKSNFSLITGGPGTGKTTTVArlllALVKQSPKQGKLRIALAAPTGKAAARLAESLRK---AV 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    523 VRVCAKSREAIDSPVSFLALHnqirnmetnselkKLQQLKdetgelssADEKRYRNLKRaaeNQLleAADVicctcvgag 602
Cdd:TIGR01447  217 KNLAAAEALIAALPSEAVTIH-------------RLLGIK--------PDTKRFRHHER---NPL--PLDV--------- 261
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 18859757    603 dgrlsrvkftsILIDE-SMQSTEPEC-MVPVVLGAKQLILVGDHCQLGPV 650
Cdd:TIGR01447  262 -----------LVVDEaSMVDLPLMAkLLKALPPNTKLILLGDKNQLPSV 300
AAA_19 pfam13245
AAA domain;
459-517 8.46e-09

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 55.30  E-value: 8.46e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18859757    459 AVKHALQRPLSLIQGPPGTGKTVTSATIVYQLVKLHGG--TVLVCAPSNTAVDQLTEK-------IHR 517
Cdd:pfam13245    4 AVRTALPSKVVLLTGGPGTGKTTTIRHIVALLVALGGVsfPILLAAPTGRAAKRLSERtglpastIHR 71
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
452-513 8.68e-09

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: 56.42  E-value: 8.68e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859757    452 LNRSQVYAVKHAL--QRPLSLIQGPPGTGKTvTSATIVYQLVKLHGGTVLVCAPSNTAVDQLTE 513
Cdd:pfam13604    2 LNAEQAAAVRALLtsGDRVAVLVGPAGTGKT-TALKALREAWEAAGYRVIGLAPTGRAAKVLGE 64
COG3972 COG3972
Superfamily I DNA and RNA helicases [Replication, recombination and repair];
401-847 1.17e-07

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


Pssm-ID: 443172 [Multi-domain]  Cd Length: 565  Bit Score: 55.99  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  401 TRALCKFAIDR-NSVSNFIYSRLLGHGRADsndevLFRGPQPKLFSAPHLPDLNRSQVYAVKHALQRPLsLIQGPPGTGK 479
Cdd:COG3972  113 LRLLAASRRDFlFALLLPEIPPAPFVQALR-----LLNLVSLEDFFLPLIAVLDLQQERIARSIPDGPQ-RIRGVAGSGK 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  480 TVTSAtivYQLVKLH----GGTVL-VCApSNTAVDQLTEKIHRTNLKvvrvcaKSREAIDSPVSFLALHNQIRNMETNSE 554
Cdd:COG3972  187 TVLLA---AKAAYLAlkhpGWRILvTCF-NRSLADHLRDLIPRFLRR------FSNGEPEDNVKLIVFHAWGGKLLKQYG 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  555 LKKLQQlkdetgelsSADEKRYrnlkRAAENQLLEAAdvicctcvgagDGRLSRVKFTSILIDESmQSTEPECMVPVVL- 633
Cdd:COG3972  257 IPPLTF---------SQPNEAF----DEACKALLEAI-----------QGEIIPPIYDAILIDEA-QDFEPEFLRLLYQl 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  634 ---GAKQLILVGDHcqlgpvvmckkaaraglSQSLFER--LVVLGI-----RPFRLEVQYRMHPELSQFpSNFFYEGSLQ 703
Cdd:COG3972  312 lkpPKKRLIWAYDE-----------------AQNIYGRkiPSAGGIpagigRDTILKKNYRNTRPILTF-AHAFGMGLLR 373
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  704 NGVCAEDRrlKLDFPWPQPERPMFFLVTQGQEEIAGSG---TSFLNRTEAAN--VEKITTRFLKAGIKPEQIGIITP--Y 776
Cdd:COG3972  374 PPGLLQGD--AEDYEVERPGDKVTLIRPPEPAGRKGPLpefKKYDDRAEELEaiAEEIKKNLRDEGLRPSDIAVIYLgnN 451
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  777 EGQR--AYLVQYMQYQG----SLHSRLYQEIE-------IASVDAFQGREKDIIImsCVRSNE-RQGIGFLNDPRRLNVA 842
Cdd:COG3972  452 EAKElgDRLAAALERQGidsyIAGARSDPNFFwkdggvtISTIHRAKGLEAPVVI--IVGLDQlAKGESLERLRNLLYVA 529

                 ....*
gi 18859757  843 LTRAK 847
Cdd:COG3972  530 MTRAR 534
DEXDc smart00487
DEAD-like helicases superfamily;
456-517 2.85e-05

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 46.33  E-value: 2.85e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18859757     456 QVYAVKHALQRPLS-LIQGPPGTGKTVTSAT-IVYQLVKLHGGTVLVCAPSNTAVDQLTEKIHR 517
Cdd:smart00487   13 QKEAIEALLSGLRDvILAAPTGSGKTLAALLpALEALKRGKGGRVLVLVPTRELAEQWAEELKK 76
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
470-517 3.42e-05

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 48.10  E-value: 3.42e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 18859757  470 LIQGPPGTGKTVTSATIVYQLvkLHGGTVLVCAPSNTAVDQLTEKIHR 517
Cdd:COG1061  104 LVVAPTGTGKTVLALALAAEL--LRGKRVLVLVPRRELLEQWAEELRR 149
gammaCoV_Nsp13-helicase cd21720
helicase domain of gammacoronavirus non-structural protein 13; This model represents the ...
722-853 5.26e-05

helicase domain of gammacoronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from gammacoronavirus, including Avian infectious bronchitis virus. 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. Coronavirus (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: 409653 [Multi-domain]  Cd Length: 343  Bit Score: 46.83  E-value: 5.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757  722 PERPMFF--LVTQGQEEIAGSGTSFLNRTEAANVEkittRFLKAGIKPEQIGIITPYEG--QRAYlvqymqyqgslhsRL 797
Cdd:cd21720  215 PESRQCFkvIVNNGNSDVGHESGSAYNTTQLEFVK----DFVCRNKEWREATFISPYNAmnQRAY-------------RM 277
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18859757  798 YQeIEIASVDAFQGREKDIIIMsCVRSNERQGIGFlndpRRLNVALTRAKFGIIIV 853
Cdd:cd21720  278 LG-LNVQTVDSSQGSEYDYVIF-CVTADSQHALNI----NRFNVALTRAKRGILVV 327
recD PRK10875
exodeoxyribonuclease V subunit alpha;
427-513 3.30e-04

exodeoxyribonuclease V subunit alpha;


Pssm-ID: 236783 [Multi-domain]  Cd Length: 615  Bit Score: 44.93  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757   427 RADSNDEVLFRGPQPKLF-SAPHLPDLnrsQVYAVKHALQRPLSLIQGPPGTGKTVTSATIVYQLVKLHGGTVLV---CA 502
Cdd:PRK10875  130 HAIEVDEALLRQTLDALFgPVTDEVDW---QKVAAAVALTRRISVISGGPGTGKTTTVAKLLAALIQLADGERCRirlAA 206
                          90
                  ....*....|.
gi 18859757   503 PSNTAVDQLTE 513
Cdd:PRK10875  207 PTGKAAARLTE 217
cdc6 PRK00411
ORC1-type DNA replication protein;
430-482 3.36e-04

ORC1-type DNA replication protein;


Pssm-ID: 234751 [Multi-domain]  Cd Length: 394  Bit Score: 44.45  E-value: 3.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18859757   430 SNDEVLFRgpQPKLFSAPHLPD-LN------RSQVYAVKHALQ--RPL-SLIQGPPGTGKTVT 482
Cdd:PRK00411   11 MWDETIFK--DEEVLEPDYVPEnLPhreeqiEELAFALRPALRgsRPLnVLIYGPPGTGKTTT 71
ResIII pfam04851
Type III restriction enzyme, res subunit;
452-515 1.15e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 41.12  E-value: 1.15e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    452 LNRSQVYAVKHALQRPLS-----LIQGPPGTGKTVTSATIVYQLVKLHGGT-VLVCAPSNTAVDQLTEKI 515
Cdd:pfam04851    4 LRPYQIEAIENLLESIKNgqkrgLIVMATGSGKTLTAAKLIARLFKKGPIKkVLFLVPRKDLLEQALEEF 73
deltaCoV_Nsp13-helicase cd21721
helicase domain of deltacoronavirus non-structural protein 13; This model represents the ...
805-853 1.96e-03

helicase domain of deltacoronavirus non-structural protein 13; This model represents the helicase domain of non-structural protein 13 (Nsp13) from deltacoronavirus, including Bulbul coronavirus (CoV) HKU11 and Common moorhen CoV HKU21. 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: 409654 [Multi-domain]  Cd Length: 342  Bit Score: 41.83  E-value: 1.96e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 18859757  805 SVDAFQGREKDIIIMsCVRSNERQGIGFlndpRRLNVALTRAKFGIIIV 853
Cdd:cd21721  283 TVDSSQGSEYDYVIF-CVTTDSAHALNM----SRLNVALTRAKIGILVV 326
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
456-536 2.24e-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: 40.18  E-value: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859757    456 QVYAVKHALQRPLS------LIQGPPGTGKTVTSATIVYQLVKLHGGTVLVCAPSNTAVDQLTEKIHRTNLkVVRVCAKS 529
Cdd:pfam13191    8 ELEQLLDALDRVRSgrppsvLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPLLEALTREGL-LRQLLDEL 86

                   ....*..
gi 18859757    530 REAIDSP 536
Cdd:pfam13191   87 ESSLLEA 93
DEAD-like_helicase_N cd17912
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
470-519 2.82e-03

N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase superfamily is a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. The N-terminal domain contains the ATP-binding region.


Pssm-ID: 350670 [Multi-domain]  Cd Length: 81  Bit Score: 37.88  E-value: 2.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18859757  470 LIQGPPGTGKTVTsATIVYQLVKLHGGTVLVCAPSNTAVDQ---LTEKIHRTN 519
Cdd:cd17912    3 LHLGPTGSGKTLV-AIQKIASAMSSGKSVLVVTPTKLLAHEiliVIDEIQ*IL 54
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
470-521 4.87e-03

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: 38.89  E-value: 4.87e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 18859757     470 LIQGPPGTGKTVTSATIVYQLVKLHGGTVLVCAPSNTAVDQLTEKIHRTNLK 521
Cdd:smart00382    6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGK 57
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
470-511 7.52e-03

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 38.15  E-value: 7.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 18859757  470 LIQGPPGTGKTVTSATIVYQLVKLHGGTVLVCAPSNTAVDQL 511
Cdd:cd00046    5 LITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALQT 46
AAA_22 pfam13401
AAA domain;
465-515 7.97e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.71  E-value: 7.97e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 18859757    465 QRPLSLIQGPPGTGKTVTSATIVYQLVKLHGGTVLVCAPSNTAVDQLTEKI 515
Cdd:pfam13401    4 GAGILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRAL 54
DEAD-like_helicase_C cd09300
C-terminal helicase domain of the DEAD-like helicases; This hierarchy of DEAD-like helicases ...
801-847 8.99e-03

C-terminal helicase domain of the DEAD-like helicases; This hierarchy of DEAD-like helicases is composed of two superfamilies, SF1 and SF2, that share almost identical folds and extensive structural similarity in their catalytic core. Helicases are involved in ATP-dependent RNA or DNA unwinding. Two distinct types of helicases exist, those forming toroidal, predominantly hexameric structures, and those that do not. SF1 and SF2 helicases do not form toroidal structures, while SF3-6 helicases do. Their conserved 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: 350171 [Multi-domain]  Cd Length: 59  Bit Score: 35.60  E-value: 8.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 18859757  801 IEIASVDAFQG---REKDIIIMSCVRsnerqgigflNDPRRLNVALTRAK 847
Cdd:cd09300    8 VLIAVN*ALTGfdaPELNTIIVDKNL----------RSYRGLNQAFGRAN 47
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH