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Conserved domains on  [gi|2085193927|ref|XP_043089379|]
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regulator of nonsense transcripts 1 isoform X1 [Puntigrus tetrazona]

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

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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 ...
450-683 1.13e-176

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: 516.03  E-value: 1.13e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  450 DLNHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLKVVRLCAKSR 529
Cdd:cd18039      1 ELNHSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVDQLTEKIHQTGLKVVRLCAKSR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  530 EAIDSPVSFLALHNQIRNMDSMPELQKLQQLKDETGELSSSDEKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKMQ 609
Cdd:cd18039     81 EAVESPVSFLALHNQVRNLDSAEKLELLKLLKLETGELSSADEKRYRKLKRKAERELLRNADVICCTCVGAGDPRLSKMK 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2085193927  610 FRSILIDESTQATEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQYR 683
Cdd:cd18039    161 FRTVLIDEATQATEPECLIPLVHGAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVQLGIRPIRLQVQYR 234
UPF1_Zn_bind pfam09416
RNA helicase (UPF2 interacting domain); UPF1 is an essential RNA helicase that detects mRNAs ...
100-251 9.33e-117

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: 356.56  E-value: 9.33e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  100 HACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKCKEVTLHKDGPLGETVLECYNCGCRNVFLLGFIPAK 179
Cdd:pfam09416    1 HACAYCGIHDPACVVKCLTCGKWFCNGRGNTSGSHIINHLVRSKHKEVSLHPDSPLGDTVLECYNCGSKNVFLLGFIPAK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2085193927  180 ADSVVVLLCRQPCASQSSLKDINWDSSQWQPLIQDRCFLSWLVKIPSEQEQLRARQITAQQINKLEELWKEN 251
Cdd:pfam09416   81 SDSVVVLLCRQPCAQAKSLKDMNWDTSQWQPLIEDRQFLPWLVKVPSEEEQLRARQITPAQINKLEELWKDN 152
TIGR00376 super family cl36628
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
358-880 3.66e-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: 294.80  E-value: 3.66e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  358 GHVIKVPDNYgdeIAIELRSSAgaPVEVPHNFQVDFVWKSTSFDRMQSALKTFAVDETSVSGyiyhKLLGHEVEDVIIKC 437
Cdd:TIGR00376   78 GVVTRVGKRF---ITVALEESV--PQWSLKRVRIDLYANDVTFKRMKEALRALTENHSRLLE----FLLGREAPSKASEI 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  438 QLPKRFTaqglPDLNHSQVYAVK-TVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNgPVLVCAPSNIAVDQLTEKIHQ 516
Cdd:TIGR00376  149 HDFQFFD----PNLNESQKEAVLfALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGL-RVLVTAPSNIAVDNLLERLAL 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  517 TGLKVVRLCAKSR-------------------------------EAIDSPVSFLALHNQIRNmdSMPELQKLQQLKDETG 565
Cdd:TIGR00376  224 CDQKIVRLGHPARllksnkqhsldylienhpkyqivadirekidELIEERNKKTKPSPQKRR--GLSDIKILRKALKKRE 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  566 ----------------ELSSSDEKRYRALKRTAER---ELLMNADViccTCVGAGDPRLAKMQFRSILIDESTQATEPEC 626
Cdd:TIGR00376  302 argieslkiasmaewiETNKSIDRLLKLLPESEERimnEILAESDA---TNSMAGSEILNGQYFDVAVIDEASQAMEPSC 378
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  627 MVPVVlGAKQLILVGDHCQLGPVVMCKKAAkaGLSQSLFERLVVL-GIRPIRLQVQYRMHPALSAFPSNIFYEGSLQNGV 705
Cdd:TIGR00376  379 LIPLL-KARKLILAGDHKQLPPTILSHDAE--ELSLTLFERLIKEyPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHE 455
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  706 TAADRIKKGFDFQWPQPDK-------PMFFYVTQGQE----EIASSgTSYLNRTEAANVEKITTRLLKAGAKPDQIGIIT 774
Cdd:TIGR00376  456 SVANILLRDLPKVEATESEddletgiPLLFIDTSGCElfelKEADS-TSKYNPGEAELVSEIIQALVKMGVPANDIGVIT 534
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  775 PYEGQRSYLVQYMQFSgslHTklyqEVEIASVDAFQGREKDFIILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVG 854
Cdd:TIGR00376  535 PYDAQVDLLRQLLEHR---HI----DIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIG 607
                          570       580
                   ....*....|....*....|....*.
gi 2085193927  855 NPKALSKQPLWNHLLNYYKEQKVLVE 880
Cdd:TIGR00376  608 DSRTLSNHKFYKRLIEWCKQHGEVRE 633
1B_UPF1-like cd21407
1B domain of eukaryotic UPF1 RNA helicase and related proteins; Helicases catalyze ...
304-393 1.14e-52

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: 178.88  E-value: 1.14e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  304 TQDNITVRWDLGLNKKRIAYFTLPKTDSGDMRLMQGDEICLRYKGDMAPLWKGIGHVIKVPDNYGDEIAIELRSSAGAPV 383
Cdd:cd21407      1 TQENISVRWDVGLNKKRLAYFTLPKLDESELRLMVGDELRLRYKGDLREPWEGVGHVIKIPDNYSEEVALELRSSKNAPT 80
                           90
                   ....*....|
gi 2085193927  384 EVPHNFQVDF 393
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 ...
450-683 1.13e-176

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: 516.03  E-value: 1.13e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  450 DLNHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLKVVRLCAKSR 529
Cdd:cd18039      1 ELNHSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVDQLTEKIHQTGLKVVRLCAKSR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  530 EAIDSPVSFLALHNQIRNMDSMPELQKLQQLKDETGELSSSDEKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKMQ 609
Cdd:cd18039     81 EAVESPVSFLALHNQVRNLDSAEKLELLKLLKLETGELSSADEKRYRKLKRKAERELLRNADVICCTCVGAGDPRLSKMK 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2085193927  610 FRSILIDESTQATEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQYR 683
Cdd:cd18039    161 FRTVLIDEATQATEPECLIPLVHGAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVQLGIRPIRLQVQYR 234
UPF1_Zn_bind pfam09416
RNA helicase (UPF2 interacting domain); UPF1 is an essential RNA helicase that detects mRNAs ...
100-251 9.33e-117

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: 356.56  E-value: 9.33e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  100 HACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKCKEVTLHKDGPLGETVLECYNCGCRNVFLLGFIPAK 179
Cdd:pfam09416    1 HACAYCGIHDPACVVKCLTCGKWFCNGRGNTSGSHIINHLVRSKHKEVSLHPDSPLGDTVLECYNCGSKNVFLLGFIPAK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2085193927  180 ADSVVVLLCRQPCASQSSLKDINWDSSQWQPLIQDRCFLSWLVKIPSEQEQLRARQITAQQINKLEELWKEN 251
Cdd:pfam09416   81 SDSVVVLLCRQPCAQAKSLKDMNWDTSQWQPLIEDRQFLPWLVKVPSEEEQLRARQITPAQINKLEELWKDN 152
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
358-880 3.66e-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: 294.80  E-value: 3.66e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  358 GHVIKVPDNYgdeIAIELRSSAgaPVEVPHNFQVDFVWKSTSFDRMQSALKTFAVDETSVSGyiyhKLLGHEVEDVIIKC 437
Cdd:TIGR00376   78 GVVTRVGKRF---ITVALEESV--PQWSLKRVRIDLYANDVTFKRMKEALRALTENHSRLLE----FLLGREAPSKASEI 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  438 QLPKRFTaqglPDLNHSQVYAVK-TVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNgPVLVCAPSNIAVDQLTEKIHQ 516
Cdd:TIGR00376  149 HDFQFFD----PNLNESQKEAVLfALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGL-RVLVTAPSNIAVDNLLERLAL 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  517 TGLKVVRLCAKSR-------------------------------EAIDSPVSFLALHNQIRNmdSMPELQKLQQLKDETG 565
Cdd:TIGR00376  224 CDQKIVRLGHPARllksnkqhsldylienhpkyqivadirekidELIEERNKKTKPSPQKRR--GLSDIKILRKALKKRE 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  566 ----------------ELSSSDEKRYRALKRTAER---ELLMNADViccTCVGAGDPRLAKMQFRSILIDESTQATEPEC 626
Cdd:TIGR00376  302 argieslkiasmaewiETNKSIDRLLKLLPESEERimnEILAESDA---TNSMAGSEILNGQYFDVAVIDEASQAMEPSC 378
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  627 MVPVVlGAKQLILVGDHCQLGPVVMCKKAAkaGLSQSLFERLVVL-GIRPIRLQVQYRMHPALSAFPSNIFYEGSLQNGV 705
Cdd:TIGR00376  379 LIPLL-KARKLILAGDHKQLPPTILSHDAE--ELSLTLFERLIKEyPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHE 455
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  706 TAADRIKKGFDFQWPQPDK-------PMFFYVTQGQE----EIASSgTSYLNRTEAANVEKITTRLLKAGAKPDQIGIIT 774
Cdd:TIGR00376  456 SVANILLRDLPKVEATESEddletgiPLLFIDTSGCElfelKEADS-TSKYNPGEAELVSEIIQALVKMGVPANDIGVIT 534
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  775 PYEGQRSYLVQYMQFSgslHTklyqEVEIASVDAFQGREKDFIILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVG 854
Cdd:TIGR00376  535 PYDAQVDLLRQLLEHR---HI----DIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIG 607
                          570       580
                   ....*....|....*....|....*.
gi 2085193927  855 NPKALSKQPLWNHLLNYYKEQKVLVE 880
Cdd:TIGR00376  608 DSRTLSNHKFYKRLIEWCKQHGEVRE 633
ZBD_UPF1-like cd21400
Cys/His rich zinc-binding domain (CH/ZBD) of eukaryotic UPF1 RNA helicase and related proteins; ...
101-221 6.24e-85

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: 269.89  E-value: 6.24e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  101 ACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKCKEVTLHKDGPLGETVLECYNCGCRNVFLLGFIPAKA 180
Cdd:cd21400      1 ACAYCGIHDPACLVKCLTCGKWFCNGRGNTSGSHIVQHLVRSKHKEVSLHPDSPLGDTVLECYNCGSRNVFLLGFIPAKA 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2085193927  181 DSVVVLLCRQPCASQSSlKDINWDSSQWQPLIQDRCFLSWL 221
Cdd:cd21400     81 DSVVVLLCRQPCLSQSS-KDMNWDLSQWQPLIDDRQFLPWL 120
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
684-873 2.05e-81

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: 262.94  E-value: 2.05e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  684 MHPALSAFPSNIFYEGSLQNGVTAADRIkkgFDFQWPQPDKPMFFYVTQGQEEIASSGTSYLNRTEAANVEKITTRLLKA 763
Cdd:cd18808      1 MHPEISEFPSKLFYEGKLKAGVSVAARL---NPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKS 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  764 GAKPDQIGIITPYEGQRSYLVQYMQFSGSlhtkLYQEVEIASVDAFQGREKDFIILSCVRANEHQG-IGFLNDPRRLNVA 842
Cdd:cd18808     78 GVKPSSIGVITPYRAQVALIRELLRKRGG----LLEDVEVGTVDNFQGREKDVIILSLVRSNESGGsIGFLSDPRRLNVA 153
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2085193927  843 LTRARYGVIIVGNPKALSKQPLWNHLLNYYK 873
Cdd:cd18808    154 LTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
660-857 4.09e-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: 257.09  E-value: 4.09e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  660 LSQSLFERLVVLG-IRPIRLQVQYRMHPALSAFPSNIFYEGSLQNGVTAADRIKKGfDFQWPQPDKPMFFY-VTQGQEEI 737
Cdd:pfam13087    1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPD-DFHLPDPLGPLVFIdVDGSEEEE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  738 ASSGTSYLNRTEAANVEKITTRLLKAGAKPD-QIGIITPYEGQRSYLVQYmqFSGSLHTKLyqEVEIASVDAFQGREKDF 816
Cdd:pfam13087   80 SDGGTSYSNEAEAELVVQLVEKLIKSGPEEPsDIGVITPYRAQVRLIRKL--LKRKLGGKL--EIEVNTVDGFQGREKDV 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2085193927  817 IILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVGNPK 857
Cdd:pfam13087  156 IIFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNAK 196
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
553-875 1.90e-71

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 255.05  E-value: 1.90e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  553 ELQKLQQLKDETGELSSSDEKRyRALKRTAERELLMNADVICCTCVGAGD-PRLAKMQFRSILIDESTQATEPECMVPVV 631
Cdd:COG1112    499 LIAELREAARLRRALRRELKKR-RELRKLLWDALLELAPVVGMTPASVARlLPLGEGSFDLVIIDEASQATLAEALGALA 577
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  632 LgAKQLILVGDHCQLGPVVMC---KKAAKAGLSQSLFERLV-VLGIRPIRLQVQYRMHPALSAFPSNIFYEGSLQNGVTA 707
Cdd:COG1112    578 R-AKRVVLVGDPKQLPPVVFGeeaEEVAEEGLDESLLDRLLaRLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSP 656
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  708 ADRikkgfdfQWPQPDKPMFFYVTQGQEEiaSSGTSYLNRTEAANVEKITTRLLKAGAKPDQIGIITPYEGQRSYLVQYM 787
Cdd:COG1112    657 KAR-------RLADPDSPLVFIDVDGVYE--RRGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRELL 727
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  788 QfsgSLHTKLYQEVEIASVDAFQGREKDFIILSCVRANEH---QGIGFLN-DPRRLNVALTRARYGVIIVGNPKALSKQP 863
Cdd:COG1112    728 R---EALGDGLEPVFVGTVDRFQGDERDVIIFSLVYSNDEdvpRNFGFLNgGPRRLNVAVSRARRKLIVVGSRELLDSDP 804
                          330
                   ....*....|....*
gi 2085193927  864 ---LWNHLLNYYKEQ 875
Cdd:COG1112    805 stpALKRLLEYLERA 819
1B_UPF1-like cd21407
1B domain of eukaryotic UPF1 RNA helicase and related proteins; Helicases catalyze ...
304-393 1.14e-52

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: 178.88  E-value: 1.14e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  304 TQDNITVRWDLGLNKKRIAYFTLPKTDSGDMRLMQGDEICLRYKGDMAPLWKGIGHVIKVPDNYGDEIAIELRSSAGAPV 383
Cdd:cd21407      1 TQENISVRWDVGLNKKRLAYFTLPKLDESELRLMVGDELRLRYKGDLREPWEGVGHVIKIPDNYSEEVALELRSSKNAPT 80
                           90
                   ....*....|
gi 2085193927  384 EVPHNFQVDF 393
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 ...
454-651 1.79e-49

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: 176.00  E-value: 1.79e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  454 SQVYAVKTVLQRP-LSLIQGPPGTGKTVTsatIVYHLARQGNGP---------VLVCAPSNIAVDQLTEKIHQTG----L 519
Cdd:pfam13086    1 SQREAIRSALSSShFTLIQGPPGTGKTTT---IVELIRQLLSYPatsaaagprILVCAPSNAAVDNILERLLRKGqkygP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  520 KVVRLCAKsrEAIDSPVSFLALHNQIRNMDSMPEL------------------------------------------QKL 557
Cdd:pfam13086   78 KIVRIGHP--AAISEAVLPVSLDYLVESKLNNEEDaqivkdiskeleklakalrafekeiivekllksrnkdkskleQER 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  558 QQLKDETGELSssdeKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKM-QFRSILIDESTQATEPECMVPVVLGAKQ 636
Cdd:pfam13086  156 RKLRSERKELR----KELRRREQSLEREILDEAQIVCSTLSGAGSRLLSSLaNFDVVIIDEAAQALEPSTLIPLLRGPKK 231
                          250
                   ....*....|....*
gi 2085193927  637 LILVGDHCQLGPVVM 651
Cdd:pfam13086  232 VVLVGDPKQLPPTVI 246
UPF1_1B_dom pfam18141
RNA helicase UPF1, 1B domain; UPF1 (or regulator of nonsense transcripts 1 homolog) is an ...
303-394 9.02e-45

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: 156.32  E-value: 9.02e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  303 QTQDNITVRWDLGLNKKRIAYFTLPKTDSGDMRLMQGDEICLRYKGDMAPLWKGIGHVIKVPDNYGDEIAIELRSSA-GA 381
Cdd:pfam18141    1 QTQDDISVRWDVGLNKKHLAWFSLPKLDSGEMKLAVGDELRLRYTGSLAEPWEGVGHVVKIPDNSSEEVTLELRSSSnNP 80
                           90
                   ....*....|...
gi 2085193927  382 PVEVPHNFQVDFV 394
Cdd:pfam18141   81 PTDLTHGFTVEFV 93
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
407-861 1.29e-16

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: 84.26  E-value: 1.29e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  407 LKTFAVDETSVSGYIyHKLLGHEVEDVIIKCQLPKRFTAQGLpDLNHSQVYAVKTVL-QRPLSLIQGPPGTGKTVTSATI 485
Cdd:COG0507     83 LTRLLEAEQRLARRL-RRLARPALDEADVEAALAALEPRAGI-TLSDEQREAVALALtTRRVSVLTGGAGTGKTTTLRAL 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  486 VYHLARQGnGPVLVCAPSNIAVDQLTEKIhqtglkvvrlcakSREAidspvsfLALHnqirnmdsmpelQKLQQLKDETG 565
Cdd:COG0507    161 LAALEALG-LRVALAAPTGKAAKRLSEST-------------GIEA-------RTIH------------RLLGLRPDSGR 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  566 elsssdekryralKRTAERELLMNADVicctcvgagdprlakmqfrsILIDESTqatepecMVPVVLGAK---------- 635
Cdd:COG0507    208 -------------FRHNRDNPLTPADL--------------------LVVDEAS-------MVDTRLMAAllealpraga 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  636 QLILVGDHCQLGPVVmckkaakAGlsqSLFERLVVLGIRP-IRLQVQYRMhpalsAFPSNIfyegslqngVTAADRIKKG 714
Cdd:COG0507    248 RLILVGDPDQLPSVG-------AG---AVLRDLIESGTVPvVELTEVYRQ-----ADDSRI---------IELAHAIREG 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  715 -FDFQWPQPDKPMFFYVTQGQEEIASS-----------------------GTSYLNR----------TEAANVEKITTRL 760
Cdd:COG0507    304 dAPEALNARYADVVFVEAEDAEEAAEAivelyadrpaggediqvlaptnaGVDALNQairealnpagELERELAEDGELE 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  761 LKAGAK-------PD------QIGIITPYEGQRSYLVqyMQFSGSLHTKlYQEVEIASVD-AF-------QGREKD--FI 817
Cdd:COG0507    384 LYVGDRvmftrndYDlgvfngDIGTVLSIDEDEGRLT--VRFDGREIVT-YDPSELDQLElAYaitvhksQGSTFDrvIL 460
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 2085193927  818 ILScvraNEHQGigfLNDPRRLNVALTRARYGVIIVGNPKALSK 861
Cdd:COG0507    461 VLP----SEHSP---LLSRELLYTALTRARELLTLVGDRDALAR 497
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
417-649 2.03e-07

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: 55.15  E-value: 2.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  417 VSGYIYHKLLGHEVEDVIIKCQ--LPKRFTAQGLPDLNHS---------QVYAVKTVLQRPLSLIQGPPGTGKTVTSATI 485
Cdd:TIGR01447  100 CDGRLYLRRYWREEEKLAAKLRtlLEARKRTAPSAILENLfpllneqnwRKTAVALALKSNFSLITGGPGTGKTTTVARL 179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  486 VYHLARQ----GNGPVLVCAPSNIAVDQLTEKIHQtglKVVRLCAKSREAIDSPVSFLALHnqirnmdsmpelqKLQQLK 561
Cdd:TIGR01447  180 LLALVKQspkqGKLRIALAAPTGKAAARLAESLRK---AVKNLAAAEALIAALPSEAVTIH-------------RLLGIK 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  562 detgelssSDEKRYRALKRTAerellMNADVicctcvgagdprlakmqfrsILIDESTQATEP--ECMVPVVLGAKQLIL 639
Cdd:TIGR01447  244 --------PDTKRFRHHERNP-----LPLDV--------------------LVVDEASMVDLPlmAKLLKALPPNTKLIL 290
                          250
                   ....*....|
gi 2085193927  640 VGDHCQLGPV 649
Cdd:TIGR01447  291 LGDKNQLPSV 300
DEXDc smart00487
DEAD-like helicases superfamily;
455-514 3.72e-06

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 49.03  E-value: 3.72e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2085193927   455 QVYAVKTVLQRPLS-LIQGPPGTGKTVTSAT-IVYHLARQGNGPVLVCAPSNIAVDQLTEKI 514
Cdd:smart00487   13 QKEAIEALLSGLRDvILAAPTGSGKTLAALLpALEALKRGKGGRVLVLVPTRELAEQWAEEL 74
 
Name Accession Description Interval E-value
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
450-683 1.13e-176

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: 516.03  E-value: 1.13e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  450 DLNHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLKVVRLCAKSR 529
Cdd:cd18039      1 ELNHSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVDQLTEKIHQTGLKVVRLCAKSR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  530 EAIDSPVSFLALHNQIRNMDSMPELQKLQQLKDETGELSSSDEKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKMQ 609
Cdd:cd18039     81 EAVESPVSFLALHNQVRNLDSAEKLELLKLLKLETGELSSADEKRYRKLKRKAERELLRNADVICCTCVGAGDPRLSKMK 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2085193927  610 FRSILIDESTQATEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQYR 683
Cdd:cd18039    161 FRTVLIDEATQATEPECLIPLVHGAKQVILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVQLGIRPIRLQVQYR 234
UPF1_Zn_bind pfam09416
RNA helicase (UPF2 interacting domain); UPF1 is an essential RNA helicase that detects mRNAs ...
100-251 9.33e-117

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: 356.56  E-value: 9.33e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  100 HACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKCKEVTLHKDGPLGETVLECYNCGCRNVFLLGFIPAK 179
Cdd:pfam09416    1 HACAYCGIHDPACVVKCLTCGKWFCNGRGNTSGSHIINHLVRSKHKEVSLHPDSPLGDTVLECYNCGSKNVFLLGFIPAK 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2085193927  180 ADSVVVLLCRQPCASQSSLKDINWDSSQWQPLIQDRCFLSWLVKIPSEQEQLRARQITAQQINKLEELWKEN 251
Cdd:pfam09416   81 SDSVVVLLCRQPCAQAKSLKDMNWDTSQWQPLIEDRQFLPWLVKVPSEEEQLRARQITPAQINKLEELWKDN 152
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
358-880 3.66e-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: 294.80  E-value: 3.66e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  358 GHVIKVPDNYgdeIAIELRSSAgaPVEVPHNFQVDFVWKSTSFDRMQSALKTFAVDETSVSGyiyhKLLGHEVEDVIIKC 437
Cdd:TIGR00376   78 GVVTRVGKRF---ITVALEESV--PQWSLKRVRIDLYANDVTFKRMKEALRALTENHSRLLE----FLLGREAPSKASEI 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  438 QLPKRFTaqglPDLNHSQVYAVK-TVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNgPVLVCAPSNIAVDQLTEKIHQ 516
Cdd:TIGR00376  149 HDFQFFD----PNLNESQKEAVLfALSSKDLFLIHGPPGTGKTRTVVELIRQLVKRGL-RVLVTAPSNIAVDNLLERLAL 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  517 TGLKVVRLCAKSR-------------------------------EAIDSPVSFLALHNQIRNmdSMPELQKLQQLKDETG 565
Cdd:TIGR00376  224 CDQKIVRLGHPARllksnkqhsldylienhpkyqivadirekidELIEERNKKTKPSPQKRR--GLSDIKILRKALKKRE 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  566 ----------------ELSSSDEKRYRALKRTAER---ELLMNADViccTCVGAGDPRLAKMQFRSILIDESTQATEPEC 626
Cdd:TIGR00376  302 argieslkiasmaewiETNKSIDRLLKLLPESEERimnEILAESDA---TNSMAGSEILNGQYFDVAVIDEASQAMEPSC 378
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  627 MVPVVlGAKQLILVGDHCQLGPVVMCKKAAkaGLSQSLFERLVVL-GIRPIRLQVQYRMHPALSAFPSNIFYEGSLQNGV 705
Cdd:TIGR00376  379 LIPLL-KARKLILAGDHKQLPPTILSHDAE--ELSLTLFERLIKEyPERSRTLNVQYRMNQKIMEFPSREFYNGKLTAHE 455
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  706 TAADRIKKGFDFQWPQPDK-------PMFFYVTQGQE----EIASSgTSYLNRTEAANVEKITTRLLKAGAKPDQIGIIT 774
Cdd:TIGR00376  456 SVANILLRDLPKVEATESEddletgiPLLFIDTSGCElfelKEADS-TSKYNPGEAELVSEIIQALVKMGVPANDIGVIT 534
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  775 PYEGQRSYLVQYMQFSgslHTklyqEVEIASVDAFQGREKDFIILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVG 854
Cdd:TIGR00376  535 PYDAQVDLLRQLLEHR---HI----DIEVSSVDGFQGREKEVIIISFVRSNRKGEVGFLKDLRRLNVALTRARRKLIVIG 607
                          570       580
                   ....*....|....*....|....*.
gi 2085193927  855 NPKALSKQPLWNHLLNYYKEQKVLVE 880
Cdd:TIGR00376  608 DSRTLSNHKFYKRLIEWCKQHGEVRE 633
ZBD_UPF1-like cd21400
Cys/His rich zinc-binding domain (CH/ZBD) of eukaryotic UPF1 RNA helicase and related proteins; ...
101-221 6.24e-85

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: 269.89  E-value: 6.24e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  101 ACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKCKEVTLHKDGPLGETVLECYNCGCRNVFLLGFIPAKA 180
Cdd:cd21400      1 ACAYCGIHDPACLVKCLTCGKWFCNGRGNTSGSHIVQHLVRSKHKEVSLHPDSPLGDTVLECYNCGSRNVFLLGFIPAKA 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2085193927  181 DSVVVLLCRQPCASQSSlKDINWDSSQWQPLIQDRCFLSWL 221
Cdd:cd21400     81 DSVVVLLCRQPCLSQSS-KDMNWDLSQWQPLIDDRQFLPWL 120
SF1_C_Upf1 cd18808
C-terminal helicase domain of Upf1-like family helicases; The Upf1-like helicase family ...
684-873 2.05e-81

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: 262.94  E-value: 2.05e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  684 MHPALSAFPSNIFYEGSLQNGVTAADRIkkgFDFQWPQPDKPMFFYVTQGQEEIASSGTSYLNRTEAANVEKITTRLLKA 763
Cdd:cd18808      1 MHPEISEFPSKLFYEGKLKAGVSVAARL---NPPPLPGPSKPLVFVDVSGGEEREESGTSKSNEAEAELVVELVKYLLKS 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  764 GAKPDQIGIITPYEGQRSYLVQYMQFSGSlhtkLYQEVEIASVDAFQGREKDFIILSCVRANEHQG-IGFLNDPRRLNVA 842
Cdd:cd18808     78 GVKPSSIGVITPYRAQVALIRELLRKRGG----LLEDVEVGTVDNFQGREKDVIILSLVRSNESGGsIGFLSDPRRLNVA 153
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2085193927  843 LTRARYGVIIVGNPKALSKQPLWNHLLNYYK 873
Cdd:cd18808    154 LTRAKRGLIIVGNPDTLSKDPLWKKLLEYLE 184
AAA_12 pfam13087
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
660-857 4.09e-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: 257.09  E-value: 4.09e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  660 LSQSLFERLVVLG-IRPIRLQVQYRMHPALSAFPSNIFYEGSLQNGVTAADRIKKGfDFQWPQPDKPMFFY-VTQGQEEI 737
Cdd:pfam13087    1 LDRSLFERLQELGpSAVVMLDTQYRMHPEIMEFPSKLFYGGKLKDGPSVAERPLPD-DFHLPDPLGPLVFIdVDGSEEEE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  738 ASSGTSYLNRTEAANVEKITTRLLKAGAKPD-QIGIITPYEGQRSYLVQYmqFSGSLHTKLyqEVEIASVDAFQGREKDF 816
Cdd:pfam13087   80 SDGGTSYSNEAEAELVVQLVEKLIKSGPEEPsDIGVITPYRAQVRLIRKL--LKRKLGGKL--EIEVNTVDGFQGREKDV 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2085193927  817 IILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVGNPK 857
Cdd:pfam13087  156 IIFSCVRSNEKGGIGFLSDPRRLNVALTRAKRGLIIVGNAK 196
DNA2 COG1112
Superfamily I DNA and/or RNA helicase [Replication, recombination and repair];
553-875 1.90e-71

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


Pssm-ID: 440729 [Multi-domain]  Cd Length: 819  Bit Score: 255.05  E-value: 1.90e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  553 ELQKLQQLKDETGELSSSDEKRyRALKRTAERELLMNADVICCTCVGAGD-PRLAKMQFRSILIDESTQATEPECMVPVV 631
Cdd:COG1112    499 LIAELREAARLRRALRRELKKR-RELRKLLWDALLELAPVVGMTPASVARlLPLGEGSFDLVIIDEASQATLAEALGALA 577
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  632 LgAKQLILVGDHCQLGPVVMC---KKAAKAGLSQSLFERLV-VLGIRPIRLQVQYRMHPALSAFPSNIFYEGSLQNGVTA 707
Cdd:COG1112    578 R-AKRVVLVGDPKQLPPVVFGeeaEEVAEEGLDESLLDRLLaRLPERGVMLREHYRMHPEIIAFSNRLFYDGKLVPLPSP 656
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  708 ADRikkgfdfQWPQPDKPMFFYVTQGQEEiaSSGTSYLNRTEAANVEKITTRLLKAGAKPDQIGIITPYEGQRSYLVQYM 787
Cdd:COG1112    657 KAR-------RLADPDSPLVFIDVDGVYE--RRGGSRTNPEEAEAVVELVRELLEDGPDGESIGVITPYRAQVALIRELL 727
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  788 QfsgSLHTKLYQEVEIASVDAFQGREKDFIILSCVRANEH---QGIGFLN-DPRRLNVALTRARYGVIIVGNPKALSKQP 863
Cdd:COG1112    728 R---EALGDGLEPVFVGTVDRFQGDERDVIIFSLVYSNDEdvpRNFGFLNgGPRRLNVAVSRARRKLIVVGSRELLDSDP 804
                          330
                   ....*....|....*
gi 2085193927  864 ---LWNHLLNYYKEQ 875
Cdd:COG1112    805 stpALKRLLEYLERA 819
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
451-683 6.79e-53

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: 183.58  E-value: 6.79e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  451 LNHSQVYAVKTVL-QRPLSLIQGPPGTGKTVTSATIVYHLARQGNgPVLVCAPSNIAVDQLTEKIHQTGLKVVRLcaksr 529
Cdd:cd18044      2 LNDSQKEAVKFALsQKDVALIHGPPGTGKTTTVVEIILQAVKRGE-KVLACAPSNIAVDNLVERLVALKVKVVRI----- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  530 eaidspvsflalHNQIRNMDSMpelqklqqlkdetgelsssdekryraLKRTAERelLMNADVICCTCVGAGDPRLAK-M 608
Cdd:cd18044     76 ------------GHPARLLESV--------------------------LDHSLDA--LVAAQVVLATNTGAGSRQLLPnE 115
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2085193927  609 QFRSILIDESTQATEPECMVPVvLGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPI--RLQVQYR 683
Cdd:cd18044    116 LFDVVVIDEAAQALEASCWIPL-LKARRCILAGDHKQLPPTILSDKAARGGLGVTLFERLVNLYGESVvrMLTVQYR 191
1B_UPF1-like cd21407
1B domain of eukaryotic UPF1 RNA helicase and related proteins; Helicases catalyze ...
304-393 1.14e-52

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: 178.88  E-value: 1.14e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  304 TQDNITVRWDLGLNKKRIAYFTLPKTDSGDMRLMQGDEICLRYKGDMAPLWKGIGHVIKVPDNYGDEIAIELRSSAGAPV 383
Cdd:cd21407      1 TQENISVRWDVGLNKKRLAYFTLPKLDESELRLMVGDELRLRYKGDLREPWEGVGHVIKIPDNYSEEVALELRSSKNAPT 80
                           90
                   ....*....|
gi 2085193927  384 EVPHNFQVDF 393
Cdd:cd21407     81 EITTGFSVEF 90
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
451-683 5.72e-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: 178.10  E-value: 5.72e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  451 LNHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLA------------RQGNGPVLVCAPSNIAVDQLTEKIHQT- 517
Cdd:cd18040      2 LNPSQNHAVRTALTKPFTLIQGPPGTGKTVTGVHIAYWFAkqnreiqsvsgeGDGGPCVLYCGPSNKSVDVVAELLLKVp 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  518 GLKVVRLCAKSREAIDSPV---------------------SFLALHNQIRNmDSMPELQKLQQ----LKDETGELSSSDE 572
Cdd:cd18040     82 GLKILRVYSEQIETTEYPIpneprhpnkksereskpnselSSITLHHRIRQ-PSNPHSQQIKAfearFERTQEKITEEDI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  573 KRYRALKRTAERELLMNADVICCTCVGAGDPRL-AKMQFRSILIDESTQATEPECMVPVVLG--AKQLILVGDHCQLGPV 649
Cdd:cd18040    161 KTYKILIWEARFEELETVDVILCTCSEAASQKMrTHANVKQCIVDECGMCTEPESLIPIVSAprAEQVVLIGDHKQLRPV 240
                          250       260       270
                   ....*....|....*....|....*....|....
gi 2085193927  650 VMCKKAAKAGLSQSLFERLVVlgiRPIRLQVQYR 683
Cdd:cd18040    241 VQNKEAQKLGLGRSLFERYAE---KACMLDTQYR 271
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
454-651 1.79e-49

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: 176.00  E-value: 1.79e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  454 SQVYAVKTVLQRP-LSLIQGPPGTGKTVTsatIVYHLARQGNGP---------VLVCAPSNIAVDQLTEKIHQTG----L 519
Cdd:pfam13086    1 SQREAIRSALSSShFTLIQGPPGTGKTTT---IVELIRQLLSYPatsaaagprILVCAPSNAAVDNILERLLRKGqkygP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  520 KVVRLCAKsrEAIDSPVSFLALHNQIRNMDSMPEL------------------------------------------QKL 557
Cdd:pfam13086   78 KIVRIGHP--AAISEAVLPVSLDYLVESKLNNEEDaqivkdiskeleklakalrafekeiivekllksrnkdkskleQER 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  558 QQLKDETGELSssdeKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKM-QFRSILIDESTQATEPECMVPVVLGAKQ 636
Cdd:pfam13086  156 RKLRSERKELR----KELRRREQSLEREILDEAQIVCSTLSGAGSRLLSSLaNFDVVIIDEAAQALEPSTLIPLLRGPKK 231
                          250
                   ....*....|....*
gi 2085193927  637 LILVGDHCQLGPVVM 651
Cdd:pfam13086  232 VVLVGDPKQLPPTVI 246
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
451-668 8.43e-48

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: 170.11  E-value: 8.43e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  451 LNHSQVYAVKTVLQR----PLSLIQGPPGTGKTVTSATIVYHLARQGNGP-VLVCAPSNIAVDQLTEKIHQTGLK---VV 522
Cdd:cd18038      2 LNDEQKLAVRNIVTGtsrpPPYIIFGPPGTGKTVTLVEAILQVLRQPPEArILVCAPSNSAADLLAERLLNALVTkreIL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  523 RLCAKSREAIDSPvsflalhnqirnmdsmPELQKLQqlkdetgelSSSDEKRYRalkrTAERELLMNADVICCTCVGAGd 602
Cdd:cd18038     82 RLNAPSRDRASVP----------------PELLPYC---------NSKAEGTFR----LPSLEELKKYRIVVCTLMTAG- 131
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2085193927  603 pRLAKMQ-----FRSILIDESTQATEPECMVPVVLGAK---QLILVGDHCQLGPVVMCKKAAKAGLSQSLFERL 668
Cdd:cd18038    132 -RLVQAGvpnghFTHIFIDEAGQATEPEALIPLSELASkntQIVLAGDPKQLGPVVRSPLARKYGLGKSLLERL 204
UPF1_1B_dom pfam18141
RNA helicase UPF1, 1B domain; UPF1 (or regulator of nonsense transcripts 1 homolog) is an ...
303-394 9.02e-45

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: 156.32  E-value: 9.02e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  303 QTQDNITVRWDLGLNKKRIAYFTLPKTDSGDMRLMQGDEICLRYKGDMAPLWKGIGHVIKVPDNYGDEIAIELRSSA-GA 381
Cdd:pfam18141    1 QTQDDISVRWDVGLNKKHLAWFSLPKLDSGEMKLAVGDELRLRYTGSLAEPWEGVGHVVKIPDNSSEEVTLELRSSSnNP 80
                           90
                   ....*....|...
gi 2085193927  382 PVEVPHNFQVDFV 394
Cdd:pfam18141   81 PTDLTHGFTVEFV 93
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
451-683 3.70e-43

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: 156.60  E-value: 3.70e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  451 LNHSQVYAVKTVLQR--PLSLIQGPPGTGKTVTSATIVYHL-----------------ARQGNGP-------VLVCAPSN 504
Cdd:cd18042      1 LNESQLEAIASALQNspGITLIQGPPGTGKTKTIVGILSVLlagkyrkyyekvkkklrKLQRNLNnkkkknrILVCAPSN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  505 IAVDQLTEKIHQTGL----------KVVRLcaksreaidspvsflalhnqirnmdsmpelqklqqlkdetGelsssdekr 574
Cdd:cd18042     81 AAVDEIVLRLLSEGFldgdgrsykpNVVRV----------------------------------------G--------- 111
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  575 yralKRTAERELLMNADVICCTCVGAGDPRLAKMQ--FRSILIDESTQATEPECMVPVVLGAKQLILVGDHCQLGPVVMC 652
Cdd:cd18042    112 ----RQELRASILNEADIVCTTLSSSGSDLLESLPrgFDTVIIDEAAQAVELSTLIPLRLGCKRLILVGDPKQLPATVFS 187
                          250       260       270
                   ....*....|....*....|....*....|.
gi 2085193927  653 KKAAKAGLSQSLFERLVVLGIRPIRLQVQYR 683
Cdd:cd18042    188 KVAQKLGYDRSLFERLQLAGYPVLMLTTQYR 218
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
451-683 2.05e-39

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: 145.07  E-value: 2.05e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  451 LNHSQVYAVKTVLQ-RPLSLIQGPPGTGKTVTSATIVYHLARQGNGpVLVCAPSNIAVDQLTEKIHQTGLKVVRLCAKSR 529
Cdd:cd18041      2 LNKDQRQAIKKVLNaKDYALILGMPGTGKTTTIAALVRILVALGKS-VLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  530 eaIDSPVSFLALHNQIRNMDSMPELQklqqlkdetgelsssdekryralkrtaerELLMNADVICCTCVGAGDPRLAKMQ 609
Cdd:cd18041     81 --IHPDVQEFTLEAILKSCKSVEELE-----------------------------SKYESVSVVATTCLGINHPIFRRRT 129
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2085193927  610 FRSILIDESTQATEPECMVPVVLgAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIR-LQVQYR 683
Cdd:cd18041    130 FDYCIVDEASQITLPICLGPLRL-AKKFVLVGDHYQLPPLVKSREARELGMDESLFKRLSEAHPDAVVqLTIQYR 203
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
450-669 2.78e-32

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: 125.56  E-value: 2.78e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  450 DLNHSQVYAVKTVLQ---RPLS-LIQGPPGTGKTVTSA----TIVYHLARQgngPVLVCAPSNIAVDQLTEKIHQTGLKV 521
Cdd:cd18078      1 DLNELQKEAVKRILGgecRPLPyILFGPPGTGKTVTIIeailQVVYNLPRS---RILVCAPSNSAADLVTSRLHESKVLK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  522 VRLCAKsreaidspvsfLALHNQIRNMDSmpelqklqqlkdetgelsssdEKRYRALKRTAERELLMNADVICCTCVGAG 601
Cdd:cd18078     78 PGDMVR-----------LNAVNRFESTVI---------------------DARKLYCRLGEDLSKASRHRIVISTCSTAG 125
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2085193927  602 dpRLAKMQFRS-----ILIDESTQATEPECMVPVVL---GAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLV 669
Cdd:cd18078    126 --LLYQMGLPVghfthVFVDEAGQATEPESLIPLGLissRDGQIILAGDPMQLGPVIKSRLASAYGLGVSFLERLM 199
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
467-682 1.66e-31

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: 119.51  E-value: 1.66e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  467 LSLIQGPPGTGKTVTSATIVYHLARQ---GNGPVLVCAPSNIAVDQLtekihqtglkvvrlcaksreaidspvsflalhn 543
Cdd:cd17914      1 LSLIQGPPGTGKTRVLVKIVAALMQNkngEPGRILLVTPTNKAAAQL--------------------------------- 47
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  544 qirnmdsmpelqklqqlkdetgelsssdekryralkrtaerellmnadvicctcvgagdprlakmqfRSILIDESTQATE 623
Cdd:cd17914     48 -------------------------------------------------------------------DNILVDEAAQILE 60
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2085193927  624 PECM--VPVVLGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQY 682
Cdd:cd17914     61 PETSrlIDLALDQGRVILVGDHDQLGPVWRGAVLAKICNEQSLFTRLVRLGVSLIRLQVQY 121
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
467-683 1.58e-30

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: 116.57  E-value: 1.58e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  467 LSLIQGPPGTGKTVTSATIVYHLARQGNGP-VLVCAPSNIAVDqltekihqtglkvvrlcaksreaidspvsflalhnqi 545
Cdd:cd17934      1 ISLIQGPPGTGKTTTIAAIVLQLLKGLRGKrVLVTAQSNVAVD------------------------------------- 43
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  546 rnmdsmpelqklqqlkdetgelsssdekryralkrtaerellmNADVIcctcvgagdprlakmqfrsiLIDESTQATEPE 625
Cdd:cd17934     44 -------------------------------------------NVDVV--------------------IIDEASQITEPE 60
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2085193927  626 CMVPVvLGAKQLILVGDHCQLGPVVMCKKAAKAG----LSQSLFERLVVLGIRPIRLQVQYR 683
Cdd:cd17934     61 LLIAL-IRAKKVVLVGDPKQLPPVVQEDHAALLGlsfiLSLLLLFRLLLPGSPKVMLDTQYR 121
1B_UPF1_nv_SF1_Hel-like cd21344
1B domain of eukaryotic UPF1 helicase, nidovirus SF1 helicases including coronavirus Nsp13 and ...
306-392 2.33e-30

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: 115.10  E-value: 2.33e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  306 DNITVRWDLGLNKKRIAYFTLPKTDSgDMRLMQGDEICLRYKGDMAPLWKGIGHVIKVPDNYGDEIAIELRSSAGAPVEV 385
Cdd:cd21344      1 LIITVRWRLALNDFRGAYFSLEKGKS-QCKPPLGDEIVLTYYGDTVPLWEGIGEVIDLPNTGNDDDALELKGSTTYPLTV 79

                   ....*..
gi 2085193927  386 PHNFQVD 392
Cdd:cd21344     80 THIFVLT 86
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
451-682 6.03e-29

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: 114.18  E-value: 6.03e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  451 LNHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSA----TIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGL-KVVRLc 525
Cdd:cd17936      2 LDPSQLEALKHALTSELALIQGPPGTGKTFLGVklvrALLQNQDLSITGPILVVCYTNHALDQFLEGLLDFGPtKIVRL- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  526 aksreaidspvsflalhnqirnmdsmpelqklqqlkdetgelsssdekryralkrtaerellmNADVICCTCVGAGDPR- 604
Cdd:cd17936     81 ---------------------------------------------------------------GARVIGMTTTGAAKYRe 97
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  605 -LAKMQFRSILIDESTQATEPE---CMVPVVlgaKQLILVGDHCQLGPVVMCKK--AAKAGLSQSLFERLVVLGIRPIRL 678
Cdd:cd17936     98 lLQALGPKVVIVEEAAEVLEAHilaALTPST---EHLILIGDHKQLRPKVNVYEltAKKYNLDVSLFERLVKNGLPFVTL 174

                   ....
gi 2085193927  679 QVQY 682
Cdd:cd17936    175 NVQR 178
SF1_C cd18786
C-terminal helicase domain of superfamily 1 DEAD/H-box helicases; Superfamily (SF)1 family ...
769-854 4.46e-26

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: 102.90  E-value: 4.46e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  769 QIGIITPYEGQRSYLVQYMQFSgSLHTKLYQEVEIASVDAFQGREKDFIILSCVRANEHqgigflnDPRRLNVALTRARY 848
Cdd:cd18786     12 KGVVLTPYHRDRAYLNQYLQGL-SLDEFDLQLVGAITIDSSQGLTFDVVTLYLPTANSL-------TPRRLYVALTRARK 83

                   ....*.
gi 2085193927  849 GVIIVG 854
Cdd:cd18786     84 RLVIYD 89
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
452-690 7.13e-21

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: 92.10  E-value: 7.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  452 NHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLarQGNGP---VLVCAPSNIAVDQLTEKIhqtglkvvrlcaks 528
Cdd:cd17935      7 TPTQIEAIRSGMQPGLTMVVGPPGTGKTDVAVQIISNL--YHNFPnqrTLIVTHSNQALNQLFEKI-------------- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  529 rEAIDSPvsflalhnqirnmdsmpelqklqqlkdetgelsssdekryralkrtaERELL---MNADVICCTCVGAGDPR- 604
Cdd:cd17935     71 -MALDID-----------------------------------------------ERHLLrlgHGAKIIAMTCTHAALKRg 102
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  605 -LAKMQFR--SILIDESTQATEPECMVPVVL--------GAKQLILVGDHCQLGPVVMCKKAAK-AGLSQSLFERLVVLG 672
Cdd:cd17935    103 eLVELGFKydNILMEEAAQILEIETFIPLLLqnpedgpnRLKRLIMIGDHHQLPPVIKNMAFQKySNMEQSLFTRLVRLG 182
                          250
                   ....*....|....*...
gi 2085193927  673 IRPIRLQVQYRMHPALSA 690
Cdd:cd17935    183 VPTVDLDAQGRARASISS 200
ZBD_UPF1_nv_SF1_Hel-like cd21343
Cys/His rich zinc-binding domain (CH/ZBD) of eukaryotic UPF1 helicase, nidovirus SF1 helicases ...
101-190 2.80e-18

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: 79.84  E-value: 2.80e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  101 ACSYCGIHDpacVVYCNTS--KKWFCNgrgntsgSHIVNHLVRAKCKEVTLHKdgplgetVLECYNCGCRNVFLLGFipa 178
Cdd:cd21343      1 ACYVCGSHT---VVRCGTCirRPWFCN-------SCIYDHLIRTKHKEVLLAS-------PYVCAGCGESDITLLYF--- 60
                           90
                   ....*....|..
gi 2085193927  179 kadSVVVLLCRQ 190
Cdd:cd21343     61 ---GGVSYRCVD 69
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
407-861 1.29e-16

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: 84.26  E-value: 1.29e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  407 LKTFAVDETSVSGYIyHKLLGHEVEDVIIKCQLPKRFTAQGLpDLNHSQVYAVKTVL-QRPLSLIQGPPGTGKTVTSATI 485
Cdd:COG0507     83 LTRLLEAEQRLARRL-RRLARPALDEADVEAALAALEPRAGI-TLSDEQREAVALALtTRRVSVLTGGAGTGKTTTLRAL 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  486 VYHLARQGnGPVLVCAPSNIAVDQLTEKIhqtglkvvrlcakSREAidspvsfLALHnqirnmdsmpelQKLQQLKDETG 565
Cdd:COG0507    161 LAALEALG-LRVALAAPTGKAAKRLSEST-------------GIEA-------RTIH------------RLLGLRPDSGR 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  566 elsssdekryralKRTAERELLMNADVicctcvgagdprlakmqfrsILIDESTqatepecMVPVVLGAK---------- 635
Cdd:COG0507    208 -------------FRHNRDNPLTPADL--------------------LVVDEAS-------MVDTRLMAAllealpraga 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  636 QLILVGDHCQLGPVVmckkaakAGlsqSLFERLVVLGIRP-IRLQVQYRMhpalsAFPSNIfyegslqngVTAADRIKKG 714
Cdd:COG0507    248 RLILVGDPDQLPSVG-------AG---AVLRDLIESGTVPvVELTEVYRQ-----ADDSRI---------IELAHAIREG 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  715 -FDFQWPQPDKPMFFYVTQGQEEIASS-----------------------GTSYLNR----------TEAANVEKITTRL 760
Cdd:COG0507    304 dAPEALNARYADVVFVEAEDAEEAAEAivelyadrpaggediqvlaptnaGVDALNQairealnpagELERELAEDGELE 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  761 LKAGAK-------PD------QIGIITPYEGQRSYLVqyMQFSGSLHTKlYQEVEIASVD-AF-------QGREKD--FI 817
Cdd:COG0507    384 LYVGDRvmftrndYDlgvfngDIGTVLSIDEDEGRLT--VRFDGREIVT-YDPSELDQLElAYaitvhksQGSTFDrvIL 460
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 2085193927  818 ILScvraNEHQGigfLNDPRRLNVALTRARYGVIIVGNPKALSK 861
Cdd:COG0507    461 VLP----SEHSP---LLSRELLYTALTRARELLTLVGDRDALAR 497
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
451-668 2.65e-16

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: 79.45  E-value: 2.65e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  451 LNHSQVYAVkTVLQRPLS------LIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVD-QLTEKIHqtglkvvr 523
Cdd:cd18077      2 LNAKQKEAV-LAITTPLSiqlppvLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAADlYIKEYLH-------- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  524 lcaKSREAIDSPVSFLALHNQIRNMDSMPELQKLQQLKDETGELsssdekryralkRTAERELLMNADVICCT-----CV 598
Cdd:cd18077     73 ---PYVETGNPRARPLRVYYRNRWVKTVHPVVQKYCLIDEHGTF------------RMPTREDVMRHRVVVVTlstsqYL 137
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2085193927  599 GAGDprLAKMQFRSILIDESTQATEPECMVPVVLGAK--QLILVGDHCQLGPVVMCKKAAKAGLSQSLFERL 668
Cdd:cd18077    138 CQLD--LEPGFFTHILLDEAAQAMECEAIMPLALATKstRIVLAGDHMQLSPEVYSEFARERNLHISLLERL 207
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
452-651 5.82e-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: 63.76  E-value: 5.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  452 NHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNGpVLVCAPSNIAvdqltekihqtgLKVVRLcaksrea 531
Cdd:cd18043      1 DSSQEAAIISARNGKNVVIQGPPGTGKSQTIANIIANALARGKR-VLFVSEKKAA------------LDVVRF------- 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  532 idsPVSFLALHNQIRNMDsmpelqklqqlkdetgelsssdekryralkrtaerellmnadvicctcvgagdprLAKMQFR 611
Cdd:cd18043     61 ---PCWIMSPLSVSQYLP-------------------------------------------------------LNRNLFD 82
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2085193927  612 SILIDESTQAtEPECMVPVVLGAKQLILVGDHCQLGPVVM 651
Cdd:cd18043     83 LVIFDEASQI-PIEEALPALFRGKQVVVVGDDKQLPPSIL 121
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
455-514 1.89e-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: 63.34  E-value: 1.89e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  455 QVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLaRQGNGPVLVCAPSNIAVDQLTEKI 514
Cdd:cd17933      2 QKAAVRLVLRNRVSVLTGGAGTGKTTTLKALLAAL-EAEGKRVVLAAPTGKAAKRLSEST 60
DEXXQc_HELZ2-N cd18076
N-terminal DEXXQ-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
466-668 4.50e-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: 64.14  E-value: 4.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  466 PLsLIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVD-QLTEKIHQtglkvvRLCAKSREAIdsPVSFLALHNQ 544
Cdd:cd18076     25 PL-LIYGPFGTGKTFTLAMAALEVIREPGTKVLICTHTNSAADiYIREYFHP------YVDKGHPEAR--PLRIKATDRP 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  545 IRNMDsmPELQKLQQLKDEtgelsssdekryRALKRTAERELLMNADVICCTCVGAGDPRLAKMQFRSILIDESTQATEP 624
Cdd:cd18076     96 NAITD--PDTITYCCLTKD------------RQCFRLPTRDELDFHNIVITTTAMAFNLHVLSGFFTHIFIDEAAQMLEC 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2085193927  625 ECMVPVVLGA--KQLILVGDHCQLGPVVMCKKAAKAGlSQSLFERL 668
Cdd:cd18076    162 EALIPLSYAGpkTRVVLAGDHMQMTPKLFSVADYNRA-NHTLLNRL 206
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
451-685 9.89e-10

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: 59.11  E-value: 9.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  451 LNHSQVYAVKTVL--QRPLSLIQGPPGTGKTVTSATIVYHLARQGnGPVLVCAPSNIAVDQLtekihqtglkvvrlcaks 528
Cdd:pfam13604    2 LNAEQAAAVRALLtsGDRVAVLVGPAGTGKTTALKALREAWEAAG-YRVIGLAPTGRAAKVL------------------ 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  529 REAIDSPVSFLAlhnqirnmdsmpelqklqqlkdetgelsssdekryRALKRTAERELLMNADVicctcvgagdprlakm 608
Cdd:pfam13604   63 GEELGIPADTIA-----------------------------------KLLHRLGGRAGLDPGTL---------------- 91
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  609 qfrsILIDESTQATEPEcMVPVV-----LGAKqLILVGDHCQLGPVvmckkaaKAGlsqSLFERLVVLGIRPIRLQVQYR 683
Cdd:pfam13604   92 ----LIVDEAGMVGTRQ-MARLLklaedAGAR-VILVGDPRQLPSV-------EAG---GAFRDLLAAGIGTAELTEIVR 155

                   ..
gi 2085193927  684 MH 685
Cdd:pfam13604  156 QR 157
AAA_19 pfam13245
AAA domain;
458-519 1.10e-08

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 54.92  E-value: 1.10e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2085193927  458 AVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQG--NGPVLVCAPSNIAVDQLTEKihqTGL 519
Cdd:pfam13245    4 AVRTALPSKVVLLTGGPGTGKTTTIRHIVALLVALGgvSFPILLAAPTGRAAKRLSER---TGL 64
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
417-649 2.03e-07

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: 55.15  E-value: 2.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  417 VSGYIYHKLLGHEVEDVIIKCQ--LPKRFTAQGLPDLNHS---------QVYAVKTVLQRPLSLIQGPPGTGKTVTSATI 485
Cdd:TIGR01447  100 CDGRLYLRRYWREEEKLAAKLRtlLEARKRTAPSAILENLfpllneqnwRKTAVALALKSNFSLITGGPGTGKTTTVARL 179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  486 VYHLARQ----GNGPVLVCAPSNIAVDQLTEKIHQtglKVVRLCAKSREAIDSPVSFLALHnqirnmdsmpelqKLQQLK 561
Cdd:TIGR01447  180 LLALVKQspkqGKLRIALAAPTGKAAARLAESLRK---AVKNLAAAEALIAALPSEAVTIH-------------RLLGIK 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  562 detgelssSDEKRYRALKRTAerellMNADVicctcvgagdprlakmqfrsILIDESTQATEP--ECMVPVVLGAKQLIL 639
Cdd:TIGR01447  244 --------PDTKRFRHHERNP-----LPLDV--------------------LVVDEASMVDLPlmAKLLKALPPNTKLIL 290
                          250
                   ....*....|
gi 2085193927  640 VGDHCQLGPV 649
Cdd:TIGR01447  291 LGDKNQLPSV 300
ResIII pfam04851
Type III restriction enzyme, res subunit;
451-525 2.81e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 48.44  E-value: 2.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  451 LNHSQVYAVKTVLQRPLS-----LIQGPPGTGKTVTSATIVYHLARQGNG-PVLVCAPSNIAVDQLTEKIHQTGLKVVRL 524
Cdd:pfam04851    4 LRPYQIEAIENLLESIKNgqkrgLIVMATGSGKTLTAAKLIARLFKKGPIkKVLFLVPRKDLLEQALEEFKKFLPNYVEI 83

                   .
gi 2085193927  525 C 525
Cdd:pfam04851   84 G 84
DEXDc smart00487
DEAD-like helicases superfamily;
455-514 3.72e-06

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 49.03  E-value: 3.72e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2085193927   455 QVYAVKTVLQRPLS-LIQGPPGTGKTVTSAT-IVYHLARQGNGPVLVCAPSNIAVDQLTEKI 514
Cdd:smart00487   13 QKEAIEALLSGLRDvILAAPTGSGKTLAALLpALEALKRGKGGRVLVLVPTRELAEQWAEEL 74
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
469-516 1.59e-04

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 45.79  E-value: 1.59e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2085193927  469 LIQGPPGTGKTVTSATIVYHLARQgnGPVLVCAPSNIAVDQLTEKIHQ 516
Cdd:COG1061    104 LVVAPTGTGKTVLALALAAELLRG--KRVLVLVPRRELLEQWAEELRR 149
DEAD-like_helicase_C cd09300
C-terminal helicase domain of the DEAD-like helicases; This hierarchy of DEAD-like helicases ...
801-848 2.69e-04

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: 39.84  E-value: 2.69e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2085193927  801 VEIASVDAFQG---REKDFIILSCVRanehqgigflNDPRRLNVALTRARY 848
Cdd:cd09300      8 VLIAVN*ALTGfdaPELNTIIVDKNL----------RSYRGLNQAFGRANR 48
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
455-580 6.87e-04

DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family 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: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 42.34  E-value: 6.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  455 QVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGN-GPVLVCAPSNIAVDQLTEKI----HQTGLKVVRLCAKSR 529
Cdd:cd18013      5 QKVAINFIIEHPYCGLFLDMGLGKTVTTLTALSDLQLDDFtRRVLVIAPLRVARSTWPDEVekwnHLRNLTVSVAVGTER 84
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2085193927  530 E---AIDSPVSFLalhnqIRNMDSMPELQKLQQLK--------DETGELSSSDEKRYRALKR 580
Cdd:cd18013     85 QrskAANTPADLY-----VINRENLKWLVNKSGDPwpfdmvviDELSSFKSPRSKRFKALRK 141
gammaCoV_Nsp13-helicase cd21720
helicase domain of gammacoronavirus non-structural protein 13; This model represents the ...
801-853 1.65e-03

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: 41.83  E-value: 1.65e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2085193927  801 VEIASVDAFQGREKDFIILsCVRANEHQGIGFlndpRRLNVALTRARYGVIIV 853
Cdd:cd21720    280 LNVQTVDSSQGSEYDYVIF-CVTADSQHALNI----NRFNVALTRAKRGILVV 327
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
455-535 2.30e-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: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  455 QVYAVKTVLQRPLS------LIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLkVVRLCAKS 528
Cdd:pfam13191    8 ELEQLLDALDRVRSgrppsvLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPLLEALTREGL-LRQLLDEL 86

                   ....*..
gi 2085193927  529 REAIDSP 535
Cdd:pfam13191   87 ESSLLEA 93
CoV_Nsp13-helicase cd21718
helicase domain of coronavirus non-structural protein 13; This model represents the helicase ...
448-853 2.30e-03

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


Pssm-ID: 409652 [Multi-domain]  Cd Length: 341  Bit Score: 41.36  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  448 LPDLNHSQVYAVKTVLQRPLSLIQGPPGTGKT--VTSATIVYHLARqgngpVLVCAPSNIAVDQLTEKIHQTgLKVvRLC 525
Cdd:cd21718      8 IPHDFSNHVPSYQKIGKQKYTTVQGPPGTGKShfAIGLALYYPGAR-----IVYTACSHAAVDALCEKASKW-LPN-DKC 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  526 AK---SREAIDSPVSFLALHNQIR----NMDSMPELqklqqlkdetgelsssdekryralkrtaerellmNADVIcctcv 598
Cdd:cd21718     81 SRivpQRARVECFDGFKVNNTNAQyifsTINALPEC----------------------------------SADIV----- 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  599 gagdprlakmqfrsiLIDESTQATEPE-CMVPVVLGAKQLILVGDHCQL-GPVVMCKKAAKAGLSQSLFERLVVlGIRP- 675
Cdd:cd21718    122 ---------------VVDEVSMCTNYDlSVVNARLKYKHIVYVGDPAQLpAPRTLLTEGSLEPKDYNVVTRLMV-GSGPd 185
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  676 IRLQVQYRMHPALSAFPSNIFYEGSLQngvtaadrikkgfdfqwPQPDKPMFFYVTQGQEEIASSGTSYLNRTEAANVEK 755
Cdd:cd21718    186 VFLSKCYRCPKEIVDTVSKLVYDNKLK-----------------AIKPKSRQCFKTFGKGDVRHDNGSAINRPQLEFVKR 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2085193927  756 ITTRllkaGAKPDQIGIITPYEGQRSYLVQYMQFSgslhtklyqeveIASVDAFQGREKDFIILsCVRANEHQGIGFlnd 835
Cdd:cd21718    249 FLDR----NPRWRKAVFISPYNAMNNRASRLLGLS------------TQTVDSSQGSEYDYVIF-CQTTDTAHALNI--- 308
                          410
                   ....*....|....*...
gi 2085193927  836 pRRLNVALTRARYGVIIV 853
Cdd:cd21718    309 -NRFNVAITRAKHGILVI 325
deltaCoV_Nsp13-helicase cd21721
helicase domain of deltacoronavirus non-structural protein 13; This model represents the ...
805-853 5.96e-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: 40.29  E-value: 5.96e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2085193927  805 SVDAFQGREKDFIILsCVRANEHQGIGFlndpRRLNVALTRARYGVIIV 853
Cdd:cd21721    283 TVDSSQGSEYDYVIF-CVTTDSAHALNM----SRLNVALTRAKIGILVV 326
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
469-520 9.91e-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: 37.74  E-value: 9.91e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2085193927   469 LIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLK 520
Cdd:smart00382    6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGK 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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