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Conserved domains on  [gi|1546556163|gb|RUS22009|]
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RNA helicase-domain-containing protein, partial [Endogone sp. FLAS-F59071]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UPF1_Zn_bind pfam09416
RNA helicase (UPF2 interacting domain); UPF1 is an essential RNA helicase that detects mRNAs ...
124-275 4.05e-115

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: 339.61  E-value: 4.05e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 124 HACRYCGIHSPASVVKCVTCSKWFCNSRGNTSGSHIINHLVRAKHKEVVLHHQSPLGETALECYNCGCRNVFLLGFIPAK 203
Cdd:pfam09416   1 HACAYCGIHDPACVVKCLTCGKWFCNGRGNTSGSHIINHLVRSKHKEVSLHPDSPLGDTVLECYNCGSKNVFLLGFIPAK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1546556163 204 SDTVVVLLCRQPCAAMPSSKDMNWDTSQWMPLIDDRCFLTWLVKVPSEQEQLRARQITAHQINKLEELWKDD 275
Cdd:pfam09416  81 SDSVVVLLCRQPCAQAKSLKDMNWDTSQWQPLIEDRQFLPWLVKVPSEEEQLRARQITPAQINKLEELWKDN 152
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
474-611 9.87e-87

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


The actual alignment was detected with superfamily member cd18039:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 234  Bit Score: 269.50  E-value: 9.87e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 474 ELNHSQVYAVKSVLQKPLSLIQGPPGTGKTVTSASIVYHLAKMNPGQVLVCAPSNVAVDQLTEKIHATGLKVVRLTAKSR 553
Cdd:cd18039     1 ELNHSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVDQLTEKIHQTGLKVVRLCAKSR 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1546556163 554 EALDSPVSFLTLHEQVHNNDTNVELQKLIQLKQEQGELSASDEKKYKMLKRACEKEIL 611
Cdd:cd18039    81 EAVESPVSFLALHNQVRNLDSAEKLELLKLLKLETGELSSADEKRYRKLKRKAERELL 138
1B_UPF1-like cd21407
1B domain of eukaryotic UPF1 RNA helicase and related proteins; Helicases catalyze ...
328-417 5.54e-55

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: 181.19  E-value: 5.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 328 TCDDIVVRWDIGLNQKRIAWFFFPKLEMGEVRLAVGDELRLRYRGELHEPWECVGHVIKIPNNVSDEVGLELRRNDNTPA 407
Cdd:cd21407     1 TQENISVRWDVGLNKKRLAYFTLPKLDESELRLMVGDELRLRYKGDLREPWEGVGHVIKIPDNYSEEVALELRSSKNAPT 80
                          90
                  ....*....|
gi 1546556163 408 DCTHNFSVDF 417
Cdd:cd21407    81 EITTGFSVEF 90
 
Name Accession Description Interval E-value
UPF1_Zn_bind pfam09416
RNA helicase (UPF2 interacting domain); UPF1 is an essential RNA helicase that detects mRNAs ...
124-275 4.05e-115

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: 339.61  E-value: 4.05e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 124 HACRYCGIHSPASVVKCVTCSKWFCNSRGNTSGSHIINHLVRAKHKEVVLHHQSPLGETALECYNCGCRNVFLLGFIPAK 203
Cdd:pfam09416   1 HACAYCGIHDPACVVKCLTCGKWFCNGRGNTSGSHIINHLVRSKHKEVSLHPDSPLGDTVLECYNCGSKNVFLLGFIPAK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1546556163 204 SDTVVVLLCRQPCAAMPSSKDMNWDTSQWMPLIDDRCFLTWLVKVPSEQEQLRARQITAHQINKLEELWKDD 275
Cdd:pfam09416  81 SDSVVVLLCRQPCAQAKSLKDMNWDTSQWQPLIEDRQFLPWLVKVPSEEEQLRARQITPAQINKLEELWKDN 152
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
474-611 9.87e-87

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: 269.50  E-value: 9.87e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 474 ELNHSQVYAVKSVLQKPLSLIQGPPGTGKTVTSASIVYHLAKMNPGQVLVCAPSNVAVDQLTEKIHATGLKVVRLTAKSR 553
Cdd:cd18039     1 ELNHSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVDQLTEKIHQTGLKVVRLCAKSR 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1546556163 554 EALDSPVSFLTLHEQVHNNDTNVELQKLIQLKQEQGELSASDEKKYKMLKRACEKEIL 611
Cdd:cd18039    81 EAVESPVSFLALHNQVRNLDSAEKLELLKLLKLETGELSSADEKRYRKLKRKAERELL 138
ZBD_UPF1-like cd21400
Cys/His rich zinc-binding domain (CH/ZBD) of eukaryotic UPF1 RNA helicase and related proteins; ...
125-245 3.33e-82

Cys/His rich zinc-binding domain (CH/ZBD) of eukaryotic UPF1 RNA helicase and related proteins; Helicases catalyze NTP-dependent unwinding of nucleic acid duplexes into single strands and are classified based on the arrangement of conserved motifs into six superfamilies. UPF1 belongs to helicase superfamily 1 (SF1). The CH/ZBD has 3 zinc-finger (ZnF1-3) motifs. UPF1 participates in nonsense-mediated mRNA decay (NMD), a pathway which degrades transcripts with premature termination codons. The N-terminal CH/ZBD of UPF1 interacts with UPF2, a factor also involved in NMD. UPF1 has an N-terminal CH/ZBD, a 1B domain, and a SF1 helicase core.


Pssm-ID: 439167  Cd Length: 120  Bit Score: 253.71  E-value: 3.33e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 125 ACRYCGIHSPASVVKCVTCSKWFCNSRGNTSGSHIINHLVRAKHKEVVLHHQSPLGETALECYNCGCRNVFLLGFIPAKS 204
Cdd:cd21400     1 ACAYCGIHDPACLVKCLTCGKWFCNGRGNTSGSHIVQHLVRSKHKEVSLHPDSPLGDTVLECYNCGSRNVFLLGFIPAKA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1546556163 205 DTVVVLLCRQPCAAmPSSKDMNWDTSQWMPLIDDRCFLTWL 245
Cdd:cd21400    81 DSVVVLLCRQPCLS-QSSKDMNWDLSQWQPLIDDRQFLPWL 120
1B_UPF1-like cd21407
1B domain of eukaryotic UPF1 RNA helicase and related proteins; Helicases catalyze ...
328-417 5.54e-55

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: 181.19  E-value: 5.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 328 TCDDIVVRWDIGLNQKRIAWFFFPKLEMGEVRLAVGDELRLRYRGELHEPWECVGHVIKIPNNVSDEVGLELRRNDNTPA 407
Cdd:cd21407     1 TQENISVRWDVGLNKKRLAYFTLPKLDESELRLMVGDELRLRYKGDLREPWEGVGHVIKIPDNYSEEVALELRSSKNAPT 80
                          90
                  ....*....|
gi 1546556163 408 DCTHNFSVDF 417
Cdd:cd21407    81 EITTGFSVEF 90
UPF1_1B_dom pfam18141
RNA helicase UPF1, 1B domain; UPF1 (or regulator of nonsense transcripts 1 homolog) is an ...
327-418 5.40e-50

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: 167.88  E-value: 5.40e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 327 QTCDDIVVRWDIGLNQKRIAWFFFPKLEMGEVRLAVGDELRLRYRGELHEPWECVGHVIKIPNNVSDEVGLELRRNDN-T 405
Cdd:pfam18141   1 QTQDDISVRWDVGLNKKHLAWFSLPKLDSGEMKLAVGDELRLRYTGSLAEPWEGVGHVVKIPDNSSEEVTLELRSSSNnP 80
                          90
                  ....*....|...
gi 1546556163 406 PADCTHNFSVDFV 418
Cdd:pfam18141  81 PTDLTHGFTVEFV 93
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
478-588 3.94e-20

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


Pssm-ID: 404072 [Multi-domain]  Cd Length: 248  Bit Score: 90.10  E-value: 3.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 478 SQVYAVKSVLQKP-LSLIQGPPGTGKTVTSASIVYHLAKMN------PGQVLVCAPSNVAVDQLTEKIHATG----LKVV 546
Cdd:pfam13086   1 SQREAIRSALSSShFTLIQGPPGTGKTTTIVELIRQLLSYPatsaaaGPRILVCAPSNAAVDNILERLLRKGqkygPKIV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1546556163 547 RLTAKsrEALDSPVSFLTLHEQVHNNDTNVELQKLIQLKQEQ 588
Cdd:pfam13086  81 RIGHP--AAISEAVLPVSLDYLVESKLNNEEDAQIVKDISKE 120
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
357-600 9.03e-19

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: 90.26  E-value: 9.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 357 EVRLAVGDELRLRYRGELHEpwECVGHVIKIPNNVSDeVGLElrrnDNTPADCTHNFSVDFVWKSTSFDRMQLAMKTFAV 436
Cdd:TIGR00376  55 ATEISVGDIVLVSRGNPLQS--DLTGVVTRVGKRFIT-VALE----ESVPQWSLKRVRIDLYANDVTFKRMKEALRALTE 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 437 DETSVSGYIYHRLLGHDVePQVLKTQMPKrfsahnlPELNHSQVYAVK-SVLQKPLSLIQGPPGTGKTVTSASIVYHLAK 515
Cdd:TIGR00376 128 NHSRLLEFLLGREAPSKA-SEIHDFQFFD-------PNLNESQKEAVLfALSSKDLFLIHGPPGTGKTRTVVELIRQLVK 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 516 MNPgQVLVCAPSNVAVDQLTEKIHATGLKVVRLTAKSReALDSPVSFlTLHEQVHNNDTNvelQKLIQLKQEQGELSASD 595
Cdd:TIGR00376 200 RGL-RVLVTAPSNIAVDNLLERLALCDQKIVRLGHPAR-LLKSNKQH-SLDYLIENHPKY---QIVADIREKIDELIEER 273

                  ....*
gi 1546556163 596 EKKYK 600
Cdd:TIGR00376 274 NKKTK 278
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
428-538 1.14e-10

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: 64.23  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 428 QLAMKTFAVDETSVSGYIyHRLLGHDVEPQVLKTQMPKRFSAHNLpELNHSQVYAVKSVLQK-PLSLIQGPPGTGKTVTS 506
Cdd:COG0507    80 RRYLTRLLEAEQRLARRL-RRLARPALDEADVEAALAALEPRAGI-TLSDEQREAVALALTTrRVSVLTGGAGTGKTTTL 157
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1546556163 507 ASIVYHLAKMNpGQVLVCAPSNVAVDQLTEKI 538
Cdd:COG0507   158 RALLAALEALG-LRVALAAPTGKAAKRLSEST 188
DEXDc smart00487
DEAD-like helicases superfamily;
467-538 7.58e-07

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 50.18  E-value: 7.58e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1546556163  467 FSAHNLPELNHSQVYAVKSVLQKPLS-LIQGPPGTGKTVT-SASIVYHLAKMNPGQVLVCAPSNVAVDQLTEKI 538
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLRDvILAAPTGSGKTLAaLLPALEALKRGKGGRVLVLVPTRELAEQWAEEL 74
recD PRK10875
exodeoxyribonuclease V subunit alpha;
487-566 1.23e-04

exodeoxyribonuclease V subunit alpha;


Pssm-ID: 236783 [Multi-domain]  Cd Length: 615  Bit Score: 44.93  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 487 LQKPLSLIQGPPGTGKTVTSASIVYHLAKMNPGQVLV---CAPSNVAVDQLTEKIHATgLKVVRLTAKSREALdsPVSFL 563
Cdd:PRK10875  165 LTRRISVISGGPGTGKTTTVAKLLAALIQLADGERCRirlAAPTGKAAARLTESLGKA-LRQLPLTDEQKKRI--PEEAS 241

                  ...
gi 1546556163 564 TLH 566
Cdd:PRK10875  242 TLH 244
 
Name Accession Description Interval E-value
UPF1_Zn_bind pfam09416
RNA helicase (UPF2 interacting domain); UPF1 is an essential RNA helicase that detects mRNAs ...
124-275 4.05e-115

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: 339.61  E-value: 4.05e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 124 HACRYCGIHSPASVVKCVTCSKWFCNSRGNTSGSHIINHLVRAKHKEVVLHHQSPLGETALECYNCGCRNVFLLGFIPAK 203
Cdd:pfam09416   1 HACAYCGIHDPACVVKCLTCGKWFCNGRGNTSGSHIINHLVRSKHKEVSLHPDSPLGDTVLECYNCGSKNVFLLGFIPAK 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1546556163 204 SDTVVVLLCRQPCAAMPSSKDMNWDTSQWMPLIDDRCFLTWLVKVPSEQEQLRARQITAHQINKLEELWKDD 275
Cdd:pfam09416  81 SDSVVVLLCRQPCAQAKSLKDMNWDTSQWQPLIEDRQFLPWLVKVPSEEEQLRARQITPAQINKLEELWKDN 152
DEXXQc_UPF1 cd18039
DEXXQ-box helicase domain of UPF1; UPF1 (also called RNA Helicase And ATPase, Regulator Of ...
474-611 9.87e-87

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: 269.50  E-value: 9.87e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 474 ELNHSQVYAVKSVLQKPLSLIQGPPGTGKTVTSASIVYHLAKMNPGQVLVCAPSNVAVDQLTEKIHATGLKVVRLTAKSR 553
Cdd:cd18039     1 ELNHSQVDAVKTALQRPLSLIQGPPGTGKTVTSATIVYHLVKQGNGPVLVCAPSNVAVDQLTEKIHQTGLKVVRLCAKSR 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1546556163 554 EALDSPVSFLTLHEQVHNNDTNVELQKLIQLKQEQGELSASDEKKYKMLKRACEKEIL 611
Cdd:cd18039    81 EAVESPVSFLALHNQVRNLDSAEKLELLKLLKLETGELSSADEKRYRKLKRKAERELL 138
ZBD_UPF1-like cd21400
Cys/His rich zinc-binding domain (CH/ZBD) of eukaryotic UPF1 RNA helicase and related proteins; ...
125-245 3.33e-82

Cys/His rich zinc-binding domain (CH/ZBD) of eukaryotic UPF1 RNA helicase and related proteins; Helicases catalyze NTP-dependent unwinding of nucleic acid duplexes into single strands and are classified based on the arrangement of conserved motifs into six superfamilies. UPF1 belongs to helicase superfamily 1 (SF1). The CH/ZBD has 3 zinc-finger (ZnF1-3) motifs. UPF1 participates in nonsense-mediated mRNA decay (NMD), a pathway which degrades transcripts with premature termination codons. The N-terminal CH/ZBD of UPF1 interacts with UPF2, a factor also involved in NMD. UPF1 has an N-terminal CH/ZBD, a 1B domain, and a SF1 helicase core.


Pssm-ID: 439167  Cd Length: 120  Bit Score: 253.71  E-value: 3.33e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 125 ACRYCGIHSPASVVKCVTCSKWFCNSRGNTSGSHIINHLVRAKHKEVVLHHQSPLGETALECYNCGCRNVFLLGFIPAKS 204
Cdd:cd21400     1 ACAYCGIHDPACLVKCLTCGKWFCNGRGNTSGSHIVQHLVRSKHKEVSLHPDSPLGDTVLECYNCGSRNVFLLGFIPAKA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1546556163 205 DTVVVLLCRQPCAAmPSSKDMNWDTSQWMPLIDDRCFLTWL 245
Cdd:cd21400    81 DSVVVLLCRQPCLS-QSSKDMNWDLSQWQPLIDDRQFLPWL 120
1B_UPF1-like cd21407
1B domain of eukaryotic UPF1 RNA helicase and related proteins; Helicases catalyze ...
328-417 5.54e-55

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: 181.19  E-value: 5.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 328 TCDDIVVRWDIGLNQKRIAWFFFPKLEMGEVRLAVGDELRLRYRGELHEPWECVGHVIKIPNNVSDEVGLELRRNDNTPA 407
Cdd:cd21407     1 TQENISVRWDVGLNKKRLAYFTLPKLDESELRLMVGDELRLRYKGDLREPWEGVGHVIKIPDNYSEEVALELRSSKNAPT 80
                          90
                  ....*....|
gi 1546556163 408 DCTHNFSVDF 417
Cdd:cd21407    81 EITTGFSVEF 90
UPF1_1B_dom pfam18141
RNA helicase UPF1, 1B domain; UPF1 (or regulator of nonsense transcripts 1 homolog) is an ...
327-418 5.40e-50

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: 167.88  E-value: 5.40e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 327 QTCDDIVVRWDIGLNQKRIAWFFFPKLEMGEVRLAVGDELRLRYRGELHEPWECVGHVIKIPNNVSDEVGLELRRNDN-T 405
Cdd:pfam18141   1 QTQDDISVRWDVGLNKKHLAWFSLPKLDSGEMKLAVGDELRLRYTGSLAEPWEGVGHVVKIPDNSSEEVTLELRSSSNnP 80
                          90
                  ....*....|...
gi 1546556163 406 PADCTHNFSVDFV 418
Cdd:pfam18141  81 PTDLTHGFTVEFV 93
DEXXc_HELZ2-C cd18040
C-terminal DEXX-box helicase domain of HELZ2; Helicase with zinc finger 2 (HELZ2, also known ...
475-602 3.54e-23

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: 99.52  E-value: 3.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 475 LNHSQVYAVKSVLQKPLSLIQGPPGTGKTVTSASIVYHLAKMN------------PGQVLVCAPSNVAVDQLTEKI-HAT 541
Cdd:cd18040     2 LNPSQNHAVRTALTKPFTLIQGPPGTGKTVTGVHIAYWFAKQNreiqsvsgegdgGPCVLYCGPSNKSVDVVAELLlKVP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 542 GLKVVRLTAKSREALDSPV---------------------SFLTLHEQVHnNDTNVELQKLIQ----LKQEQGELSASDE 596
Cdd:cd18040    82 GLKILRVYSEQIETTEYPIpneprhpnkksereskpnselSSITLHHRIR-QPSNPHSQQIKAfearFERTQEKITEEDI 160

                  ....*.
gi 1546556163 597 KKYKML 602
Cdd:cd18040   161 KTYKIL 166
DEXXQc_SMUBP2 cd18044
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ...
474-548 5.80e-23

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: 96.52  E-value: 5.80e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1546556163 474 ELNHSQVYAVKSVL-QKPLSLIQGPPGTGKTVTSASIVYHLAKMNPgQVLVCAPSNVAVDQLTEKIHATGLKVVRL 548
Cdd:cd18044     1 NLNDSQKEAVKFALsQKDVALIHGPPGTGKTTTVVEIILQAVKRGE-KVLACAPSNIAVDNLVERLVALKVKVVRI 75
AAA_11 pfam13086
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
478-588 3.94e-20

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


Pssm-ID: 404072 [Multi-domain]  Cd Length: 248  Bit Score: 90.10  E-value: 3.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 478 SQVYAVKSVLQKP-LSLIQGPPGTGKTVTSASIVYHLAKMN------PGQVLVCAPSNVAVDQLTEKIHATG----LKVV 546
Cdd:pfam13086   1 SQREAIRSALSSShFTLIQGPPGTGKTTTIVELIRQLLSYPatsaaaGPRILVCAPSNAAVDNILERLLRKGqkygPKIV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1546556163 547 RLTAKsrEALDSPVSFLTLHEQVHNNDTNVELQKLIQLKQEQ 588
Cdd:pfam13086  81 RIGHP--AAISEAVLPVSLDYLVESKLNNEEDAQIVKDISKE 120
TIGR00376 TIGR00376
DNA helicase, putative; The gene product may represent a DNA helicase. Eukaryotic members of ...
357-600 9.03e-19

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: 90.26  E-value: 9.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 357 EVRLAVGDELRLRYRGELHEpwECVGHVIKIPNNVSDeVGLElrrnDNTPADCTHNFSVDFVWKSTSFDRMQLAMKTFAV 436
Cdd:TIGR00376  55 ATEISVGDIVLVSRGNPLQS--DLTGVVTRVGKRFIT-VALE----ESVPQWSLKRVRIDLYANDVTFKRMKEALRALTE 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 437 DETSVSGYIYHRLLGHDVePQVLKTQMPKrfsahnlPELNHSQVYAVK-SVLQKPLSLIQGPPGTGKTVTSASIVYHLAK 515
Cdd:TIGR00376 128 NHSRLLEFLLGREAPSKA-SEIHDFQFFD-------PNLNESQKEAVLfALSSKDLFLIHGPPGTGKTRTVVELIRQLVK 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 516 MNPgQVLVCAPSNVAVDQLTEKIHATGLKVVRLTAKSReALDSPVSFlTLHEQVHNNDTNvelQKLIQLKQEQGELSASD 595
Cdd:TIGR00376 200 RGL-RVLVTAPSNIAVDNLLERLALCDQKIVRLGHPAR-LLKSNKQH-SLDYLIENHPKY---QIVADIREKIDELIEER 273

                  ....*
gi 1546556163 596 EKKYK 600
Cdd:TIGR00376 274 NKKTK 278
1B_UPF1_nv_SF1_Hel-like cd21344
1B domain of eukaryotic UPF1 helicase, nidovirus SF1 helicases including coronavirus Nsp13 and ...
330-416 1.23e-16

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: 75.04  E-value: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 330 DDIVVRWDIGLNQKRIAWFFFPKLEMgEVRLAVGDELRLRYRGELHEPWECVGHVIKIPNNVSDEVGLELRRNDNTPADC 409
Cdd:cd21344     1 LIITVRWRLALNDFRGAYFSLEKGKS-QCKPPLGDEIVLTYYGDTVPLWEGIGEVIDLPNTGNDDDALELKGSTTYPLTV 79

                  ....*..
gi 1546556163 410 THNFSVD 416
Cdd:cd21344    80 THIFVLT 86
DEXXQc_SETX cd18042
DEXXQ-box helicase domain of SETX; The RNA/DNA helicase senataxin (SETX) plays a role in ...
475-556 1.95e-16

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: 78.41  E-value: 1.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 475 LNHSQVYAVKSVLQK--PLSLIQGPPGTGKTVTSASIVYHL------------------------AKMNPGQVLVCAPSN 528
Cdd:cd18042     1 LNESQLEAIASALQNspGITLIQGPPGTGKTKTIVGILSVLlagkyrkyyekvkkklrklqrnlnNKKKKNRILVCAPSN 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1546556163 529 VAVDQLTEKIHATGL----------KVVRL-TAKSREAL 556
Cdd:cd18042    81 AAVDEIVLRLLSEGFldgdgrsykpNVVRVgRQELRASI 119
DEXXQc_Upf1-like cd17934
DEXXQ-box helicase domain of Upf1-like helicase; The Upf1-like helicase family includes UPF1, ...
491-534 2.76e-16

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: 75.35  E-value: 2.76e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1546556163 491 LSLIQGPPGTGKTVTSASIVYHLAKMNPG-QVLVCAPSNVAVDQL 534
Cdd:cd17934     1 ISLIQGPPGTGKTTTIAAIVLQLLKGLRGkRVLVTAQSNVAVDNV 45
DEXXQc_Helz-like cd18038
DEXXQ/H-box helicase domain of Helz-like helicase; This subfamily contains HELZ, Mov10L1, and ...
474-565 3.01e-16

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: 78.43  E-value: 3.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 474 ELNHSQVYAVKSVL----QKPLSLIQGPPGTGKTVTSASIVYHLAKMNPG-QVLVCAPSNVAVDQLTEK-IHATGLK--V 545
Cdd:cd18038     1 ELNDEQKLAVRNIVtgtsRPPPYIIFGPPGTGKTVTLVEAILQVLRQPPEaRILVCAPSNSAADLLAERlLNALVTKreI 80
                          90       100
                  ....*....|....*....|
gi 1546556163 546 VRLTAKSREALDSPVSFLTL 565
Cdd:cd18038    81 LRLNAPSRDRASVPPELLPY 100
EEXXEc_NFX1 cd17936
EEXXE-box helicase domain of NFX1; Human NFX1 protein was identified as a protein that ...
475-551 1.47e-14

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: 72.19  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 475 LNHSQVYAVKSVLQKPLSLIQGPPGTGKTVTSASIVY----HLAKMNPGQVLVCAPSNVAVDQLTEKIHATGL-KVVRLT 549
Cdd:cd17936     2 LDPSQLEALKHALTSELALIQGPPGTGKTFLGVKLVRallqNQDLSITGPILVVCYTNHALDQFLEGLLDFGPtKIVRLG 81

                  ..
gi 1546556163 550 AK 551
Cdd:cd17936    82 AR 83
ZBD_UPF1_nv_SF1_Hel-like cd21343
Cys/His rich zinc-binding domain (CH/ZBD) of eukaryotic UPF1 helicase, nidovirus SF1 helicases ...
125-214 4.91e-14

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


Pssm-ID: 439166  Cd Length: 70  Bit Score: 67.13  E-value: 4.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 125 ACRYCGIHSpasVVKCVTCS--KWFCNSrgntsgsHIINHLVRAKHKEVVLHhqsplgeTALECYNCGCRNVFLLGFipa 202
Cdd:cd21343     1 ACYVCGSHT---VVRCGTCIrrPWFCNS-------CIYDHLIRTKHKEVLLA-------SPYVCAGCGESDITLLYF--- 60
                          90
                  ....*....|..
gi 1546556163 203 ksdTVVVLLCRQ 214
Cdd:cd21343    61 ---GGVSYRCVD 69
DExxQc_SF1-N cd17914
DEXQ-box helicase domain of superfamily 1 helicase; The superfamily (SF)1 family members ...
491-536 4.88e-12

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: 63.27  E-value: 4.88e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1546556163 491 LSLIQGPPGTGKTVTSASIVYHLAKMN---PGQVLVCAPSNVAVDQLTE 536
Cdd:cd17914     1 LSLIQGPPGTGKTRVLVKIVAALMQNKngePGRILLVTPTNKAAAQLDN 49
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
479-538 3.45e-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: 61.80  E-value: 3.45e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 479 QVYAVKSVLQKPLSLIQGPPGTGKTVTSASIVYHLAKMNpGQVLVCAPSNVAVDQLTEKI 538
Cdd:cd17933     2 QKAAVRLVLRNRVSVLTGGAGTGKTTTLKALLAALEAEG-KRVVLAAPTGKAAKRLSEST 60
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
428-538 1.14e-10

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: 64.23  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 428 QLAMKTFAVDETSVSGYIyHRLLGHDVEPQVLKTQMPKRFSAHNLpELNHSQVYAVKSVLQK-PLSLIQGPPGTGKTVTS 506
Cdd:COG0507    80 RRYLTRLLEAEQRLARRL-RRLARPALDEADVEAALAALEPRAGI-TLSDEQREAVALALTTrRVSVLTGGAGTGKTTTL 157
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1546556163 507 ASIVYHLAKMNpGQVLVCAPSNVAVDQLTEKI 538
Cdd:COG0507   158 RALLAALEALG-LRVALAAPTGKAAKRLSEST 188
DEXXQc_DNA2 cd18041
DEXXQ-box helicase domain of DNA2; DNA2 (DNA Replication Helicase/Nuclease 2) possesses ...
475-583 1.65e-10

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: 60.71  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 475 LNHSQVYAVKSVLQ-KPLSLIQGPPGTGKTVTSASIVYHLAKMNPgQVLVCAPSNVAVDQLTEKIHATGLKVVRLTAKSR 553
Cdd:cd18041     2 LNKDQRQAIKKVLNaKDYALILGMPGTGKTTTIAALVRILVALGK-SVLLTSYTHSAVDNILLKLKKFGVNFLRLGRLKK 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1546556163 554 EalDSPVSFLTLHEQVHNNDTNVELQKLIQ 583
Cdd:cd18041    81 I--HPDVQEFTLEAILKSCKSVEELESKYE 108
EEXXQc_AQR cd17935
EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds ...
471-540 4.20e-10

EEXXQ-box helicase domain of AQR; Aquarius (AQR) is a multifunctional RNA helicase that binds precursor-mRNA introns at a defined position and is part of a pentameric intron-binding complex (IBC). It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350693 [Multi-domain]  Cd Length: 207  Bit Score: 59.75  E-value: 4.20e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1546556163 471 NLPELNHSQVYAVKSVLQKPLSLIQGPPGTGKTVTSASIVYHLAKMNPGQ-VLVCAPSNVAVDQLTEKIHA 540
Cdd:cd17935     2 NTVKFTPTQIEAIRSGMQPGLTMVVGPPGTGKTDVAVQIISNLYHNFPNQrTLIVTHSNQALNQLFEKIMA 72
DEXXQc_Mov10L1 cd18078
DEXXQ-box helicase domain of Mov10L1; Moloney leukemia virus 10-like protein 1 (Mov10L1) binds ...
475-553 4.87e-10

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: 60.08  E-value: 4.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 475 LNHSQVYAVKSVLQ---KPLS-LIQGPPGTGKTVTSASIVYHLAKMNPG-QVLVCAPSNVAVDQLTEKIHATGL----KV 545
Cdd:cd18078     2 LNELQKEAVKRILGgecRPLPyILFGPPGTGKTVTIIEAILQVVYNLPRsRILVCAPSNSAADLVTSRLHESKVlkpgDM 81

                  ....*...
gi 1546556163 546 VRLTAKSR 553
Cdd:cd18078    82 VRLNAVNR 89
DEXXQc_SF1 cd18043
DEXXQ-box helicase domain of Superfamily 1 helicases; Superfamily 1 (SF1) helicases are ...
476-532 6.25e-10

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: 57.21  E-value: 6.25e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1546556163 476 NHSQVYAVKSVLQKPLSLIQGPPGTGKTVTSASIVYHLAKMNPgQVLVCAPSNVAVD 532
Cdd:cd18043     1 DSSQEAAIISARNGKNVVIQGPPGTGKSQTIANIIANALARGK-RVLFVSEKKAALD 56
AAA_19 pfam13245
AAA domain;
482-543 2.47e-08

AAA domain;


Pssm-ID: 433059 [Multi-domain]  Cd Length: 136  Bit Score: 52.99  E-value: 2.47e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1546556163 482 AVKSVLQKPLSLIQGPPGTGKTVTSASIVYHLAKMN--PGQVLVCAPSNVAVDQLTEkihATGL 543
Cdd:pfam13245   4 AVRTALPSKVVLLTGGPGTGKTTTIRHIVALLVALGgvSFPILLAAPTGRAAKRLSE---RTGL 64
AAA_30 pfam13604
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
474-536 7.72e-08

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


Pssm-ID: 433343 [Multi-domain]  Cd Length: 191  Bit Score: 52.95  E-value: 7.72e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1546556163 474 ELNHSQVYAVKSVLQKP--LSLIQGPPGTGKTvTSASIVYHLAKMNPGQVLVCAPSNVAVDQLTE 536
Cdd:pfam13604   1 TLNAEQAAAVRALLTSGdrVAVLVGPAGTGKT-TALKALREAWEAAGYRVIGLAPTGRAAKVLGE 64
DEXDc smart00487
DEAD-like helicases superfamily;
467-538 7.58e-07

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 50.18  E-value: 7.58e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1546556163  467 FSAHNLPELNHSQVYAVKSVLQKPLS-LIQGPPGTGKTVT-SASIVYHLAKMNPGQVLVCAPSNVAVDQLTEKI 538
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLRDvILAAPTGSGKTLAaLLPALEALKRGKGGRVLVLVPTRELAEQWAEEL 74
ResIII pfam04851
Type III restriction enzyme, res subunit;
474-538 1.48e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 48.44  E-value: 1.48e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1546556163 474 ELNHSQVYAVKSVLQKPLS-----LIQGPPGTGKTVTSASIVYHLAKMNPGQ-VLVCAPSNVAVDQLTEKI 538
Cdd:pfam04851   3 ELRPYQIEAIENLLESIKNgqkrgLIVMATGSGKTLTAAKLIARLFKKGPIKkVLFLVPRKDLLEQALEEF 73
recD TIGR01447
exodeoxyribonuclease V, alpha subunit; This family describes the exodeoxyribonuclease V alpha ...
471-566 6.74e-06

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


Pssm-ID: 273631 [Multi-domain]  Cd Length: 582  Bit Score: 48.99  E-value: 6.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 471 NLPELNhSQVYAVKSVLQKPLSLIQGPPGTGKTVTSASIVYHLAKMNP----GQVLVCAPSNVAVDQLTEKIhatGLKVV 546
Cdd:TIGR01447 142 LLNEQN-WRKTAVALALKSNFSLITGGPGTGKTTTVARLLLALVKQSPkqgkLRIALAAPTGKAAARLAESL---RKAVK 217
                          90       100
                  ....*....|....*....|
gi 1546556163 547 RLTAKSREALDSPVSFLTLH 566
Cdd:TIGR01447 218 NLAAAEALIAALPSEAVTIH 237
DEXXQc_HELZ cd18077
DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that ...
475-532 1.19e-05

DEXXQ-box helicase domain of HELZ; Helicase with zinc finger (HELZ) acts as a helicase that plays a role in RNA metabolism during development. HELZ is a member of the family I class of RNA helicases of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350835 [Multi-domain]  Cd Length: 226  Bit Score: 46.71  E-value: 1.19e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1546556163 475 LNHSQVYAVKSV-----LQKPLSLIQGPPGTGKTVTSASIVYHLAKMNPGQVLVCAPSNVAVD 532
Cdd:cd18077     2 LNAKQKEAVLAIttplsIQLPPVLLIGPFGTGKTFTLAQAVKHILQQPETRILICTHSNSAAD 64
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
493-538 7.75e-05

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: 7.75e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1546556163 493 LIQGPPGTGKTVTSASIVYHLAkmNPGQVLVCAPSNVAVDQLTEKI 538
Cdd:COG1061   104 LVVAPTGTGKTVLALALAAELL--RGKRVLVLVPRRELLEQWAEEL 147
recD PRK10875
exodeoxyribonuclease V subunit alpha;
487-566 1.23e-04

exodeoxyribonuclease V subunit alpha;


Pssm-ID: 236783 [Multi-domain]  Cd Length: 615  Bit Score: 44.93  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 487 LQKPLSLIQGPPGTGKTVTSASIVYHLAKMNPGQVLV---CAPSNVAVDQLTEKIHATgLKVVRLTAKSREALdsPVSFL 563
Cdd:PRK10875  165 LTRRISVISGGPGTGKTTTVAKLLAALIQLADGERCRirlAAPTGKAAARLTESLGKA-LRQLPLTDEQKKRI--PEEAS 241

                  ...
gi 1546556163 564 TLH 566
Cdd:PRK10875  242 TLH 244
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
493-536 1.48e-03

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 39.31  E-value: 1.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1546556163 493 LIQGPPGTGKTVTSASIVYHLAKMNPGQVLVCAPSN-VAVDQLTE 536
Cdd:cd00046     5 LITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKaLALQTAER 49
ZBD_mv_SF1_Hel-like cd21402
Cys/His rich zinc-binding domain (CH/ZBD) of mesnidovirus SF1 helicase and related proteins; ...
126-168 1.63e-03

Cys/His rich zinc-binding domain (CH/ZBD) of mesnidovirus SF1 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. This mesnidovirus group includes the Bontag Baru virus (BBaV) replication helicase encoded on ORF1b and belongs to helicase superfamily 1 (SF1). The CH/ZBD has 3 zinc-finger (ZnF1-3) motifs. Members of this group belong to a family of nindoviral replication helicases which include includes Severe Acute Respiratory Syndrome coronavirus (SARS-CoV) non-structural protein 13 (SARS-Nsp13), 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.


Pssm-ID: 394809  Cd Length: 111  Bit Score: 38.65  E-value: 1.63e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1546556163 126 CRYCGihsPASVVKCVTCSKWFCNSRGNTSGSHIINHLVRAKH 168
Cdd:cd21402     3 CYVCG---ENAYLTCATCERAFCNSADTNHGSHIEQHLQYSGH 42
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
475-582 2.04e-03

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs 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: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 39.08  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 475 LNHSQVYAVKSVLQ-----KPLSLIQGPPGTGKTVTSASIVYHLAKMNPGQ-VLVCAPSNVAVDQLTEKI--HATGLKVV 546
Cdd:cd18032     1 PRYYQQEAIEALEEarekgQRRALLVMATGTGKTYTAAFLIKRLLEANRKKrILFLAHREELLEQAERSFkeVLPDGSFG 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1546556163 547 RLTAKSREALDSPVSFLT---LHEQVHNNDTNVELQKLI 582
Cdd:cd18032    81 NLKGGKKKPDDARVVFATvqtLNKRKRLEKFPPDYFDLI 119
DEXSMc_CoV_Nsp13 cd22649
DEXSM-box helicase domain of coronavirus Nsp13 helicase; Helicases catalyze the NTP-dependent ...
456-553 4.03e-03

DEXSM-box helicase domain of coronavirus Nsp13 helicase; Helicases catalyze the NTP-dependent unwinding of nucleic acid duplexes into single strands and are classified into six superfamilies based on the arrangement of conserved motifs. This family contains coronavirus (CoV) non-structural protein 13 (Nsp13) helicase, including those from highly pathogenic human betaCoVs such as Severe Acute Respiratory Syndrome coronavirus (SARS) and SARS-CoV-2 (also known as 2019 novel CoV (2019-nCoV) or COVID-19 virus). Nsp13 helicase is a component of the viral RNA synthesis replication and transcription complex (RTC). SARS-Nsp13 is strongly inhibited by natural flavonoids, myricetin and scutellarein, and is emerging as a target for development of anti-SARS medications. It contains an N-terminal Cys/His rich zinc-binding domain (CH/ZBD), a stalk domain, a 1B regulatory domain, and an SF1 helicase core that carries a DEAD-box helicase domain. Nsp13 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: 438713 [Multi-domain]  Cd Length: 202  Bit Score: 38.92  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 456 PQVLKTQMPKRFSAHNLPELNHSQVYAVKSVLQKPLSLIQGPPGTGKTvtsaSIVYHLAKMNPG-QVLVCAPSNVAVDQL 534
Cdd:cd22649     1 PQENYVRITGLYPTLNVPEEFSNNVPNYQKIGMQKYTTVQGPPGTGKS----HFAIGLALYYPSaRVVYTACSHAAVDAL 76
                          90       100
                  ....*....|....*....|...
gi 1546556163 535 TEKIHaTGLKVVRLT----AKSR 553
Cdd:cd22649    77 CEKAF-KFLNIDKCTriipARAR 98
betaCoV_Nsp13-helicase cd21722
helicase domain of betacoronavirus non-structural protein 13; This model represents the ...
467-539 4.19e-03

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


Pssm-ID: 409655 [Multi-domain]  Cd Length: 340  Bit Score: 39.78  E-value: 4.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1546556163 467 FSAHNLPELNHSQVYAVKSVLQKPLSLIQGPPGTGKT--VTSASIVYHLAKmnpgqVLVCAPSNVAVDQLTEKIH 539
Cdd:cd21722     3 YPTYNVPEEFQNNVVNYQKIGMKRYCTVQGPPGTGKShlAIGLAVYYPTAR-----VVYTACSHAAVDALCEKAF 72
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
493-611 5.00e-03

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.12  E-value: 5.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163  493 LIQGPPGTGKTVTSASIVYHLAKMNPGQVLVCAPSNVAVDQLTEKIHATGLKVVRLTAKSREALdspvsfltLHEQVHNN 572
Cdd:smart00382   6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRL--------ALALARKL 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1546556163  573 DTNV----ELQKLIQLKQEQGELSASDEKKYKMLKRACEKEIL 611
Cdd:smart00382  78 KPDVlildEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
CoV_Nsp13-helicase cd21718
helicase domain of coronavirus non-structural protein 13; This model represents the helicase ...
468-537 6.52e-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: 39.05  E-value: 6.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1546556163 468 SAHNLPELNHSQVYAVKSVLQKPLSLIQGPPGTGKTvtsaSIVYHLAKMNPG-QVLVCAPSNVAVDQLTEK 537
Cdd:cd21718     4 PGNVIPHDFSNHVPSYQKIGKQKYTTVQGPPGTGKS----HFAIGLALYYPGaRIVYTACSHAAVDALCEK 70
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
479-558 8.58e-03

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 37.29  E-value: 8.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1546556163 479 QVYAVKSVLQKP---LSLIQGPPGTGKTVTSASIVYHLAKMNpgqVLVCAPSNVAVDQLTEKIHATGLKVV--RLTAKSR 553
Cdd:cd17926     5 QEEALEAWLAHKnnrRGILVLPTGSGKTLTALALIAYLKELR---TLIVVPTDALLDQWKERFEDFLGDSSigLIGGGKK 81

                  ....*
gi 1546556163 554 EALDS 558
Cdd:cd17926    82 KDFDD 86
 
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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