3.6.1.15: nucleoside-triphosphate phosphatase
This is an abbreviated version!
For detailed information about nucleoside-triphosphate phosphatase, go to the full flat file.
Word Map on EC 3.6.1.15
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3.6.1.15
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adp
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ectonucleotidases
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purinergic
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viruses
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unwind
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5'-nucleotidase
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potato
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single-stranded
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non-structural
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purine
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platelet
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virion
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ecto-5\'-nucleotidase
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deaminase
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sars-cov-2
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coronavirus
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vaccinia
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nucleotidase
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toxoplasma
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gondii
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apyrase
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ecto-nucleoside
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polyproteins
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duplex
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nsp2
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ecto-atpase
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nucleocytoplasmic
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flaviviridae
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tachyzoite
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ecto-enzymes
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polynucleotides
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3.6.1.5
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mutt
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guanylyltransferase
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ntp-binding
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reoviridae
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primase
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encapsidated
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positive-stranded
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bluetongue
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polyu
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entpd1
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phosphohydrolytic
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replicase
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reovirus
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ssrna
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adpase
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potexvirus
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surface-located
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medicine
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nucleotide-mediated
- 3.6.1.15
- adp
- ectonucleotidases
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purinergic
- viruses
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unwind
- 5'-nucleotidase
- potato
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single-stranded
-
non-structural
- purine
- platelet
- virion
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ecto-5\'-nucleotidase
- deaminase
- sars-cov-2
- coronavirus
- vaccinia
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nucleotidase
- toxoplasma
- gondii
- apyrase
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ecto-nucleoside
- polyproteins
- duplex
- nsp2
- ecto-atpase
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nucleocytoplasmic
- flaviviridae
- tachyzoite
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ecto-enzymes
- polynucleotides
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3.6.1.5
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mutt
-
guanylyltransferase
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ntp-binding
- reoviridae
- primase
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encapsidated
-
positive-stranded
- bluetongue
- polyu
- entpd1
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phosphohydrolytic
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replicase
- reovirus
- ssrna
- adpase
- potexvirus
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surface-located
- medicine
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nucleotide-mediated
Reaction
Synonyms
AAA-type nucleoside triphosphatase phosphohydrolase, ankyrin repeat-rich membrane spanning protein, cell division control protein Cdc48, DEAH-box Prp22 protein, DEAH-box splicing factor Prp22, DExH-Box NTPase, DR_0079, germ-cell-specific leucine-rich repeat protein, GP086L protein, HCR-NTPase, HrpB, HrpB NTPase, human cancer-related nucleoside triphosphatase, KAP NTPase, Kidins220, kinase D interacting substance of 220 kDa, LDBPK_100150, LdNTPDase2, LINF_150005200, LiNTPDase1, LMXM_10_0170, LMXM_15_0030, LmxNTPDase1, LmxNTPDase2, M86L protein, MC100R, Mg2+-dependent NTPase, More, Msm0858, NALP14, non-specific nucleoside triphosphatase, nonstructural protein 13, NPH I, NS3, NS3 protein, NS3FL, nsp13, NTP1, NTP3, NTPase, NTPase 1, NTPase 2, NTPase-I, NTPase-II, NTPase/helicase, NTPDase, NTPDase 1, NTPDase1, NTPDase2, nucleic acid-independent nucleoside triphosphatase, nucleoside 5-triphosphatase, nucleoside triphosphatase, nucleoside triphosphatase (NTPase)/helicase, nucleoside triphosphate diphospho-hydrolase, nucleoside triphosphate diphosphohydrolase, nucleoside triphosphate diphosphohydrolase 1, nucleoside triphosphate hydrolase, nucleoside triphosphate hydrolases I, nucleoside triphosphate hydrolases II, nucleoside triphosphate phosphohydrolase, nucleoside triphosphate phosphohydrolase I, nucleoside-5-triphosphate phosphohydrolase, nucleoside-triphosphatase 1, nucleoside-triphosphatase 2, nucleotide 5'-triphosphatase, P-loop NTPase, phosphatase, nucleoside tri-, PilB, PilT, PilU, polypeptide p41, protein NS3, PVA coat protein, PVA CP, PVx coat protein, PVX CP, Rad55B, RNA-dependent nucleoside triphosphatase, SHVp41, Sso0909, T4P motor protein, type IV pilus motor protein, YtkD
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3.6.1.15 nucleoside-triphosphate phosphataseAdvanced search results
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results (General Information
General Information on EC 3.6.1.15 - nucleoside-triphosphate phosphatase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
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evolution of cation binding in the active sites of P-loop nucleoside triphosphatases in relation to the basic catalytic mechanism, overview
evolution
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evolution of cation binding in the active sites of P-loop nucleoside triphosphatases in relation to the basic catalytic mechanism, overview
evolution
nucleoside triphosphate diphosphohydrolases (NTPDases) belong to the GDA1/CD39 protein superfamily, E-NTPDase family. Existence of several isoforms with different specificities with respect to divalent cations (magnesium, calcium, manganese, and zinc) and substrates. Sequence comparisons of regions of the putative Leishmania NTPDases with human CD39 (NTPDase 1)
evolution
nucleoside triphosphate diphosphohydrolases (NTPDases) belong to the GDA1/CD39 protein superfamily, E-NTPDase family. Existence of several isoforms with different specificities with respect to divalent cations (magnesium, calcium, manganese, and zinc) and substrates. Sequence comparisons of regions of the putative Leishmania NTPDases with human CD39 (NTPDase 1)
evolution
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nucleoside triphosphate diphosphohydrolases (NTPDases) belong to the GDA1/CD39 protein superfamily, E-NTPDase family. Existence of several isoforms with different specificities with respect to divalent cations (magnesium, calcium, manganese, and zinc) and substrates. The sequential hydrolysis of extracellular ATP to adenosine indicates that not only E-NTPDase but also 5'-nucleotidases are present in the plasma membrane. Sequence comparisons of regions of the putative Leishmania NTPDases with human CD39 (NTPDase 1)
evolution
Sequence similarity analysis and distance tree show high level (98%) of identity between Trypanosoma evansi and Trypanosoma brucei brucei (UniProt ID D6XLB5) NTPDase. Trypanosoma evansi NTPDase encloses the GDA1/CD39 nucleoside phosphatase family domain as well as exopolyphosphatase (Ppx-GppA) domain following five apyrase conserved regions (ACR)
evolution
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nucleoside triphosphate diphosphohydrolases (NTPDases) belong to the GDA1/CD39 protein superfamily, E-NTPDase family. Existence of several isoforms with different specificities with respect to divalent cations (magnesium, calcium, manganese, and zinc) and substrates. Sequence comparisons of regions of the putative Leishmania NTPDases with human CD39 (NTPDase 1)
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evolution
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enzyme NPH I is a member of the DEXH box helicase family
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evolution
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nucleoside triphosphate diphosphohydrolases (NTPDases) belong to the GDA1/CD39 protein superfamily, E-NTPDase family. Existence of several isoforms with different specificities with respect to divalent cations (magnesium, calcium, manganese, and zinc) and substrates. Sequence comparisons of regions of the putative Leishmania NTPDases with human CD39 (NTPDase 1)
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malfunction
knockouts of isozymes NTPase II and I are not essential for growth or virulence in CD1 mice and do not affect STAT1 transcription. In contrast to the NTPase I mutant, deletion of NTPase II causes only a mild change in inhibition of the FLUC activity in both HeLa cells and RAW-264.7 macrophages
malfunction
knockouts of isozymes NTPase II and I are not essential for growth or virulence in CD1 mice and do not affect STAT1 transcription. The NTPase I knockout in the type I strain mirrors the less inhibitory phenotype of type II (ME49) and III (CTG) strains, which naturally lack NTPase I
malfunction
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mutation of the conserved NTPase motifs blocks enzyme activity and viral replication in cells. The RNA destabilization activity is not affected by mutagenesis of the conserved motifs of NTPase
malfunction
simultaneous mutations of the D1 and D2 active-site motifs are required to abolish ATPase activity. ATPase activity is effaced by mutation of the putative D2 arginine finger, suggesting that Msm0858 might oligomerize during the ATPase reaction cycle. A truncated variant Msm0858 (amino acids 212-745) that lacks the N domain is characterized as a catalytically active homodimer
malfunction
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simultaneous mutations of the D1 and D2 active-site motifs are required to abolish ATPase activity. ATPase activity is effaced by mutation of the putative D2 arginine finger, suggesting that Msm0858 might oligomerize during the ATPase reaction cycle. A truncated variant Msm0858 (amino acids 212-745) that lacks the N domain is characterized as a catalytically active homodimer
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malfunction
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simultaneous mutations of the D1 and D2 active-site motifs are required to abolish ATPase activity. ATPase activity is effaced by mutation of the putative D2 arginine finger, suggesting that Msm0858 might oligomerize during the ATPase reaction cycle. A truncated variant Msm0858 (amino acids 212-745) that lacks the N domain is characterized as a catalytically active homodimer
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physiological function
bacterial DExH-box proteins play important roles as co-/posttranscriptional gene regulators, aiding in the adaptation of bacteria to stress conditions. HrpB does not affect curli and biofilm formation in Escherichia coli K-12
physiological function
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in parasites of the genus Leishmania, the causative agents of leishmaniasis, two NTPDase isoforms, termed NTPDase-1 and NTPDase-2 have been described. Independently of their cellular localization, whether cell-surface localized, secreted or targeted to other organelles, in some Leishmania species these NTPDases are involved in parasite growth, infectivity, and virulence. Nucleoside triphosphate diphosphohydrolases (NTPDases) catalyze the hydrolysis of a variety of nucleoside tri- and diphosphates to the monophosphate forms and have been implicated in adenosine acquisition, the regulation of blood clotting, inflammatory responses, immune reactions, and microbial virulence
physiological function
in parasites of the genus Leishmania, the causative agents of leishmaniasis, two NTPDase isoforms, termed NTPDase-1 and NTPDase-2 have been described. Independently of their cellular localization, whether cell-surface localized, secreted or targeted to other organelles, in some Leishmania species these NTPDases are involved in parasite growth, infectivity, and virulence. Nucleoside triphosphate diphosphohydrolases (NTPDases) catalyze the hydrolysis of a variety of nucleoside tri- and diphosphates to the monophosphate forms and have been implicated in adenosine acquisition, the regulation of blood clotting, inflammatory responses, immune reactions, and microbial virulence
physiological function
in parasites of the genus Leishmania, the causative agents of leishmaniasis, two NTPDase isoforms, termed NTPDase-1 and NTPDase-2 have been described. Independently of their cellular localization, whether cell-surface localized, secreted or targeted to other organelles, in some Leishmania species these NTPDases are involved in parasite growth, infectivity, and virulence. Nucleoside triphosphate diphosphohydrolases (NTPDases) catalyze the hydrolysis of a variety of nucleoside tri- and diphosphates to the monophosphate forms and have been implicated in adenosine acquisition, the regulation of blood clotting, inflammatory responses, immune reactions, and microbial virulence
physiological function
nucleoside triphosphate diphospho-hydrolases (NTPDases) catalyze the hydrolysis of several nucleosides tri and diphosphate playing major roles in eukaryotes including purinergic signaling, inflammation, hemostasis, purine salvage and host-pathogen interactions
physiological function
strong negative influence of NTPase I on the FLUC activity in both HeLa cells and RAW-264.7 macrophages
physiological function
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in parasites of the genus Leishmania, the causative agents of leishmaniasis, two NTPDase isoforms, termed NTPDase-1 and NTPDase-2 have been described. Independently of their cellular localization, whether cell-surface localized, secreted or targeted to other organelles, in some Leishmania species these NTPDases are involved in parasite growth, infectivity, and virulence. Nucleoside triphosphate diphosphohydrolases (NTPDases) catalyze the hydrolysis of a variety of nucleoside tri- and diphosphates to the monophosphate forms and have been implicated in adenosine acquisition, the regulation of blood clotting, inflammatory responses, immune reactions, and microbial virulence
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physiological function
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in parasites of the genus Leishmania, the causative agents of leishmaniasis, two NTPDase isoforms, termed NTPDase-1 and NTPDase-2 have been described. Independently of their cellular localization, whether cell-surface localized, secreted or targeted to other organelles, in some Leishmania species these NTPDases are involved in parasite growth, infectivity, and virulence. Nucleoside triphosphate diphosphohydrolases (NTPDases) catalyze the hydrolysis of a variety of nucleoside tri- and diphosphates to the monophosphate forms and have been implicated in adenosine acquisition, the regulation of blood clotting, inflammatory responses, immune reactions, and microbial virulence
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additional information
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antibodies against B domain recognize Leishmania infantum promastigote NTPDase 1 and have in vitro antileishmanial activity. IgG1 and IgG2 subclasses binding-epitopes within B domain, IgG1 and IgG2 seropositivity for r-pot B domain recombinant polypeptide, overview
additional information
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combined comparative structure analysis with molecular dynamics simulations of Mg-ATP and Mg-GTP complexes in water and in the presence of potassium, sodium, or ammonium ions. In all analyzed structures of diverse P-loop NTPases, the conserved P-loop motif keeps the triphosphate chain of bound NTPs (or their analogues) in an extended, catalytically prone conformation, similar to that imposed on NTPs in water by potassium or ammonium ions. Mg-NTP complexes and their binding in the active sites of P-loop NTPases, substrate binding, structure overview. Catalytic activity of P-loop NTPases typically depends upon their interaction with other proteins or domains of the same protein or RNA/DNA molecules, upon this interaction, activating Arg or Lys fingers are inserted into the catalytic site. Some P-loop NTPases functionally depend not on Arg/Lys fingers, but on monovalent cations. Molecular dynamics simulations, overview
additional information
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combined comparative structure analysis with molecular dynamics simulations of Mg-ATP and Mg-GTP complexes in water and in the presence of potassium, sodium, or ammonium ions. In all analyzed structures of diverse P-loop NTPases, the conserved P-loop motif keeps the triphosphate chain of bound NTPs (or their analogues) in an extended, catalytically prone conformation, similar to that imposed on NTPs in water by potassium or ammonium ions. Mg-NTP complexes and their binding in the active sites of P-loop NTPases, substrate binding, structure overview. Catalytic activity of P-loop NTPases typically depends upon their interaction with other proteins or domains of the same protein or RNA/DNA molecules, upon this interaction, activating Arg or Lys fingers are inserted into the catalytic site. Some P-loop NTPases functionally depend not on Arg/Lys fingers, but on monovalent cations. Molecular dynamics simulations, overview
additional information
crystal structure analysis, detailed overview. A globular head is composed of dual RecA, winged-helix, helical bundle and oligonucleotide/oligosaccharide-binding domains, resembling a compact version of eukaryotic DExH-box proteins. Additionally, HrpB harbors a C-terminal region not found in proteins with known structure, which bestows the protein with unique interaction potential. The protein binds RNA but not DNA, hydrolyzes all nucleoside triphosphates in an RNA-stimulated manner, but does not unwind diverse model RNAs in vitro. The entire structure can be divided into seven domains or regions, i.e., two RecA-like domains (RecA1, residues 1-178, and RecA2, residues 179-355), a WH domain (residues 356-416), an HB domain (residues 417-498), an OB domain (residues 499-566), a connector element (CON, residues 567-602) and a C-terminal region (CTR, residues 603-805). The RecA1, RecA2, WH, HB, and OB domains are arranged in a circular fashion, forming the head module, while the remainder of the protein, CON and CTR, forms the C-terminal stalk. Structure comparisons
additional information
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crystal structure analysis, detailed overview. A globular head is composed of dual RecA, winged-helix, helical bundle and oligonucleotide/oligosaccharide-binding domains, resembling a compact version of eukaryotic DExH-box proteins. Additionally, HrpB harbors a C-terminal region not found in proteins with known structure, which bestows the protein with unique interaction potential. The protein binds RNA but not DNA, hydrolyzes all nucleoside triphosphates in an RNA-stimulated manner, but does not unwind diverse model RNAs in vitro. The entire structure can be divided into seven domains or regions, i.e., two RecA-like domains (RecA1, residues 1-178, and RecA2, residues 179-355), a WH domain (residues 356-416), an HB domain (residues 417-498), an OB domain (residues 499-566), a connector element (CON, residues 567-602) and a C-terminal region (CTR, residues 603-805). The RecA1, RecA2, WH, HB, and OB domains are arranged in a circular fashion, forming the head module, while the remainder of the protein, CON and CTR, forms the C-terminal stalk. Structure comparisons
additional information
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MNV NS3 has three domains: the N-terminal domain (NTD, 1-105) with a linker (106-129), the core domain (130-285) and the C-terminal domain (CTD, 290-364). The conserved motifs are crucial to the NTPase activity of NS3
additional information
mutational analysis of the A-box and B-box motifs indicated that the D1 and D2 AAA domains are both capable of ATP hydrolysis, structure comparisons of the enzymes with mammalian protein p97, homology of the tandem AAA domains of Msm0858 and p97, overview
additional information
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mutational analysis of the A-box and B-box motifs indicated that the D1 and D2 AAA domains are both capable of ATP hydrolysis, structure comparisons of the enzymes with mammalian protein p97, homology of the tandem AAA domains of Msm0858 and p97, overview
additional information
Leishmania infantum MHOM/BR/1972/BH46
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antibodies against B domain recognize Leishmania infantum promastigote NTPDase 1 and have in vitro antileishmanial activity. IgG1 and IgG2 subclasses binding-epitopes within B domain, IgG1 and IgG2 seropositivity for r-pot B domain recombinant polypeptide, overview
-
additional information
-
mutational analysis of the A-box and B-box motifs indicated that the D1 and D2 AAA domains are both capable of ATP hydrolysis, structure comparisons of the enzymes with mammalian protein p97, homology of the tandem AAA domains of Msm0858 and p97, overview
-
additional information
-
mutational analysis of the A-box and B-box motifs indicated that the D1 and D2 AAA domains are both capable of ATP hydrolysis, structure comparisons of the enzymes with mammalian protein p97, homology of the tandem AAA domains of Msm0858 and p97, overview
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