2-(3-amino-3-carboxypropyl)histidine synthase subunit 1/2 (Dph1/Dph2) is required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue
Putative diphthamide synthesis protein; Diphthamide_syn, diphthamide synthase, catalyzes the ...
76-377
3.18e-163
Putative diphthamide synthesis protein; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step of diphthamide biosynthesis using ammonium and ATP. Swiss:Q16439 is a candidate tumour suppressor gene. DPH2 from yeast, which confers resistance to diphtheria toxin has been found to be involved in diphthamide synthesis. Diphtheria toxin inhibits eukaryotic protein synthesis by ADP-ribosylating diphthamide, a post-translationally modified histidine residue present in EF2. Diphthamide synthase is evolutionarily conserved in eukaryotes. Diphthamide is a post-translationally modified histidine residue found on archaeal and eukaryotic translation elongation factor 2 (eEF-2).
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Pssm-ID: 460365 Cd Length: 302 Bit Score: 461.61 E-value: 3.18e-163
Putative diphthamide synthesis protein; Diphthamide_syn, diphthamide synthase, catalyzes the ...
76-377
3.18e-163
Putative diphthamide synthesis protein; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step of diphthamide biosynthesis using ammonium and ATP. Swiss:Q16439 is a candidate tumour suppressor gene. DPH2 from yeast, which confers resistance to diphtheria toxin has been found to be involved in diphthamide synthesis. Diphtheria toxin inhibits eukaryotic protein synthesis by ADP-ribosylating diphthamide, a post-translationally modified histidine residue present in EF2. Diphthamide synthase is evolutionarily conserved in eukaryotes. Diphthamide is a post-translationally modified histidine residue found on archaeal and eukaryotic translation elongation factor 2 (eEF-2).
Pssm-ID: 460365 Cd Length: 302 Bit Score: 461.61 E-value: 3.18e-163
diphthamide biosynthesis enzyme Dph1/Dph2 domain; Archaea and Eukaryotes, but not Eubacteria, ...
53-367
4.78e-150
diphthamide biosynthesis enzyme Dph1/Dph2 domain; Archaea and Eukaryotes, but not Eubacteria, share the property of having a covalently modified residue, 2'-[3-carboxamido-3-(trimethylammonio)propyl]histidine, as a part of a cytosolic protein. The modified His, termed diphthamide, is part of translation elongation factor EF-2 and is the site for ADP-ribosylation by diphtheria toxin. This model includes both Dph1 and Dph2 from Saccharomyces cerevisiae, although only Dph2 is found in the Archaea (see TIGR03682). Dph2 has been shown to act analogously to the radical SAM (rSAM) family (pfam04055), with 4Fe-4S-assisted cleavage of S-adenosylmethionine to create a free radical, but a different organic radical than in rSAM.
Pssm-ID: 273013 Cd Length: 318 Bit Score: 428.54 E-value: 4.78e-150
Putative diphthamide synthesis protein; Diphthamide_syn, diphthamide synthase, catalyzes the ...
76-377
3.18e-163
Putative diphthamide synthesis protein; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step of diphthamide biosynthesis using ammonium and ATP. Swiss:Q16439 is a candidate tumour suppressor gene. DPH2 from yeast, which confers resistance to diphtheria toxin has been found to be involved in diphthamide synthesis. Diphtheria toxin inhibits eukaryotic protein synthesis by ADP-ribosylating diphthamide, a post-translationally modified histidine residue present in EF2. Diphthamide synthase is evolutionarily conserved in eukaryotes. Diphthamide is a post-translationally modified histidine residue found on archaeal and eukaryotic translation elongation factor 2 (eEF-2).
Pssm-ID: 460365 Cd Length: 302 Bit Score: 461.61 E-value: 3.18e-163
diphthamide biosynthesis enzyme Dph1/Dph2 domain; Archaea and Eukaryotes, but not Eubacteria, ...
53-367
4.78e-150
diphthamide biosynthesis enzyme Dph1/Dph2 domain; Archaea and Eukaryotes, but not Eubacteria, share the property of having a covalently modified residue, 2'-[3-carboxamido-3-(trimethylammonio)propyl]histidine, as a part of a cytosolic protein. The modified His, termed diphthamide, is part of translation elongation factor EF-2 and is the site for ADP-ribosylation by diphtheria toxin. This model includes both Dph1 and Dph2 from Saccharomyces cerevisiae, although only Dph2 is found in the Archaea (see TIGR03682). Dph2 has been shown to act analogously to the radical SAM (rSAM) family (pfam04055), with 4Fe-4S-assisted cleavage of S-adenosylmethionine to create a free radical, but a different organic radical than in rSAM.
Pssm-ID: 273013 Cd Length: 318 Bit Score: 428.54 E-value: 4.78e-150
diphthamide biosynthesis enzyme Dph2; Members of this family are the archaeal protein Dph2, ...
68-379
4.07e-51
diphthamide biosynthesis enzyme Dph2; Members of this family are the archaeal protein Dph2, members of the universal archaeal protein family designated arCOG04112. The chemical function of this protein is analogous to the radical SAM family (pfam04055), although the sequence is not homologous. The chemistry involves [4Fe-4S]-aided formation of a 3-amino-3-carboxypropyl radical rather than the canonical 5'-deoxyadenosyl radical of the radical SAM family.
Pssm-ID: 274721 Cd Length: 308 Bit Score: 174.80 E-value: 4.07e-51
diphthamide biosynthesis protein 2; This protein has been shown in Saccharomyces cerevisiae to ...
55-372
2.35e-28
diphthamide biosynthesis protein 2; This protein has been shown in Saccharomyces cerevisiae to be one of several required for the modification of a particular histidine residue of translation elongation factor 2 to diphthamide. This modified site can then become the target for ADP-ribosylation by diphtheria toxin. [Protein fate, Protein modification and repair]
Pssm-ID: 272990 Cd Length: 496 Bit Score: 116.96 E-value: 2.35e-28
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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