diphthine--ammonia ligase family protein belonging to the adenine nucleotide alpha hydrolase (AANH) superfamily, similar to diphthine--ammonia ligase, an amidase that catalyzes the conversion of diphthine to diphthamide using ammonium and ATP
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
2-219
2.91e-112
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus furiosus putative ATP pyrophosphatase PF0828 and Pyrococcus horikoshii PH1257. They belong to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.
:
Pssm-ID: 467498 Cd Length: 211 Bit Score: 321.93 E-value: 2.91e-112
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
2-219
2.91e-112
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus furiosus putative ATP pyrophosphatase PF0828 and Pyrococcus horikoshii PH1257. They belong to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.
Pssm-ID: 467498 Cd Length: 211 Bit Score: 321.93 E-value: 2.91e-112
MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two ...
1-242
3.87e-67
MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two apparent ortholog families in the Archaea, one of which is universal among the first four completed archaeal genomes, and YLR143W, a much longer protein from Saccharomyces cerevisiae. The domain comprises the full length of the archaeal proteins and the first third of the yeast protein.
Pssm-ID: 273000 Cd Length: 223 Bit Score: 207.71 E-value: 3.87e-67
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step ...
1-242
1.09e-45
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step of diphthamide biosynthesis using ammonium and ATP. 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). In some members of this family, this domain is associated with pfam01042. The enzyme classification is EC:6.3.1.14.
Pssm-ID: 280139 Cd Length: 219 Bit Score: 152.65 E-value: 1.09e-45
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
2-219
2.91e-112
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus furiosus putative ATP pyrophosphatase PF0828 and Pyrococcus horikoshii PH1257. They belong to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.
Pssm-ID: 467498 Cd Length: 211 Bit Score: 321.93 E-value: 2.91e-112
MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two ...
1-242
3.87e-67
MJ0570-related uncharacterized domain; Proteins with this uncharacterized domain include two apparent ortholog families in the Archaea, one of which is universal among the first four completed archaeal genomes, and YLR143W, a much longer protein from Saccharomyces cerevisiae. The domain comprises the full length of the archaeal proteins and the first third of the yeast protein.
Pssm-ID: 273000 Cd Length: 223 Bit Score: 207.71 E-value: 3.87e-67
arCOG00187 universal archaeal metal-binding-domain/4Fe-4S-binding-domain containing ABC transporter, ATP-binding protein; This protein consists of an N-terminal possible metal-binding domain (pfam04068) followed by a 4Fe-4S cluster binding domain (pfam00037) followed by a C-terminal ABC transporter, ATP-binding domain (pfam00005). This combination of N-terminal domains is observed in the RNase L inhibitor, RLI. This model has the same scope as an archaeal COG (arCOG00187) and is found in all completely sequenced archaea and does not recognize any known non-archaeal genes.
Pssm-ID: 188368 Cd Length: 218 Bit Score: 201.33 E-value: 9.81e-65
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step ...
1-242
1.09e-45
Diphthamide synthase; Diphthamide_syn, diphthamide synthase, catalyzes the last amidation step of diphthamide biosynthesis using ammonium and ATP. 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). In some members of this family, this domain is associated with pfam01042. The enzyme classification is EC:6.3.1.14.
Pssm-ID: 280139 Cd Length: 219 Bit Score: 152.65 E-value: 1.09e-45
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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