nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
217-382
5.11e-14
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
The actual alignment was detected with superfamily member cd02165:
Pssm-ID: 469580 [Multi-domain] Cd Length: 192 Bit Score: 69.96 E-value: 5.11e-14
Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, ...
25-102
7.53e-04
Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, and is thought to be specifically required at some stage in the process of transformation. This Pfam family consists of putative competence-damaged proteins from the cin operon. Some members of this family have nicotinamide mononucleotide (NMN) deamidase activity.
The actual alignment was detected with superfamily member pfam02464:
Pssm-ID: 480889 Cd Length: 155 Bit Score: 39.82 E-value: 7.53e-04
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate mononucleotide (NMN/ NaMN)adenylyltransferase (NMNAT). NMNAT represents the primary bacterial and eukaryotic adenylyltransferases for nicotinamide-nucleotide and for the deamido form, nicotinate nucleotide. It is an indispensable enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. Human NMNAT displays unique dual substrate specificity toward both NMN and NaMN, and can participate in both de novo and salvage pathways of NAD synthesis.
Pssm-ID: 185680 [Multi-domain] Cd Length: 192 Bit Score: 69.96 E-value: 5.11e-14
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
214-382
1.29e-10
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; Nicotinate-nucleotide adenylyltransferase NadD is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 440677 [Multi-domain] Cd Length: 197 Bit Score: 60.14 E-value: 1.29e-10
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
220-381
6.43e-09
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the predominant bacterial/eukaryotic adenylyltransferase for nicotinamide-nucleotide, its deamido form nicotinate nucleotide, or both. The first activity, nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1), synthesizes NAD by the salvage pathway, while the second, nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) synthesizes the immediate precursor of NAD by the de novo pathway. In E. coli, NadD activity is biased toward the de novo pathway while salvage activity is channeled through the multifunctional NadR protein, but this division of labor may be exceptional. The given name of this model, nicotinate (nicotinamide) nucleotide adenylyltransferase, reflects the lack of absolute specificity with respect to substrate amidation state in most species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
Pssm-ID: 273101 [Multi-domain] Cd Length: 193 Bit Score: 55.40 E-value: 6.43e-09
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
217-382
9.15e-07
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.
Pssm-ID: 396172 [Multi-domain] Cd Length: 134 Bit Score: 47.70 E-value: 9.15e-07
Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, ...
25-102
7.53e-04
Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, and is thought to be specifically required at some stage in the process of transformation. This Pfam family consists of putative competence-damaged proteins from the cin operon. Some members of this family have nicotinamide mononucleotide (NMN) deamidase activity.
Pssm-ID: 460565 Cd Length: 155 Bit Score: 39.82 E-value: 7.53e-04
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; ...
37-102
3.80e-03
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; Nicotinamide mononucleotide (NMN) deamidase PncC is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 441155 Cd Length: 154 Bit Score: 37.72 E-value: 3.80e-03
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate mononucleotide (NMN/ NaMN)adenylyltransferase (NMNAT). NMNAT represents the primary bacterial and eukaryotic adenylyltransferases for nicotinamide-nucleotide and for the deamido form, nicotinate nucleotide. It is an indispensable enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. Human NMNAT displays unique dual substrate specificity toward both NMN and NaMN, and can participate in both de novo and salvage pathways of NAD synthesis.
Pssm-ID: 185680 [Multi-domain] Cd Length: 192 Bit Score: 69.96 E-value: 5.11e-14
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
214-382
1.29e-10
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; Nicotinate-nucleotide adenylyltransferase NadD is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 440677 [Multi-domain] Cd Length: 197 Bit Score: 60.14 E-value: 1.29e-10
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
220-381
6.43e-09
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the predominant bacterial/eukaryotic adenylyltransferase for nicotinamide-nucleotide, its deamido form nicotinate nucleotide, or both. The first activity, nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1), synthesizes NAD by the salvage pathway, while the second, nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) synthesizes the immediate precursor of NAD by the de novo pathway. In E. coli, NadD activity is biased toward the de novo pathway while salvage activity is channeled through the multifunctional NadR protein, but this division of labor may be exceptional. The given name of this model, nicotinate (nicotinamide) nucleotide adenylyltransferase, reflects the lack of absolute specificity with respect to substrate amidation state in most species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
Pssm-ID: 273101 [Multi-domain] Cd Length: 193 Bit Score: 55.40 E-value: 6.43e-09
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
217-382
9.15e-07
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.
Pssm-ID: 396172 [Multi-domain] Cd Length: 134 Bit Score: 47.70 E-value: 9.15e-07
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
215-234
5.56e-04
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.
Pssm-ID: 272920 [Multi-domain] Cd Length: 66 Bit Score: 38.06 E-value: 5.56e-04
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
215-305
5.81e-04
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown.
Pssm-ID: 185678 [Multi-domain] Cd Length: 143 Bit Score: 39.73 E-value: 5.81e-04
Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, ...
25-102
7.53e-04
Competence-damaged protein; CinA is the first gene in the competence-inducible (cin) operon, and is thought to be specifically required at some stage in the process of transformation. This Pfam family consists of putative competence-damaged proteins from the cin operon. Some members of this family have nicotinamide mononucleotide (NMN) deamidase activity.
Pssm-ID: 460565 Cd Length: 155 Bit Score: 39.82 E-value: 7.53e-04
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; ...
37-102
3.80e-03
Nicotinamide mononucleotide (NMN) deamidase PncC [Coenzyme transport and metabolism]; Nicotinamide mononucleotide (NMN) deamidase PncC is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 441155 Cd Length: 154 Bit Score: 37.72 E-value: 3.80e-03
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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