ribonucleoside-triphosphate reductase, adenosylcobalamin-dependent; This model represents a ...
2-674
0e+00
ribonucleoside-triphosphate reductase, adenosylcobalamin-dependent; This model represents a group of adenosylcobalamin(B12)-dependent ribonucleotide reductases (RNR) related to the characterized species from Lactococcus leichmannii. RNR's are responsible for the conversion of the ribose sugar of RNA into the deoxyribose sugar of DNA. This is the rate-limiting step of DNA biosynthesis. Thus model identifies NrdJ enzymes only in cyanobacteria, lactococcus and certain bacteriophage. A separate model (TIGR02504) identifies a larger group of divergent B12-dependent RNR's. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
The actual alignment was detected with superfamily member TIGR02505:
Pssm-ID: 274169 [Multi-domain] Cd Length: 713 Bit Score: 756.76 E-value: 0e+00
ribonucleoside-triphosphate reductase, adenosylcobalamin-dependent; This model represents a ...
2-674
0e+00
ribonucleoside-triphosphate reductase, adenosylcobalamin-dependent; This model represents a group of adenosylcobalamin(B12)-dependent ribonucleotide reductases (RNR) related to the characterized species from Lactococcus leichmannii. RNR's are responsible for the conversion of the ribose sugar of RNA into the deoxyribose sugar of DNA. This is the rate-limiting step of DNA biosynthesis. Thus model identifies NrdJ enzymes only in cyanobacteria, lactococcus and certain bacteriophage. A separate model (TIGR02504) identifies a larger group of divergent B12-dependent RNR's. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
Pssm-ID: 274169 [Multi-domain] Cd Length: 713 Bit Score: 756.76 E-value: 0e+00
Class II ribonucleotide reductase, monomeric form; Ribonucleotide reductase (RNR) catalyzes ...
10-673
2.34e-134
Class II ribonucleotide reductase, monomeric form; Ribonucleotide reductase (RNR) catalyzes the reductive synthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, and bacteriophage, use a diiron-tyrosyl radical. Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs, found in anaerobic bacteria, bacteriophage, and archaea, use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. Many organisms have more than one class of RNR present in their genomes. All three RNRs have a ten-stranded alpha-beta barrel domain that is structurally similar to the domain of PFL (pyruvate formate lyase). Class II RNRs are found in bacteria that can live under both aerobic and anaerobic conditions. Many, but not all members of this class, are found to be homodimers. This particular subfamily is found to be active as a monomer. Adenosylcobalamin interacts directly with an active site cysteine to form the reactive cysteine radical.
Pssm-ID: 153085 [Multi-domain] Cd Length: 658 Bit Score: 409.59 E-value: 2.34e-134
Ribonucleotide reductase alpha subunit [Nucleotide transport and metabolism]; Ribonucleotide ...
12-632
3.09e-55
Ribonucleotide reductase alpha subunit [Nucleotide transport and metabolism]; Ribonucleotide reductase alpha subunit is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 439979 [Multi-domain] Cd Length: 665 Bit Score: 200.03 E-value: 3.09e-55
ribonucleoside-triphosphate reductase, adenosylcobalamin-dependent; This model represents a ...
2-674
0e+00
ribonucleoside-triphosphate reductase, adenosylcobalamin-dependent; This model represents a group of adenosylcobalamin(B12)-dependent ribonucleotide reductases (RNR) related to the characterized species from Lactococcus leichmannii. RNR's are responsible for the conversion of the ribose sugar of RNA into the deoxyribose sugar of DNA. This is the rate-limiting step of DNA biosynthesis. Thus model identifies NrdJ enzymes only in cyanobacteria, lactococcus and certain bacteriophage. A separate model (TIGR02504) identifies a larger group of divergent B12-dependent RNR's. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
Pssm-ID: 274169 [Multi-domain] Cd Length: 713 Bit Score: 756.76 E-value: 0e+00
Class II ribonucleotide reductase, monomeric form; Ribonucleotide reductase (RNR) catalyzes ...
10-673
2.34e-134
Class II ribonucleotide reductase, monomeric form; Ribonucleotide reductase (RNR) catalyzes the reductive synthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, and bacteriophage, use a diiron-tyrosyl radical. Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs, found in anaerobic bacteria, bacteriophage, and archaea, use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. Many organisms have more than one class of RNR present in their genomes. All three RNRs have a ten-stranded alpha-beta barrel domain that is structurally similar to the domain of PFL (pyruvate formate lyase). Class II RNRs are found in bacteria that can live under both aerobic and anaerobic conditions. Many, but not all members of this class, are found to be homodimers. This particular subfamily is found to be active as a monomer. Adenosylcobalamin interacts directly with an active site cysteine to form the reactive cysteine radical.
Pssm-ID: 153085 [Multi-domain] Cd Length: 658 Bit Score: 409.59 E-value: 2.34e-134
ribonucleoside-diphosphate reductase, adenosylcobalamin-dependent; This model represents a ...
13-636
1.30e-59
ribonucleoside-diphosphate reductase, adenosylcobalamin-dependent; This model represents a group of adenosylcobalamin(B12)-dependent ribonucleotide reductases (Class II RNRs) related to the characterized species from Pyrococcus, Thermoplasma, Corynebacterium, and Deinococcus. RNR's are responsible for the conversion of the ribose sugar of RNA into the deoxyribose sugar of DNA. This is the rate-limiting step of DNA biosynthesis. This model identifies genes in a wide range of deeply branching bacteria. All are structurally related to the class I (non-heme iron dependent) RNRs. In most species this gene is known as NrdJ, while in mycobacteria it is called NrdZ. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]
Pssm-ID: 274168 [Multi-domain] Cd Length: 575 Bit Score: 210.26 E-value: 1.30e-59
Ribonucleotide reductase alpha subunit [Nucleotide transport and metabolism]; Ribonucleotide ...
12-632
3.09e-55
Ribonucleotide reductase alpha subunit [Nucleotide transport and metabolism]; Ribonucleotide reductase alpha subunit is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 439979 [Multi-domain] Cd Length: 665 Bit Score: 200.03 E-value: 3.09e-55
Class II ribonucleotide reductase, dimeric form; Ribonucleotide reductase (RNR) catalyzes the ...
199-507
2.44e-49
Class II ribonucleotide reductase, dimeric form; Ribonucleotide reductase (RNR) catalyzes the reductive synthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, and bacteriophage, use a diiron-tyrosyl radical. Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs, found in anaerobic bacteria, bacteriophage, and archaea, use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. Many organisms have more than one class of RNR present in their genomes. All three RNRs have a ten-stranded alpha-beta barrel domain that is structurally similar to the domain of PFL (pyruvate formate lyase). Class II RNRs are found in bacteria that can live under both aerobic and anaerobic conditions. Many, but not all members of this class are found to be homodimers. Adenosylcobalamin interacts directly with an active site cysteine to form the reactive cysteine radical.
Pssm-ID: 153089 [Multi-domain] Cd Length: 464 Bit Score: 179.35 E-value: 2.44e-49
Ribonucleotide reductase alpha domain; This is the alpha helical domain of ribonucleotide ...
6-78
7.03e-24
Ribonucleotide reductase alpha domain; This is the alpha helical domain of ribonucleotide reductases. Family members include Ribonucleotide reductase (RNR, EC:1.17.4.1), which catalyze the reductive synthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs divide into three classes on the basis of their metallocofactor usage. This domain is found in Class II. Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Many organizms have more than one class of RNR present in their genomes. Ribonucleotide reductase is an oligomeric enzyme composed of a large sub-unit (700 to 1000 residues) and a small sub-unit (300 to 400 residues) - class II RNRs are less complex, using the small molecule B12 in place of the small chain. Some family members carry ATP cone domain which acts as a functional regulator. Competitive binding of ATP and dATP to an N-terminal ATP-cone domain determines enzyme activity. As the ratio of dATP to ATP increases above a certain threshold, the enzyme activity is turned off. Substrate nucleotides are recognized by relatively simple H-bonding interactions at the N-terminus of one or more alpha helices. In the monomeric class II RNR, the effector binds in a pocket formed by helices in a 130 amino acid insertion which constitutes this domain.
Pssm-ID: 465599 [Multi-domain] Cd Length: 101 Bit Score: 96.55 E-value: 7.03e-24
Class I ribonucleotide reductase; Ribonucleotide reductase (RNR) catalyzes the reductive ...
200-514
1.23e-22
Class I ribonucleotide reductase; Ribonucleotide reductase (RNR) catalyzes the reductive synthesis of deoxyribonucleotides from their corresponding ribonucleotides. It provides the precursors necessary for DNA synthesis. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs, found in eukaryotes, bacteria, and many viruses, use a diiron-tyrosyl radical. Class II RNRs, found in bacteria, bacteriophage, algae and archaea, use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs, found in anaerobic bacteria, bacteriophages, and archaea, use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. Many organisms have more than one class of RNR present in their genomes. All three RNRs have a ten-stranded alpha-beta barrel domain that is structurally similar to the domain of PFL (pyruvate formate lyase). Class I RNR is oxygen-dependent and can be subdivided into classes Ia (eukaryotes, prokaryotes, viruses and phages) and Ib (which is found in prokaryotes only). It is a tetrameric enzyme of two alpha and two beta subunits; this model covers the major part of the alpha or large subunit, called R1 in class Ia and R1E in class Ib.
Pssm-ID: 153088 [Multi-domain] Cd Length: 460 Bit Score: 101.47 E-value: 1.23e-22
Ribonucleotide reductase and Pyruvate formate lyase; Ribonucleotide reductase (RNR) and ...
204-569
4.39e-10
Ribonucleotide reductase and Pyruvate formate lyase; Ribonucleotide reductase (RNR) and pyruvate formate lyase (PFL) are believed to have diverged from a common ancestor. They have a structurally similar ten-stranded alpha-beta barrel domain that hosts the active site, and are radical enzymes. RNRs are found in all organisms and provide the only mechanism by which nucleotides are converted to deoxynucleotides. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs use a diiron-tyrosyl radical while Class II RNRs use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. PFL, an essential enzyme in anaerobic bacteria, catalyzes the conversion of pyruvate and CoA to acteylCoA and formate in a mechanism that uses a glycyl radical.
Pssm-ID: 153083 [Multi-domain] Cd Length: 401 Bit Score: 62.17 E-value: 4.39e-10
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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