| Accession | TIGR02826 |
| Name | RNR_activ_nrdG3 |
| Function | anaerobic ribonucleoside-triphosphate reductase activating protein |
| Gene Symbol | nrdG |
| Trusted Cutoff | 151.70 |
| Domain Trusted Cutoff | 151.70 |
| Noise Cutoff | 77.35 |
| Domain Noise Cutoff | 77.35 |
| Isology Type | equivalog |
| EC Number | 1.97.1.4 |
| HMM Length | 148 |
| Mainrole Category | Purines, pyrimidines, nucleosides, and nucleotides |
| Subrole Category | 2'-Deoxyribonucleotide metabolism |
| Gene Ontology Term | GO:0008998: ribonucleoside-triphosphate reductase activity molecular_function |
| | GO:0009265: 2'-deoxyribonucleotide biosynthetic process biological_process |
| | GO:0043364: catalysis of free radical formation molecular_function |
| | GO:0051536: iron-sulfur cluster binding molecular_function |
| Author | Haft DH |
| Entry Date | Feb 17 2006 10:26AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | Members of this family represent a set of proteins related to, yet architecturally different from, the activating protein for the glycine radical-containing, oxygen-sensitive ribonucleoside-triphosphate reductase (RNR) as described in model TIGR02491. Members of this family are found paired with members of a similarly divergent set of anaerobic ribonucleoside-triphosphate reductases. Identification of this protein as an RNR activitating protein is partly from pairing with a candidate RNR. It is further supported by our finding that upstream of these operons are examples of a conserved regulatory element (described Rodionov and Gelfand) that is found in nearly all bacteria and that occurs specifically upstream of operons for all three classes of RNR genes. |
| References | DR TIGRFAMs; TIGR02491; anaerobic ribonucleoside-triphosphate reductase activating protein.
RN [1]
RM 15949864
RT Identification of a bacterial regulatory system for ribonucleotide reductases by phylogenetic profiling.
RA Rodionov DA, Gelfand MS.
RL Trends Genet. 2005 Jul;21(7):385-9. |
| Genome Property | GenProp0291: class III (anaerobic) ribonucleotide reductase (HMM) |
