|Function||anaerobic ribonucleoside-triphosphate reductase activating protein|
|Domain Trusted Cutoff||151.70|
|Domain Noise Cutoff||77.35|
|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|
|Entry Date||Feb 17 2006 10:26AM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||Members of this family represent a set of radical SAM enzymes 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.
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)|
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