| Accession | TIGR00411 |
| Name | redox_disulf_1 |
| Function | redox-active disulfide protein 1 |
| Trusted Cutoff | 92.75 |
| Domain Trusted Cutoff | 92.75 |
| Noise Cutoff | 64.70 |
| Domain Noise Cutoff | 64.70 |
| Isology Type | hypoth_equivalog |
| HMM Length | 82 |
| Mainrole Category | Unknown function |
| Subrole Category | General |
| Author | Haft DH |
| Entry Date | Apr 20 1999 2:09PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This protein is homologous to a family of proteins that includes thioredoxins, glutaredoxins, protein-disulfide isomerases, and others, some of which have several such domains. The sequence of this protein at the redox-active disufide site, CPYC, matches glutaredoxins rather than thioredoxins, although its overall sequence seems closer to thioredoxins. It is suggested to be a ribonucleotide-reducing system component distinct from thioredoxin or glutaredoxin. |
| References | A2 hmmalign
RN [1]
RM 92268099
RT The purification, characterization, and primary structure of a small redox protein from Methanobacterium thermoautotrophicum, an archaebacterium.
RA McFarlan SC, Terrell CA, Hogenkamp HP.
RL J Biol Chem 1992 May 25;267(15):10561-9
RN [2]
RM 20290854
RT A thioredoxin from the hyperthermophilic archaeon Methanococcus jannaschii has a glutaredoxin-like fold but thioredoxin-like activities.
RA Lee DY, Ahn BY, Kim KS
RL Biochemistry. 2000 Jun 6;39(22):6652-9 |
