HMM Summary Page: TIGR00411

Functionredox-active disulfide protein 1
Trusted Cutoff92.75
Domain Trusted Cutoff92.75
Noise Cutoff64.70
Domain Noise Cutoff64.70
Isology Typehypoth_equivalog
HMM Length82
Mainrole CategoryUnknown function
Subrole CategoryGeneral
AuthorHaft DH
Entry DateApr 20 1999 2:09PM
Last ModifiedFeb 14 2011 3:27PM
CommentThis 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.
ReferencesA2 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