|PROSITE documentation PDOC51459 [for PROSITE entry PS51459]|
The fido domain of Vibrio VopS covalently modifies Rho GTPase threonine with AMP to inhibit downstream signaling events in host cells. The AMPylation activity extends to a eukaryotic fido domain in Drosophila fic homologue CG9523. AMPylation represents a newly discovered posttranslational modification used to stably modify proteins with AMP. This signaling mechanism is predicted to be functionally similar to other posttranslation modifications such as phosphorylation, SUMOylation or acetylation, because the added moiety changes the activity of the modified protein. The covalent attachment of AMP by a phosphodiester bond is predicted to be reversible and is bulky enough to provide a docking site for a putative AMP binding domain .
The fido domain contains a central motif conserved in most sequences (H-x-F-x-[DE]-[AG]-N-[GK]-R), with the motif His contributing to fic AMPylation. The fido domain adopts an α-helical fold, arranged as a six-helix up and down bundle (see <PDB:2F6S>) [2,3,4].
The profile we developed covers the entire fido domain.Last update:
July 2009 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Anantharaman V. Aravind L.|
|Title||New connections in the prokaryotic toxin-antitoxin network: relationship with the eukaryotic nonsense-mediated RNA decay system.|
|Source||Genome Biol. 4:R81-R81(2003).|
|2||Authors||Garcia-Pino A. Christensen-Dalsgaard M. Wyns L. Yarmolinsky M. Magnuson R.D. Gerdes K. Loris R.|
|Title||Doc of prophage P1 is inhibited by its antitoxin partner Phd through fold complementation.|
|Source||J. Biol. Chem. 283:30821-30827(2008).|
|3||Authors||Das D. Krishna S.S. McMullan D. Miller M.D. Xu Q. Abdubek P. Acosta C. Astakhova T. Axelrod H.L. Burra P. Carlton D. Chiu H.-J. Clayton T. Deller M.C. Duan L. Elias Y. Elsliger M.-A. Ernst D. Feuerhelm J. Grzechnik A. Grzechnik S.K. Hale J. Han G.W. Jaroszewski L. Jin K.K. Klock H.E. Knuth M.W. Kozbial P. Kumar A. Marciano D. Morse A.T. Murphy K.D. Nigoghossian E. Okach L. Oommachen S. Paulsen J. Reyes R. Rife C.L. Sefcovic N. Tien H. Trame C.B. Trout C.V. van den Bedem H. Weekes D. White A. Hodgson K.O. Wooley J. Deacon A.M. Godzik A. Lesley S.A. Wilson I.A.|
|Title||Crystal structure of the Fic (Filamentation induced by cAMP) family protein SO4266 (gi|24375750) from Shewanella oneidensis MR-1 at 1.6 A resolution.|
|4||Authors||Kinch L.N. Yarbrough M.L. Orth K. Grishin N.V.|
|Title||Fido, a novel AMPylation domain common to fic, doc, and AvrB.|
|Source||PLoS ONE 4:E5818-E5818(2009).|