v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | NfeD-like proteins are widely distributed throughout prokaryotes and are frequently associated with genes encoding stomatin-like proteins (slipins) [ ]. The homologue from hyperthermophilic archaebacterium Pyrococcus horikoshii is thought to be a serine protease involved in ion channel opening through the cleavage of a stomatin-homologue [].There appear to be three major groups of NfeD-like proteins: an ancestral group with only an N-terminal serine protease domain and this C-terminal beta sheet-rich domain which is structurally very similar to the OB-fold domain [ ], associated with its neighbouring slipin cluster; a second major group with an additional middle, membrane-spanning domain, associated in some species with eoslipin and in others with yqfA; a final 'artificial' group which unites truncated forms lacking the protease region and associated with their ancestral gene partner, either yqfA or eoslipin.This NefD, C-terminal domain appears to be the major one for relating to the associated protein. NfeD homologues are clearly reliant on their conserved gene neighbour which is assumed to be necessary for function, either through direct physical interaction or by functioning in the same pathway, possibly involve with lipid-rafts [ ]. |
| Short Name | NfeD-like_C |