{PDOC51385}
{PS51385; YJEF_N}
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* YjeF N-terminal domain profile *
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The YjeF  N-terminal  domains  occur either as single proteins or fusions with
other domains  and  are  commonly  associated  with  enzymes.  In bacteria and
archaea, YjeF  N-terminal  domains are often fused to a YjeF C-terminal domain
with high  structural homology to the members of a ribokinase-like superfamily
(see <PDOC00806>)  and/or  belong  to  operons  that encode enzymes of diverse
functions: pyridoxal  phosphate  biosynthetic  protein  PdxJ; phosphopanteine-
protein transferase;   ATP/GTP   hydrolase;   and  pyruvate-formate  lyase  1-
activating enzyme.  In  plants,  the  YjeF  N-terminal domain is fused to a C-
terminal putative  pyridoxamine  5'-phosphate oxidase. In eukaryotes, proteins
that consist  of  (Sm)-FDF-YjeF  N-terminal  domains  may  be  involved in RNA
processing [1,2].

The YjeF  N-terminal  domains  represent a novel version of the Rossmann fold,
one of  the  most  common  protein folds in nature observed in numerous enzyme
families, that  has  acquired  a  set  of  catalytic  residues  and structural
features that  distinguish them from the conventional dehydrogenases. The YjeF
N-terminal domain is comprised of a three-layer alpha-beta-alpha sandwich with
a central  beta-sheet surrounded by helices (see <PDB:2O8N>). The conservation
of the  acidic  residues  in  the predicted active site of the YjeF N-terminal
domains is reminiscent of the presence of such residues in the active sites of
diverse hydrolases [1,2].

Some proteins known to contain a YjeF N-terminal domain are listed below:

 - Escherichia coli hypothetical protein YjeF.
 - Thermotoga maritima hypothetical protein Tm0922.
 - Yeast uncharacterized protein YNL200C.
 - Yeast enhancer of mRNA-decapping protein 3 (EDC3).
 - Vertebrate enhancer of mRNA-decapping protein 3 (EDC3).
 - Mammalian  apolipoprotein  A-I  binding  protein  (AI-BP),  a  protein that
   interacts with  apolipoprotein  A-I,  a  major  constituent of high-density
   lipoprotein (HDL).

The profile we developed covers the entire YjeF N-terminal domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: June 2008 / First entry.

[ 1] Anantharaman V., Aravind L.
     "Novel conserved domains in proteins with predicted roles in
     eukaryotic cell-cycle regulation, decapping and RNA stability."
     BMC Genomics 5:45-45(2004).
     PubMed=15257761; DOI=10.1186/1471-2164-5-45
[ 2] Jha K.N., Shumilin I.A., Digilio L.C., Chertihin O., Zheng H.,
     Schmitz G., Visconti P.E., Flickinger C.J., Minor W., Herr J.C.
     "Biochemical and structural characterization of apolipoprotein A-I
     binding protein, a novel phosphoprotein with a potential role in sperm
     capacitation."
     Endocrinology 149:2108-2120(2008).
     PubMed=18202122; DOI=10.1210/en.2007-0582

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