{PDOC00489}
{PS00566; FIBRILLARIN}
{BEGIN}
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* Fibrillarin signature *
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Fibrillarin [1] is a  component of a nucleolar small nuclear ribonucleoprotein
(SnRNP) particle thought  to  participate in  the first step of the processing
of pre-rRNA.  In  mammals, fibrillarin  is associated with the U3, U8  and U13
small nuclear RNAs [2].

Fibrillarin is  an  extremely well  conserved  protein of about 320 amino acid
residues. Structurally it consists of three different domains:

 - An N-terminal domain of  about 80 amino acids which is very rich in glycine
   and contains a number of dimethylated arginine residues (DMA).
 - A central domain of about 90 residues  which  resembles that of RNA-binding
   proteins and contains an octameric  sequence similar to the RNP-2 consensus
   found in such proteins.
 - A C-terminal alpha-helical domain.

A protein   evolutionary   related   to  fibrillarin has  been  found  [3]  in
archaebacteria. This  protein  (gene flpA) is involved in pre-rRNA processing.
It lacks the Gly/Arg-rich N-terminal domain.

As a signature pattern, we selected a region that start with and encompass the
RNP-2 like octapeptide sequence.

-Consensus pattern: [GST]-[LIVMAPKR]-[IVEAT]-[FY]-[GSAC]-[IVL]-E-[FYV]-[SA]-
                    x(0,1)-[REA]-x(2)-[RQSFT]-[DEK]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2006 / Pattern revised.

[ 1] Aris J.P., Blobel G.
     "cDNA cloning and sequencing of human fibrillarin, a conserved
     nucleolar protein recognized by autoimmune antisera."
     Proc. Natl. Acad. Sci. U.S.A. 88:931-935(1991).
     PubMed=1846968
[ 2] Bandziulis R.J., Swanson M.S., Dreyfuss G.
     "RNA-binding proteins as developmental regulators."
     Genes Dev. 3:431-437(1989).
     PubMed=2470643
[ 3] Agha-Amiri K.
     J. Bacteriol. 176:2124-2127(1994).

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