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PDOC00489
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1995-07-26
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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 such as Methanococcus vannielii or voltae. This protein (gene
rrpA) is involved in pre-rRNA processing. It lacks the Gly/Arg-rich N-terminal
domain.
As a signature pattern, we selected the RNP-2 like octapeptide sequence.
-Consensus pattern: [GST]-[LIVMP]-V-Y-A-V-E-F
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in SWISS-PROT: NONE.
-Last update: June 1994 / Pattern and text revised.
[ 1] Aris J.P., Blobel G.
Proc. Natl. Acad. Sci. U.S.A. 88:931-935(1991).
[ 2] Bandziulis R.J., Swanson M.S., Dreyfuss G.
Genes Dev. 3:431-437(1989).
[ 3] Agha Amiri K.
EMBL/GenBank: X73987.