| Literature References | 1. JANSEN, R.P., HURT, E.C., KERN, H., LEHTONEN, H., CARMO-FONSECA, M.
LAPEYRE, B. AND TOLLERVEY, D.
Evolutionary conservation of the human nucleolar protein fibrillarin and
its functional expression in yeast.
J.CELL BIOL. 113 715-729 (1991).
2. GIRARD, J.P., FELIU, J., CAIZERGUES-FERRER, M. AND LAPEYRE, B.
Study of multiple fibrillarinn mRNAs reveals that 3' end formation in
Scizosaccharomyces pombe is sensitive to cold shock.
NUCLEIC ACIDS RES. 21 1881-1887 (1993).
3. SCHIMMANG, T., TOLLERVEY, D., KERN, H., FRANK, R. AND HURT, E.C.
A yeast nucleolar protein related to mammalian fibrillarin is associated
with small nucleolar RNA and is essential for viability.
EMBO J. 8 4015-4024 (1989).
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| Documentation | Fibrillarin is a component of a nucleolar small nuclear ribonucleoprotein
(SnRNP), functioning in vivo in ribosomal RNA processing [1,2]: it is
associated with U3, U8 and U13 small nuclear RNAs in mammals [1] and is
similar to the yeast NOP1 protein [3]. Fibrillarin has a well-conserved
sequence of around 320 amino acids, and contains 3 domains: an N-terminal
Gly/Arg-rich region; a central domain resembling other RNA-binding
proteins and containing an RNP-2-like consensus sequence; and a C-terminal
alpha-helical domain. An evolutionarily related pre-rRNA processing
protein, which lacks the Gly/Arg-rich domain, has been found in various
archaebacteria.
FIBRILLARIN is a 7-element fingerprint that provides a signature for
fibrillarins and fibrillarin-like proteins. The fingerprint was derived
from an initial alignment of 6 sequences: motifs 1-6 were drawn from the
central domain and motif 7 from the C-terminal alpha-helical region -
motif 4 includes the RNP-2-like consensus sequence encoded by PROSITE
pattern FIBRILLARIN (PS00566). Two iterations on OWL25.1 were required to
reach convergence, at which point a true set comprising 10 sequences was
identified.
An update on SPTR37_9f identified a true set of 14 sequences, and 1
partial match.
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