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| PROSITE documentation PDOC00489 [for PROSITE entry PS00566] |
Fibrillarin signature
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 α-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.
Last update:April 2006 / Pattern revised.
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Aris J.P. Blobel G. |
| Title | cDNA cloning and sequencing of human fibrillarin, a conserved nucleolar protein recognized by autoimmune antisera. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 88:931-935(1991). | |
| PubMed ID | 1846968 |
| 2 | Authors | Bandziulis R.J. Swanson M.S. Dreyfuss G. |
| Title | RNA-binding proteins as developmental regulators. | |
| Source | Genes Dev. 3:431-437(1989). | |
| PubMed ID | 2470643 |
| 3 | Authors | Agha-Amiri K. |
| Source | J. Bacteriol. 176:2124-2127(1994). |
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