Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00489Fibrillarin signature
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00489
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.
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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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