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Review
. 2007 Jun;6(6):889-98.
doi: 10.1128/EC.00099-07. Epub 2007 Apr 27.

Protein arginine methyltransferases: from unicellular eukaryotes to humans

François Bachand  1
Affiliations
Review

Protein arginine methyltransferases: from unicellular eukaryotes to humans

François Bachand. Eukaryot Cell. 2007 Jun.
No abstract available

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Figures

FIG. 1.
FIG. 1.
Methylated arginine derivatives and PRMTs. (A) The structure of methylated arginine derivatives. (B) Schematic representation of the nine mammalian PRMTs, all containing a conserved methyltransferase (MTase) domain. SH3, Src-homology 3; Zn, zinc finger; Myr, myristoylation; and F-box motifs of specific PRMTs are shown.
FIG. 2.
FIG. 2.
Amino acid sequence alignment of the amino-terminal domains of PRMT3 from multiple species. Identical amino acids are shown in black, and similar amino acids are shown in gray. The predicted zinc finger domain, the conserved region 1 (CR1) and CR2, and the PRMT-specific motif I are boxed. Asterisks are present under the canonical cysteine and histidine residues of the zinc finger motif. Sequence are from Neurospora crassa (Nc), Aspergillus nidulans (An), Homo sapiens (Hs), Drosophila melanogaster (Dm), Schizosaccharomyces pombe (Sp), Cryptococcus neoformans (Cn), and Toxoplasma gondii (Tg). Alignment and shading were generated using ClustalW and Boxshade software.
See this image and copyright information in PMC

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