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Table 3 Potential domain interactions between Ran homologs and Ran-binding proteins

From: Inferring protein domain interactions from databases of interacting proteins

Ran homolog domain Ran-binding protein domain   
Pfam ID Pfam accession Pfam ID Pfam accession θ E
Pfam-B_1470 PB001470 Ran_BP1 PF00638 0.31 3.6
Pfam-B_1470 PB001470 Pfam-B_102314 PB102314 0.42 0.46
Pfam-B_1470 PB001470 Pfam-B_5293 PB005293 0.14 0.19
Pfam-B_1470 PB001470 Pfam-B_93946 PB093946 0.55 0.19
Pfam-B_1470 PB001470 Pfam-B_87101 PB087101 0.20 0.19
Pfam-B_1470 PB001470 Pfam-B_73892 PB073892 0.35 0.075
Ras PF00071 Pfam-B_102314 PB102314 0.039 0.018
Ras PF00071 Pfam-B_93946 PB093946 0.092 0.014
Ras PF00071 Ran_BP1 PF00638 0.008 0.011
Ras PF00071 Pfam-B_87101 PB087101 0.013 0.009
Ras PF00071 Pfam-B_5293 PB005293 0.008 0.008
Pfam-B_1470 PB001470 zf-RanBP PF00641 0.053 0.008
Ras PF00071 Pfam-B_73892 PB073892 0.029 0.004
Ras PF00071 zf-RanBP PF00641 0.004 0.000
  1. Several domain interactions are possible in the interactions of yeast and worm Ran signal-transducing proteins with some Ran-binding proteins. Of these possible domain interactions, DPEA predicts the interaction (E = 3.6) of a Pfam-B domain [Pfam:PB001470] found at the C-termini of Ran homologs but not in other Ras family members [Pfam:PF00071] with Ran-binding domains [Pfam:PF00638, Ran_BP1]. Structural [43] and biochemical [44] studies confirm this interaction. We conclude that DPEA identified, from among several possibilities, an important domain interaction for the interaction of Ran homologs with a subset of Ran-binding proteins.