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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.