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Figure 1 | BMC Bioinformatics

Figure 1

From: Reconstituting protein interaction networks using parameter-dependent domain-domain interactions

Figure 1

Evaluation of different protein-domain annotation merging strategies. (A) Using the InterPro database, we obtained seven protein-domain annotations for yeast protein YNL271C from three databases: PFAM [32], Superfamily (SF) [33], and SMART [34, 35]. PFAM domains: FH2, Drf_FH3, and two Drf_GBD domains; SF domains: Formin homology 2 domain (FH2 domain) and ARM repeat; and SMART domain: Formin Homology. (B) The naïve domain-merging strategy identified seven unique domains for YNL271C. (C) Sequence locations helped identify some of the identical domains (FH2, FH2 domain, and Formin Homology) but was not able to differentiate between different domains that share the same sequence position. (D) Taking into consideration both sequence location and domain names/labels, our merging strategy identified four unique domains: ARM repeat, Drf_FH3, Drf_GBD, and a domain consisting of FH2 domains (FH2, FH2 domain, and Formin Homology).

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