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We thus postulate that APIP12 could represent a unique protein sharing sequence and structure similarity to Nup98 family.
In addition to Frizzled receptors, four sFRP (Soluble Frizzled Related Protein), sharing homology in the CRD domain but lacking the putative trans-membrane domain have been identified [6].
Similar results were previously obtained with HIV-1 gp120, a protein sharing with Aβ peptides a common sphingolipid-binding domain (SBD) involved in GalCer recognition [10].
In recent years, doppel protein (Dpl), a PrPC paralog, has been identified as a protein sharing common biochemical and structural properties with the latter [3], [4], [5].
It also harbors one specific CDS encoding hypothetical protein sharing highest homologies with ykris0001_25080, a hypothetical protein from Yersinia kristensenii ATCC 33638.
We also can hypothesize that Vpr77 92 sequence from entire or C-terminal processed protein sharing the penetrating properties of 89.6- Vpr77 92 sequence, should penetrate and provoke apoptosis in both infected or non infected cells.
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This protein shares highest amino acid identity (83%) with a putative dihydropyrimidinase of Mesorhizobium sp. BNC1 (YP_675206).
This protein shared high identity with RhuM, a protein from S. enterica.
RhuM (NP_462654) and the predicted phage protein shared 42.3% identity and 58.3% similarity.
We also suggest a common opening mechanism for proteins sharing the same fold as TSP-1.
The other subfamily comprises proteins sharing only the BH3 domain.
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