A member of the immunoglobulin superfamily in bacteriophage T4.
We report a prediction that the highly immunogenic outer capsid (Hoc) protein of the prokaryotic phage T4 contains three tandem immunoglobulin-like domains. Immunoglobulin-like folds have previously been identified in prokaryotic proteins but these share no recognizable sequence similarity with eukaryotic immunoglobulin superfamily (IgSF) folds, and may represent products of convergent evolution. In contrast, the Hoc immunoglobulin-like folds are proposed, based on immunoglobulin-like sequence consensus matches detected by hidden Markov modeling. We propose that the Hoc immunoglobulin-like domains and eukaryotic immunoglobulin-like domains are likely to be related by divergence from a common ancestor.
Bateman
A
A
MRC Laboratory of Molecular Biology, Cambridge, England.
Eddy
S R
SR
Mesyanzhinov
V V
VV
D000595:Amino Acid Sequence; D017122:Bacteriophage T4 / Q000235:genetics* / Q000276:immunology*; D002213:Capsid / Q000737:chemistry / Q000235:genetics* / Q000276:immunology*; D019143:Evolution, Molecular; D007136:Immunoglobulins / Q000737:chemistry / Q000235:genetics*; D008390:Markov Chains; D008969:Molecular Sequence Data; D017510:Protein Folding; D012091:Repetitive Sequences, Nucleic Acid; D017386:Sequence Homology, Amino Acid
D007136:Immunoglobulins