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thioredoxin fold domain-containing protein
LPXTG cell wall anchor motif
thioredoxin domain-containing protein
Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise. (from Pfam)
glutathione S-transferase; glutathione S-transferase family protein
glutathione S-transferase (GST) catalyzes the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress; similar to class-delta/epsilon GSTs which play major roles in insecticide resistance| glutathione S-transferase (GST) family protein similar to human failed axon connections homolog, which may play a role in axonal development
LPXTG cell wall anchor domain-containing protein
This model describes the LPXTG motif-containing region found at the C-terminus of many surface proteins of Streptococcus and Streptomyces species. Cleavage between the Thr and Gly by sortase or a related enzyme leads to covalent anchoring at the new C-terminal Thr to the cell wall. Hits that do not lie at the C-terminus or are not found in Gram-positive bacteria are probably false-positive. A common feature of this proteins containing this domain appears to be a high proportion of charged and zwitterionic residues immediatedly upstream of the LPXTG motif. This model differs from other descriptions of the LPXTG region by including a portion of that upstream charged region.
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