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PHD

Gene
phd
Protein
Antitoxin phd
Organism
Escherichia phage P1
Length
73 amino acids
Function
Binds to its own promoter repressing its expression; toxin doc acts as a corepressor or derepressor depending on the ratio, repressing or inducing expression.
Similarity
Belongs to the phD/YefM antitoxin family.
Mass
8.133 kDa
Sequence
MQSINFRTARGNLSEVLNNVEAGEEVEITRRGREPAVIVSKATFEAYKKAALDAEFASLFDTLDSTNKELVNR

Gene
phd
Protein
Antitoxin Phd
Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Length
65 amino acids
Function
Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the bacteriostatic effect of cognate toxin Doc. In M.smegmatis 3 TA systems (VapB-VapC, MazE-MazF and Phd-Doc) may be involved in monitoring the nutritional supply and physiological state of the cell, linking catabolic with anabolic reactions.
Mass
7.276 kDa
Sequence
MPSLNIDFDEAEMEQIRAAARADDLSLKKFAHAAVMERASAHKRRVAEAARLVAERSAELNRRLA

Gene
PHD
Protein
Phalloidin proprotein
Organism
Amanita ocreata
Length
31 amino acids
Function
Major toxin that belongs to the bicyclic heptapeptides called phallotoxins (PubMed:18025465). Although structurally related to amatoxins, phallotoxins have a different mode of action, which is the stabilization of F-actin (PubMed:18025465). Phallotoxins are poisonous when administered parenterally, but not orally because of poor absorption (PubMed:18025465).
Similarity
Belongs to the MSDIN fungal toxin family.
Mass
3.302 kDa
Fragment
single
Sequence
MSDINATRLPAWLATCPCAGDDVNPLLTRGE