TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.C.16.1.1









Magainin precursor of 333 aas and 1 TMS.  3-d structural determinations and simulations show the oligomeric states, transmembrane helices and tilt angles in the various states of the mature Maganin (Pino-Angeles et al. 2016).  Forms stable heterooligomers with PglA (TC# 1.C.16.1.5) at lower concentrations of the two peptides than allows each one alone to form pores in which PglA, rather than magainin 2 forms the pore (Strandberg et al. 2016).

Eukaryota
Metazoa
Magainin precursor of Xenopus laevis
*1.C.16.1.2









Preprocaerulein
Eukaryota
Metazoa
Preprocaerulein type I of Xenopus laevis
*1.C.16.1.3









Xenopsin precursor
Eukaryota
Metazoa
Xenopsin precursor of Xenopus laevis
*1.C.16.1.4









Prolevitide precursor
Eukaryota
Metazoa
Prolevitide precursor of Xenopus laevis
*1.C.16.1.5









PylA/PglA (peptide glycine-leucine-amide) precursor of 64 aas and 1 TMS.  3-d structures and simulations have revealed the overall structure, helix orientations, and tilt angles in the homo- and hetero-multimeric pores (Pino-Angeles et al. 2016).  The pore forms stable heterooligomers with magainin 2 (TC# 1.C.16.1.1) in which PglA, rather than magainin 2, forms the pore (Strandberg et al. 2016).  This occurs at lower concentrations of the two peptides than is required for each peptide to form homomeric pores.  Ulmschneider 2017 suggested that cationic antimicrobial peptides (AMPs) such as PGLa translocate across hydrophobic lipid bilayers without formation of peptide-lined channels, explaining why they induce membrane leakage and antimicrobial activity. PGLa spontaneously translocates across the membrane individually on a timescale of tens of microseconds, without forming pores. Instead, short-lived water bridges, with two or three peptides connecting at their termini, may allow both ion translocation and lipid flip-flop via a brushlike mechanism usually involving the C terminus of one peptide (Ulmschneider 2017).

Eukaryota
Metazoa
PylA/PglA precursor of Xenopus laevis
*1.C.16.1.6









Toxic magainin peptide, Magainin-R-2 of 23 aas. Magainins are membrane lytic agents.  From the parent protein (1.C.16.1.1), many antimicrobial peptides that inhibit the growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa can be derived (Tanphaichitr et al. 2016).

Eukaryota
Metazoa
Magainin-R-2 of Xenopus laevis (African clawed frog)
*1.C.16.2.1









Hypothetical Protein (99aas)
Eukaryota
Apicomplexa
Hypothetical protein of Toxoplasma gondii (B6K9W1)
*1.C.16.2.2









Uncharacterized protein of 99 aas and 1 TMS.

Eukaryota
Apicomplexa
UP of Hammondia hammondi
*1.C.16.2.3









Uncharacterized protein of 93 aas and 1 TMS.

Eukaryota
Apicomplexa
UP of Neospora caninum