Moricin is a antibacterial peptide that is highly basic. The structure of moricin reveals that it is comprised of a long alpha-helix. The N terminus of the helix is amphipathic, and the C terminus of the helix is predominately hydrophobic. The amphipathic N-terminal segment of the alpha- helix is mainly responsible for the increase in permeability of the bacterial membrane which kills the bacteria [PMID: 11997013].
Sequences retrieved from pattern (1)
CAMPMorP K-x-[GNP]-[AGIV]-x-[AI]-I-K-x(1,2)-G-x(1,3)-G-x-[AGILV]-x(2)-[AGIV]-[GI]-[NST]-[AGI]-x-[EGQS]-[TV]-x(2)-[DH]-[IV]-x-[ENS]  
  UniProt Name
  A5JSU6 Moricin-like peptide B
  A5JSU7 Moricin-like peptide C1
  A5JSU8 Moricin-like peptide C2
  A5JSU9 Moricin-like peptide C3
  A5JSV0, A5JSV1 Moricin-like peptide C4, Moricin-like peptide C5
Sequences retrieved from HMM ( 1 )
  GI UniProt Name
  146737992 A5JSU6 Moricin-like peptide B
  146737994 A5JSU7 Moricin-like peptide C1
  146737996 A5JSU8 Moricin-like peptide C2
  146737998 A5JSU9 Moricin-like peptide C3
  146738000, 146738002 A5JSV0, A5JSV1 Moricin-like peptide C4, Moricin-like peptide C5

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