Moricin
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]. |
The below sequences were used to create Moricin sequence signatures: |
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MoricinH_16, MoricinP_16
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CAMPSQ146
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146737990
KVNVNAIKKGGKAIGKGFKVISAASTAHDVYEHIKNRRH
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MoricinH_16, MoricinP_16
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CAMPSQ147
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A5JSU6
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146737992
GKIPVKAIKKGGQIIGKALRGINIASTAHDIISQFKPKKKKNH
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MoricinH_16, MoricinP_16
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CAMPSQ148
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A5JSU7
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146737994
KVPIGAIKKGGKIIKKGLGVIGAAGTAHEVYSHVKNRH
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MoricinH_16, MoricinP_16
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CAMPSQ149
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A5JSU8
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146737996
KVPIGAIKKGGKIIKKGLGVLGAAGTAHEVYNHVRNRQ
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MoricinH_16, MoricinP_16
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CAMPSQ150
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A5JSU9
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146737998
KVPIGAIKKGGKIIKKGLGVIGAAGTAHEVYSHVKNRQ
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MoricinH_16, MoricinP_16
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CAMPSQ151
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A5JSV0, A5JSV1
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146738000, 146738002
KVPVGAIKKGGKAIKTGLGVVGAAGTAHEVYSHIRNRH
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MoricinH_16, MoricinP_16
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CAMPSQ152
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A5JSV2
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146738004
KGIGSALKKGGKIIKGGLGALGAIGTGQQVYEHVQNRQ
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MoricinH_16, MoricinP_16
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CAMPSQ1027
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Q7YZB4
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159163502
GKIPVKAIKKAGAAIGKGLRAINIASTAHDVYSFFKPKHKKK
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MoricinH_16, MoricinP_16
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CAMPSQ1032
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Q86MA1
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170784960
GKIPVKAIKQAGKVIGKGLRAINIAGTTHDVVSFFRPKKKKH
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MoricinH_16, MoricinP_16
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CAMPSQ1090
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P82818, O96059
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20138941, 1246017
AKIPIKAIKTVGKAVGKGLRAINIASTANDVFNFLKPKKRKH
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MoricinH_16, MoricinP_16
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CAMPSQ1252
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P83416
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25091528
GKIPIGAIKKAGKAIGKGLRAVNIASTAHDVYTFFKPKKRH
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MoricinH_16, MoricinP_16
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CAMPSQ1657
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P82818
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21465926
AKIPIKAIKTVGKAVGKGLRAINIASTANDVFNFLKPKKRKA
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MoricinH_16, MoricinP_16
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CAMPSQ2910
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KVNANAIKKGGKAIGKGFKVISAASTAHDVYEHIKNRRH
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MoricinH_16, MoricinP_16
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CAMPSQ10738
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APKVNVNALKKGGRVIKKGLGVIGAAGTAHEVYNHVRNRNQG
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MoricinH_16, MoricinP_16
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CAMPSQ10739
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APKVNVNALRKGGRVIRKGLGVIGAAGTAHEVYNHVRNRNQG
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MoricinH_16, MoricinP_16
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CAMPSQ10740
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APKVNVNALKKGGHVIKKGLGVIGAAGTAHEVYNHVRNRNQG
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© 2022, Biomedical Informatics Centre, NIRRCH, Mumbai |
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