#=GF ID Moricin
#=GF AC PF06451.15
#=GF DE Moricin
#=GF AU Finn RD;0000-0001-8626-2148
#=GF SE Pfam-B_56760 (release 9.0)
#=GF GA 25.00 25.00;
#=GF TC 25.50 25.40;
#=GF NC 24.90 24.20;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch --cpu 4 -E 1000 -Z 75585367 HMM pfamseq
#=GF TP Domain
#=GF WK Moricin
#=GF RN [1]
#=GF RM 11997013
#=GF RT Solution structure of moricin, an antibacterial peptide,
#=GF RT isolated from the silkworm Bombyx mori.
#=GF RA Hemmi H, Ishibashi J, Hara S, Yamakawa M;
#=GF RL FEBS Lett 2002;518:33-38.
#=GF DR INTERPRO; IPR009456;
#=GF DR SCOP; 1kv4; fa;
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC Moricin is a antibacterial peptide that is highly basic. The
#=GF CC structure of moricin reveals that it is comprised of a long
#=GF CC alpha-helix. The N-terminus of the helix is amphipathic, and
#=GF CC the C-terminus of the helix is predominately hydrophobic. The
#=GF CC amphipathic N-terminal segment of the alpha- helix is mainly
#=GF CC responsible for the increase in permeability of the bacterial
#=GF CC membrane which kills the bacteria [1].
#=GF SQ 16
#=GS A0A6J1N779_BICAN/25-65 AC A0A6J1N779.1
#=GS A0A212EIS3_DANPL/25-65 AC A0A212EIS3.1
#=GS A0A6J2JVS9_BOMMA/25-65 AC A0A6J2JVS9.1
#=GS MOR1_BOMMO/25-65 AC P82818.1
#=GS MOR2_BOMMO/25-65 AC O96059.1
#=GS A0A6J1WFL0_GALME/25-63 AC A0A6J1WFL0.1
#=GS A5JSU9_GALME/25-63 AC A5JSU9.1
#=GS A0A6J1W8A6_GALME/26-66 AC A0A6J1W8A6.1
#=GS A0A6J3C6H0_GALME/25-62 AC A0A6J3C6H0.1
#=GS A0A4C1Y3B6_EUMVA/97-129 AC A0A4C1Y3B6.1
#=GS A0A835LBH7_SPOEX/25-67 AC A0A835LBH7.1
#=GS A0A8J2QH06_9NEOP/26-66 AC A0A8J2QH06.1
#=GS A0A7E5VZQ5_TRINI/29-71 AC A0A7E5VZQ5.1
#=GS A0A6J1W8A1_GALME/25-63 AC A0A6J1W8A1.1
#=GS A0A212EZ82_DANPL/26-66 AC A0A212EZ82.1
#=GS A0A6J1WFK5_GALME/25-64 AC A0A6J1WFK5.1
A0A6J1N779_BICAN/25-65 .p-KIPINAIRKGARAVGKGLRMINYASTAHDIASMFH..KKKRK.......
A0A212EIS3_DANPL/25-65 .a-RIPIGAIRKGAKAVGKGLRAINIAGTVHDIVEVFK..PRKRK.......
A0A6J2JVS9_BOMMA/25-65 .a-KIPIKAIKTVGKAVGKGLRAINIASTANDVFNFLK..PKKRK.......
MOR1_BOMMO/25-65 .a-KIPIKAIKTVGKAVGKGLRAINIASTANDVFNFLK..PKKRK.......
MOR2_BOMMO/25-65 .a-KIPIKAIKTVGKAVGKGLRAINIASTANDVFNFLK..PKKRK.......
A0A6J1WFL0_GALME/25-63 .p-KVPIGAIKKGGKIIKKGLGVIGAAGTAHEVYSHVK..N----rh.....
A5JSU9_GALME/25-63 .p-KVPIGAIKKGGKIIKKGLGVIGAAGTAHEVYSHVK..N----rq.....
A0A6J1W8A6_GALME/26-66 ..GKIPVKAIKKGGQIIGKALRGINIASTAHDIISQFK..PKKKK.......
A0A6J3C6H0_GALME/25-62 .p-KVPIGAIKKGGKIIKKGLGVLGAAGTAHEV-----..-----ynhvrnr
A0A4C1Y3B6_EUMVA/97-129 gs------AIRKGAKVIGKGLKVIGVAGTAHEV-----..-----yqsvrn.
A0A835LBH7_SPOEX/25-67 ..GKIPVKTIKKAGTAIGKGLRAINIASTAHDVYSFFKpkHKK--kh.....
A0A8J2QH06_9NEOP/26-66 ..GKIPINAIRKGAKAVGHGLRALNIASTAHDIVSAFK..HKKRK.......
A0A7E5VZQ5_TRINI/29-71 ..GKIPVKAIQKAGRAVGKGLRAINIASTAHDVYSFFKpkHKK--kh.....
A0A6J1W8A1_GALME/25-63 .p-KVPVGAIKKGGKAIKTGLGVVGAAGTAHEVYSH--..-----irnrh..
A0A212EZ82_DANPL/26-66 ..GKIPINAIRKGAKAVGHGLRALNIASTAHDIVSAFK..HKKRK.......
A0A6J1WFK5_GALME/25-64 .p-KVNVNAIKKGGKAIGKGFKVISAASTAHDVYEHIK..-----nrrh...
#=GC seq_cons .s.KIPIpAIKKGGKAlGKGLRsINlASTAHDVhshhK...+K.........
//
