#=GF ID FSAP_sig_propep
#=GF AC PF03032.19
#=GF DE Frog skin active peptide family signal and propeptide
#=GF PI Brevenin;
#=GF AU Griffiths-Jones SR;0000-0001-6043-807X
#=GF AU Eberhardt R;0000-0001-6152-1369
#=GF AU El-Gebali S;0000-0003-1378-5495
#=GF SE Pfam-B_1232 (release 6.4)
#=GF GA 27.00 27.00;
#=GF TC 43.30 43.30;
#=GF NC 26.00 24.70;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch --cpu 4 -Z 75585367 -E 1000 HMM pfamseq
#=GF TP Family
#=GF WK Amphibian_antimicrobial_peptides
#=GF RN [1]
#=GF RM 9578480
#=GF RT Solution structure of the antimicrobial peptide ranalexin and a
#=GF RT study of its interaction with perdeuterated
#=GF RT dodecylphosphocholine micelles.
#=GF RA Vignal E, Chavanieu A, Roch P, Chiche L, Grassy G, Calas B,
#=GF RA Aumelas A;
#=GF RL Eur J Biochem 1998;253:221-228.
#=GF RN [2]
#=GF RM 8306981
#=GF RT Isolation and structure of novel defensive peptides from frog
#=GF RT skin.
#=GF RA Mor A, Nicolas P;
#=GF RL Eur J Biochem 1994;219:145-154.
#=GF RN [3]
#=GF RM 23988198
#=GF RT Therapeutic potential of the peptide leucine arginine as a new
#=GF RT nonplant bowman-birk-like serine protease inhibitor.
#=GF RA Rothemund S, Sonnichsen FD, Polte T;
#=GF RL J Med Chem. 2013;56:6732-6744.
#=GF RN [4]
#=GF RM 18656510
#=GF RT Solution NMR structures of the antimicrobial peptides
#=GF RT phylloseptin-1, -2, and -3 and biological activity: the role of
#=GF RT charges and hydrogen bonding interactions in stabilizing helix
#=GF RT conformations.
#=GF RA Resende JM, Moraes CM, Prates MV, Cesar A, Almeida FC, Mundim
#=GF RA NC, Valente AP, Bemquerer MP, Pilo-Veloso D, Bechinger B;
#=GF RL Peptides. 2008;29:1633-1644.
#=GF DR INTERPRO; IPR004275;
#=GF DR TC; 1.C.52;
#=GF DR SO; 0100021; polypeptide_conserved_region;
#=GF CC This family contains a number of defence peptides secreted from
#=GF CC the skin of amphibians, including the opiate-like dermorphins
#=GF CC and deltorphins, and the antimicrobial dermoseptins and
#=GF CC temporins. The alignment for this family consists of the signal
#=GF CC peptide and propeptide regions and does not include the active
#=GF CC peptides [1] [2].Family members such as the peptide leucine
#=GF CC arginine (pLR) belongs to a class of cyclic peptides isolated
#=GF CC from frog skin. Its primary sequence is similar to the reactive
#=GF CC loop of plant Bowman-Birk inhibitors (BBI), and the circular
#=GF CC sunflower trypsin inhibitor-1 (SFTI-1) and to HV-BBI, an
#=GF CC isolated peptide from amphibian skin with trypsin-inhibitory
#=GF CC activity. pLR is a highly potent trypsin inhibitor, with
#=GF CC therapeutic potential. A study describing immunomodulatory
#=GF CC properties of pLR showed that the peptide is a potent activator
#=GF CC of histamine release [3]. Other members such as Phylloseptins
#=GF CC are antimicrobial peptides of 19-20 residues and carry an
#=GF CC amidated C-terminus [4].
#=GF SQ 3
#=GS A0A2G9SJI8_LITCT/2-24 AC A0A2G9SJI8.1
#=GS A0A2G9QHX0_LITCT/2-24 AC A0A2G9QHX0.1
#=GS A0A2G9S1W3_LITCT/2-43 AC A0A2G9S1W3.1
A0A2G9SJI8_LITCT/2-24 FTLKKSLLLLFFLGTINLSLCEE-----------------------.....
A0A2G9QHX0_LITCT/2-24 FTLKKSLLLLFFLGTITLSFCEQ-----------------------.....
A0A2G9S1W3_LITCT/2-43 FTMKKSLLLLFFLGTISLSLCEQERNADDDQGEVIEQ---------kvkra
#=GC seq_cons FTLKKSLLLLFFLGTIoLSLCEQ............................
//
