AMPDB_4080 | Dermaseptin-DI1

1 General Description

AMPDB ID: AMPDB_4080

Protein Names: Dermaseptin-DI1 (DRS-DI1) (Dermadistinctin-K) (DD-K)

Protein Family: Frog skin active peptide (FSAP) family; Dermaseptin subfamily

Gene Name: Nil

Source Organism: Phyllomedusa distincta (Monkey frog)

Protein Length: 33 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

GLWSKIKAAGKEAAKAAAKAAGKAALNAVSEAV

FASTA format

Counts of Amino Acids

'A': 13, 'R': 0, 'N': 1, 'D': 0, 'C': 0, 'Q': 0, 'E': 2, 'G': 3, 'H': 0, 'I': 1, 'L': 2, 'K': 6, 'M': 0, 'F': 0, 'P': 0, 'S': 2, 'T': 0, 'W': 1, 'Y': 0, 'V': 2

Frequencies of Amino Acids

'A': 39.39%, 'R': 0%, 'N': 3.03%, 'D': 0%, 'C': 0%, 'Q': 0%, 'E': 6.06%, 'G': 9.09%, 'H': 0%, 'I': 3.03%, 'L': 6.06%, 'K': 18.18%, 'M': 0%, 'F': 0%, 'P': 0%, 'S': 6.06%, 'T': 0%, 'W': 3.03%, 'Y': 0%, 'V': 6.06%

Missing Amino Acid(s)

C, D, F, H, M, P, Q, R, T, Y

Most Occurring Amino Acid(s)

Less Occurring Amino Acid(s)

I, N, W

Hydrophobic Amino Acid(s) Count

Hydrophilic Amino Acid(s) Count

Basic Amino Acid(s) Count

Acidic Amino Acid(s) Count

Modified Amino Acid(s) Count

Modified Amino Acid(s) Frequencies

Computed by biopython (version 1.79) & proteinAnalysis (version 1)

3 Physicochemical Properties

Sl. No.	Properties	Values	Reference
1.	Molecular Mass	3152.69 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	92.424	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	12.418	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	0.191	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.562	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	10.802	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	4	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.182, 0.182, 0.515 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.03	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	5500, 5500	Computed by ProtParam module (biopython 1.79)

4.1 Target Organism(s)

C.albicans, C.guilliermondii, C.tropicalis (Gram-negative), E.faecalis (Gram-positive), P.aeruginosa (Gram-negative), S.aureus (Gram-positive)

4.2 Antimicrobial Activity

Amphibian defense peptide, Antibiotic, Antimicrobial, Anti-candida, Anti-protozoal, Anti-gram-negative, Anti-gram-Positive

4.3 Enzymatic Activity

4.4 Inhibitory Effect

4.5 Other Biological Activity

Non-hemolytic, Non-ribosomal

Activity data manually curated from Literature and UniProt

5 Database Cross-references

5.1 Literature Database

Citation 1: Batista CV, da Silva LR, Sebben A, et al. Antimicrobial peptides from the Brazilian frog Phyllomedusa distincta. Peptides. 1999;20(6):679-86. Published 1999. doi:10.1016/s0196-9781(99)00050-9

PMID: 10477123

Citation 2: Brand GD, Leite JR, Silva LP, et al. Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta. Anti-Trypanosoma cruzi activity without cytotoxicity to mammalian cells. J Biol Chem. 2002;277(51):49332-40. Published 2002 Dec 20. doi:10.1074/jbc.M209289200

PMID: 12379643

Citation 3: Silva LP, Leite JRSA, Brand GD, et al. Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: liposomes fusion and/or lysis investigated by fluorescence and atomic force microscopy. Comp Biochem Physiol A Mol Integr Physiol. 2008;151(3):329-335. Published 2008 Nov. doi:10.1016/j.cbpa.2007.02.031

PMID: 17409003

Citation 4: Leite JRSA, Brand GD, Silva LP, et al. Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: Secondary structure, antimicrobial activity, and mammalian cell toxicity. Comp Biochem Physiol A Mol Integr Physiol. 2008;151(3):336-343. Published 2008 Nov. doi:10.1016/j.cbpa.2007.03.016

PMID: 17442605

Citation 5: Amiche M, Ladram A, Nicolas P, et al. A consistent nomenclature of antimicrobial peptides isolated from frogs of the subfamily Phyllomedusinae. Peptides. 2008;29(11):2074-82. Published 2008 Nov. doi:10.1016/j.peptides.2008.06.017

PMID: 18644413

Citation 6: Verly RM, de Moraes CM, Resende JM, et al. Structure and membrane interactions of the antibiotic peptide dermadistinctin K by multidimensional solution and oriented 15N and 31P solid-state NMR spectroscopy. Biophys J. 2009;96(6):2194-203. Published 2009 Mar 18. doi:10.1016/j.bpj.2008.11.063

PMID: 19289046

5.2 Protein Sequence Databases

5.3 3D Structure Databases

	Sl. no.	PDB ID	Method	Resolution	Access Links	3D View

AlphaFoldDB: P83638

5.4 Nucleotide Sequence Databases

No entries found in GenBank or EMBL

RefSeq: Not found

5.5 Protein-Protein Interaction Databases

STRING: Not found

IntAct: Not found

BioGRID: Not found

5.6 Ligand Databases

BindingDB: Not found

DrugBank: Not found

ChEMBL: Not found

5.7 Family & Domain Databases

InterPro: IPR022731

PANTHER: Not found

PROSITE: Not found

5.8 Genome Annotation Databases

Ensembl: Not found

5.9 Phylogenomic Databases

GeneTree: Not found

5.10 Enzyme & Pathway Databases

BRENDA: Not found

BioCyc: Not found

5.11 Protein-RNA Interaction Databases

RNAct: Not found

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