AMPDB_838 | Parabutoporin
PEPTIDE SUMMARY
Parabutoporin
1 General Description
AMPDB ID: AMPDB_838
Protein Names: Parabutoporin (PP) (Non-disulfide-bridged peptide 2.5) (NDBP-2.5) (Non-disulfide-bridged peptide 3.2) (NDBP-3.2)
Protein Family: Non-disulfide-bridged peptide (NDBP) superfamily; Long chain multifunctional peptide (group 2) family
Gene Name: Nil
Protein Length: 45 AA
Protein Existence: Evidence at protein level
2 Protein Sequence & Composition
2.1 Sequence
FKLGSFLKKAWKSKLAKKLRAKGKEMLKDYAKGLLEGGSEEVPGQ
FASTA format
2.2 Composition
Counts of Amino Acids
'A': 4, 'R': 1, 'N': 0, 'D': 1, 'C': 0, 'Q': 1, 'E': 4, 'G': 6, 'H': 0, 'I': 0, 'L': 7, 'K': 11, 'M': 1, 'F': 2, 'P': 1, 'S': 3, 'T': 0, 'W': 1, 'Y': 1, 'V': 1
Frequencies of Amino Acids
'A': 8.89%, 'R': 2.22%, 'N': 0%, 'D': 2.22%, 'C': 0%, 'Q': 2.22%, 'E': 8.89%, 'G': 13.33%, 'H': 0%, 'I': 0%, 'L': 15.56%, 'K': 24.44%, 'M': 2.22%, 'F': 4.44%, 'P': 2.22%, 'S': 6.67%, 'T': 0%, 'W': 2.22%, 'Y': 2.22%, 'V': 2.22%
Missing Amino Acid(s)
C, H, I, N, T
Most Occurring Amino Acid(s)
K
Less Occurring Amino Acid(s)
D, M, P, Q, R, V, W, Y
Hydrophobic Amino Acid(s) Count
23
Hydrophilic Amino Acid(s) Count
22
Basic Amino Acid(s) Count
5
Acidic Amino Acid(s) Count
12
Modified Amino Acid(s) Count
0
Modified Amino Acid(s) Frequencies
0
Computed by biopython (version 1.79) & proteinAnalysis (version 1)
3 Physicochemical Properties
Sl. No. Properties Values Reference
1. Molecular Mass 4994.96 Da Computed by ProtParam module (biopython 1.79)
2. Aliphatic Index 76 Computed by ProtParam module (biopython 1.79)
3. Instability Index (Half Life) 19.433 Computed by ProtParam module (biopython 1.79)
4. Hydrophobicity (GRAVY) -0.7 Computed by ProtParam module (biopython 1.79)
5. Hydrophobic Moment 0.673 Computed by ProtParam module (biopython 1.79)
6. Isoelectric Point 10.748 Computed by ProtParam module (biopython 1.79)
7. Charge (at pH 7) 7.001 Computed by ProtParam module (biopython 1.79)
8. Secondary Structure Fraction 0.267, 0.222, 0.356 [Helix, Turn, Sheet] Computed by ProtParam module (biopython 1.79)
9. Aromaticity 0.089 Computed by ProtParam module (biopython 1.79)
10. Molar Extinction Coefficient (cysteine|cystine) 6990, 6990 Computed by ProtParam module (biopython 1.79)
4 Activity Details
4.1 Target Organism(s)
Gram Negative Bacteria and Gram Positive Bacteria
4.2 Antimicrobial Activity
Antibiotic, Antimicrobial, Fungicide, Anti-gram-negative, Anti-gram-Positive
4.3 Enzymatic Activity
Not found
4.4 Inhibitory Effect
Not found
4.5 Other Biological Activity
Cytolysis, Toxin, Hemolytic, Synergistic peptide, Non-ribosomal
Activity data manually curated from Literature and UniProt
5 Database Cross-references
5.1 Literature Database
5.1.1 PubMed
Citation 1: Moerman L, Bosteels S, Noppe W, et al. Antibacterial and antifungal properties of alpha-helical, cationic peptides in the venom of scorpions from southern Africa. Eur J Biochem. 2002;269(19):4799-810. Published 2002 Oct. doi:10.1046/j.1432-1033.2002.03177.x
PMID: 12354111
Citation 2: Willems J, Noppe W, Moerman L, et al. Cationic peptides from scorpion venom can stimulate and inhibit polymorphonuclear granulocytes. Toxicon. 2002;40(12):1679-83. Published 2002 Dec. doi:10.1016/s0041-0101(02)00183-6
PMID: 12457879
Citation 3: Moerman L, Verdonck F, Willems J, et al. Antimicrobial peptides from scorpion venom induce Ca(2+) signaling in HL-60 cells. Biochem Biophys Res Commun. 2003;311(1):90-7. Published 2003 Nov 7. doi:10.1016/j.bbrc.2003.09.175
PMID: 14575699
Citation 4: Willems J, Moerman L, Bosteels S, et al. Parabutoporin--an antibiotic peptide from scorpion venom--can both induce activation and inhibition of granulocyte cell functions. Peptides. 2004;25(7):1079-84. Published 2004 Jul. doi:10.1016/j.peptides.2004.04.008
PMID: 15245865
Citation 5: Zeng XC, Corzo G, Hahin R, et al. Scorpion venom peptides without disulfide bridges. IUBMB Life. 2005;57(1):13-21. Published 2005 Jan. doi:10.1080/15216540500058899
PMID: 16036557
Citation 6: Almaaytah A, Albalas Q, Albalas Q. Scorpion venom peptides with no disulfide bridges: a review. Peptides. 2014;51:35-45. Published 2014 Jan. doi:10.1016/j.peptides.2013.10.021
PMID: 24184590
5.2 Protein Sequence Databases
UniProt: P83312
5.3 3D Structure Databases
No PDB Ids found
AlphaFoldDB: P83312
5.4 Nucleotide Sequence Databases
No entries found in GenBank or EMBL
CCDS: Not found
RefSeq: Not found
5.5 Protein-Protein Interaction Databases
STRING: Not found
IntAct: P83312
MINT: P83312
DIP: Not found
BioGRID: Not found
5.6 Ligand Databases
BindingDB: Not found
DrugBank: Not found
ChEMBL: Not found
5.7 Family & Domain Databases
InterPro: Not found
PANTHER: Not found
PROSITE: Not found
5.8 Genome Annotation Databases
Ensembl: Not found
KEGG: 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




© 2023 B&BL, DoAS, IIIT-A, UP-211015, India