Summary: Bombinin
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This is the Wikipedia entry entitled "Bombinin". More...
Bombinin Edit Wikipedia article
| Identifiers | |||||||||
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| Symbol | Bombinin | ||||||||
| Pfam | PF05298 | ||||||||
| InterPro | IPR007962 | ||||||||
| OPM family | 309 | ||||||||
| OPM protein | 2ap8 | ||||||||
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In molecular biology, the bombinin family of antimicrobial peptides includes the bombinin and maximin proteins from Bombina maxima (Giant fire-bellied toad). Two groups of antimicrobial peptides have been isolated from skin secretions of B. maxima.Peptides in the first group, named maximins 1, 2, 3, 4 and 5, are structurally related to bombinin-like peptides (BLPs). Unlike BLPs, sequence variations in maximins occurred all through the molecules. In addition to the potent antimicrobial activity, cytotoxicity against tumour cells and spermicidal action of maximins, maximin 3 possessed a significant anti-Simian-Human immunodeficiency virus (HIV) activity. Maximins 1 and 3 have been found to be toxic to mice. Peptides in the second group, termed maximins H1, H2, H3 and H4, are homologous with bombinin H peptides.[1]
[edit] References
- ^ Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y (March 2002). "Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima". Peptides 23 (3): 427435. doi:10.1016/S0196-9781(01)00641-6. PMID 11835991.
This article incorporates text from the public domain Pfam and InterPro IPR007962
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Bombinin Provide feedback
This family consists of Bombinin and Maximin proteins from Bombina maxima (Chinese red belly toad). Two groups of antimicrobial peptides have been isolated from skin secretions of Bombina maxima. Peptides in the first group, named maximins 1, 2, 3, 4 and 5, are structurally related to bombinin-like peptides (BLPs). Unlike BLPs, sequence variations in maximins occurred all through the molecules. In addition to the potent antimicrobial activity, cytotoxicity against tumour cells and spermicidal action of maximins, maximin 3 possessed a significant anti-HIV activity. Maximins 1 and 3 have been found to be toxic to mice. Peptides in the second group, termed maximins H1, H2, H3 and H4, are homologous with bombinin H peptides [1].
Literature references
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Lai R, Zheng YT, Shen JH, Liu GJ, Liu H, Lee WH, Tang SZ, Zhang Y; , Peptides 2002;23:427-435.: Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. PUBMED:11835991 EPMC:11835991
External database links
| PANDIT: | PF05298 |
| Pseudofam: | PF05298 |
| SYSTERS: | Bombinin |
This tab holds annotation information from the InterPro database.
InterPro entry IPR007962
This family consists of Bombinin and Maximin proteins from Bombina maxima (Giant fire-bellied toad). Two groups of antimicrobial peptides have been isolated from skin secretions of B. maxima. Peptides in the first group, named maximins 1, 2, 3, 4 and 5, are structurally related to bombinin-like peptides (BLPs). Unlike BLPs, sequence variations in maximins occurred all through the molecules. In addition to the potent antimicrobial activity, cytotoxicity against tumour cells and spermicidal action of maximins, maximin 3 possessed a significant anti-Simian-Human immunodeficiency virus (HIV) activity. Maximins 1 and 3 have been found to be toxic to mice. Peptides in the second group, termed maximins H1, H2, H3 and H4, are homologous with bombinin H peptides [PUBMED:11835991].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Cellular component | extracellular region (GO:0005576) |
| Biological process | defense response to bacterium (GO:0042742) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (3) |
Full (225) |
Representative proteomes | NCBI (219) |
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| RP15 (0) |
RP35 (0) |
RP55 (0) |
RP75 (0) |
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| PP/heatmap | 1 | |||||||
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (3) |
Full (225) |
Representative proteomes | NCBI (219) |
Meta (0) |
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| RP15 (0) |
RP35 (0) |
RP55 (0) |
RP75 (0) |
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_5347 (release 7.7) |
| Previous IDs: | none |
| Type: | Family |
| Author: | Moxon SJ |
| Number in seed: | 3 |
| Number in full: | 225 |
| Average length of the domain: | 135.80 aa |
| Average identity of full alignment: | 84 % |
| Average coverage of the sequence by the domain: | 98.03 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 141 | ||||||||||||
| Family (HMM) version: | 6 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Bombinin domain has been found. There are 1 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence