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0  structures 26  species 0  interactions 143  sequences 4  architectures

Family: DIM (PF08194)

Summary: DIM protein

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This is the Wikipedia entry entitled "Drosocin". More...

Drosocin Edit Wikipedia article

SymbolDrosocin, Dro or Drc

Drosocin is a 19-residue long antimicrobial peptide of flies first isolated in the fruit fly Drosophila melanogaster, and later shown to be conserved through the genus Drosophila.[1][2] Drosocin is regulated by Imd signalling in the fly.

Structure and Function

Drosocin is primarily active against Gram-negative bacteria. The peptide is Proline-rich with Proline-Arginine repeats, as well a critical threonine residue. This threonine is O-glycosylated, which is required for antimicrobial activity.[3] This O-glycosylation can be performed either by mono- or disaccharides, which have different activity spectra.[4] Like the antimicrobial peptides Pyrrhocoricin and Abaecin, Drosocin binds to bacterial DnaK, inhibiting cell machinery and replication.[5] The action of these Drosocin-like peptides is potentiated by the presence of pore-forming peptides, which facilitates the entry of Drosocin-like peptides into the baceterial cell.[6] In the absence of pore-forming peptides, the related AMP Pyrrhocoricin is taken into the bacteria by the action of uptake permeases.[7]


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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.

DIM protein Provide feedback

Drosophila immune-induced molecules (DIMs) are short proteins induced during the immune response of Drosophila. This family includes DIMs 1 to 4 that have masses below 5 kDa [1].

Literature references

  1. Uttenweiler-Joseph S, Moniatte M, Lagueux M, Van Dorsselaer A, Hoffmann JA, Bulet P; , Proc Natl Acad Sci U S A 1998;95:11342-11347.: Differential display of peptides induced during the immune response of Drosophila: a matrix-assisted laser desorption ionization time-of-flight mass spectrometry study. PUBMED:9736738 EPMC:9736738

This tab holds annotation information from the InterPro database.

InterPro entry IPR013172

Drosophila immune-induced molecules (DIMs), also know as bomanins, are short proteins induced during the immune response of Drosophila [ PUBMED:9736738 , PUBMED:25915418 ]. The Bomanins (Boms) are a family of a dozen secreted peptides, this entry includes Bomanin Short 1 to 3, Bomanin-23, Bomanin-65, Bomanin-68 and Bomanin-836.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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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.

Representative proteomes UniProt
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

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Representative proteomes UniProt

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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.

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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...


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 View help on the curation process

Seed source: Short protein clustering
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Rossi R
Number in seed: 15
Number in full: 143
Average length of the domain: 35 aa
Average identity of full alignment: 48 %
Average coverage of the sequence by the domain: 46.29 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.8 20.8
Trusted cut-off 20.8 20.8
Noise cut-off 20.6 20.6
Model length: 36
Family (HMM) version: 15
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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trRosetta Structure

The structural model below was generated by the Baker group with the trRosetta software using the Pfam UniProt multiple sequence alignment.

The InterPro website shows the contact map for the Pfam SEED alignment. Hovering or clicking on a contact position will highlight its connection to other residues in the alignment, as well as on the 3D structure.

Improved protein structure prediction using predicted inter-residue orientations. Jianyi Yang, Ivan Anishchenko, Hahnbeom Park, Zhenling Peng, Sergey Ovchinnikov, David Baker Proceedings of the National Academy of Sciences Jan 2020, 117 (3) 1496-1503; DOI: 10.1073/pnas.1914677117;