Summary: Domain of Unknown Function (DUF1542)
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Domain of unknown function Edit Wikipedia article
A Domain of unknown function (DUF) is a protein domain that has no characterised function. These families have been collected together in the Pfam database using the prefix DUF followed by a number, with examples being DUF188 and DUF1000. There are now over 3,000 DUF families within the Pfam database representing over 20% of known families.
History
The DUF naming scheme was introduced by Chris Ponting, through the addition of DUF1 and DUF2 to the SMART database.[1] These two domains were found to be widely distributed in bacterial signaling proteins. Subsequently, the functions of these domains were identified and they have since been renamed as the GGDEF domain and EAL domain respectively.
Structure
Structural genomics programmes have attempted to understand the function of DUFs through structure determination. The structures of over 250 DUF families have been solved.[2]
External Links
List of Pfam familes beginning with the letter D, including DUF families
References
- ^ Schultz J, Milpetz F, Bork P, Ponting CP (1998). "SMART, a simple modular architecture research tool: identification of signaling domains". Proc. Natl. Acad. Sci. U.S.A. 95 (11): 5857–64. PMC 34487. PMID 9600884.
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This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
"DUF" families are annotated with the Domain of unknown function Wikipedia article. This is a general article, with no specific information about individual Pfam DUFs. If you have information about this particular DUF, please let us know using the "Add annotation" button below.
Domain of Unknown Function (DUF1542) Provide feedback
This domain is found in several cell surface proteins, such as extracellular matrix-binding protein ebh [1]. Some members are involved in antibiotic resistance (e.g Q9RL69 and Q9LCJ9) [2] and/or cellular adhesion (e.g. Q931R6) [1]. In some proteins it is repeated more than fifteen times, being the most repeated domain in streptococci [3]. This is a predominantly alpha-helical domain that form a long, thin, fibre-like structure and it has been proposed to function as a stalk that helps the adhesive non-repeat region (NRR) of proteins protrude beyond the cell surface [4,5].
Literature references
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Clarke SR, Harris LG, Richards RG, Foster SJ; , Infect Immun 2002;70:6680-6687.: Analysis of Ebh, a 1.1-megadalton cell wall-associated fibronectin-binding protein of Staphylococcus aureus. PUBMED:12438342 EPMC:12438342
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Wu SW, De Lencastre H; , Microb Drug Resist 1999;5:9-18.: Mrp--a new auxiliary gene essential for optimal expression of methicillin resistance in Staphylococcus aureus. PUBMED:10332717 EPMC:10332717
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Lin IH, Hsu MT, Chang CH;, Genomics. 2012;100:370-379.: Protein domain repetition is enriched in Streptococcal cell-surface proteins. PUBMED:22921469 EPMC:22921469
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Gaytan MO, Singh AK, Woodiga SA, Patel SA, An SS, Vera-Ponce de Leon A, McGrath S, Miller AR, Bush JM, van der Linden M, Magrini V, Wilson RK, Kitten T, King SJ;, PLoS Pathog. 2021;17:e1009222.: A novel sialic acid-binding adhesin present in multiple species contributes to the pathogenesis of Infective endocarditis. PUBMED:33465168 EPMC:33465168
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Linke C, Siemens N, Oehmcke S, Radjainia M, Law RH, Whisstock JC, Baker EN, Kreikemeyer B;, J Biol Chem. 2012;287:38178-38189.: The extracellular protein factor Epf from Streptococcus pyogenes is a cell surface adhesin that binds to cells through an N-terminal domain containing a carbohydrate-binding module. PUBMED:22977243 EPMC:22977243
Internal database links
SCOOP: | GA |
This tab holds annotation information from the InterPro database.
InterPro entry IPR011439
This domain is found in several cell surface proteins, such as extracellular matrix-binding protein ebh [ PUBMED:12438342 ]. Some members are involved in antibiotic resistance (e.g. SWISSPROT and SWISSPROT ) [ PUBMED:10332717 ] and/or cellular adhesion (e.g. SWISSPROT ) [ PUBMED:12438342 ]. In some proteins it is repeated more than fifteen times, being the most repeated domain in streptococci [ PUBMED:22921469 ]. This is a predominantly alpha-helical domain that form a long, thin, fibre-like structure and it has been proposed to function as a stalk that helps the adhesive non-repeat region (NRR) of proteins protrude beyond the cell surface [ PUBMED:33465168 , PUBMED:22977243 ].
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
Alignments
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...
View options
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 (107) |
Full (756) |
Representative proteomes | UniProt (14209) |
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RP15 (120) |
RP35 (351) |
RP55 (702) |
RP75 (1726) |
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Jalview | |||||||
HTML | |||||||
PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not 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 (107) |
Full (756) |
Representative proteomes | UniProt (14209) |
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RP15 (120) |
RP35 (351) |
RP55 (702) |
RP75 (1726) |
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Raw Stockholm | |||||||
Gzipped |
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...
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: | Yeats C |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Yeats C |
Number in seed: | 107 |
Number in full: | 756 |
Average length of the domain: | 74.4 aa |
Average identity of full alignment: | 32 % |
Average coverage of the sequence by the domain: | 41.65 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 77 | ||||||||||||
Family (HMM) version: | 14 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Selections
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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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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.
Protein | Predicted structure | External Information |
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Q2FW95 | View 3D Structure | Click here |
Q2FXH4 | View 3D Structure | Click here |
Q8CY93 | View 3D Structure | Click here |