Summary: Barwin family
This is the Wikipedia entry entitled "Barwin domain". More...
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Barwin domain Edit Wikipedia article
three-dimensional structure in solution of barwin, a protein from barley seed
In molecular biology, the barwin domain is a protein domain found in barwin, a basic protein isolated from aqueous extracts of barley seeds. Barwin is 125 amino acids in length, and contains six cysteine residues that combine to form three disulphide bridges. Comparative analysis shows the sequence of barwin to be highly similar to a 122 amino acid stretch in the C-terminal of the products of two wound-induced genes (win1 and win2) from potato, the product of the hevein gene of rubber trees, and pathogenesis-related protein 4 from tobacco. The high levels of similarity to these proteins, and their ability to bind saccharides, suggest that the barwin domain may be involved in a common defence mechanism in plants.
- Svensson B, Svendsen I, Hojrup P, Roepstorff P, Ludvigsen S, Poulsen FM (September 1992). "Primary structure of barwin: a barley seed protein closely related to the C-terminal domain of proteins encoded by wound-induced plant genes". Biochemistry 31 (37): 8767–70. doi:10.1021/bi00152a012. PMID 1390663.
- Ludvigsen S, Poulsen FM (September 1992). "Secondary structure in solution of barwin from barley seed using 1H nuclear magnetic resonance spectroscopy". Biochemistry 31 (37): 8771–82. doi:10.1021/bi00152a013. PMID 1390664.
Barwin family Provide feedback
No Pfam abstract.
Internal database links
|Similarity to PfamA using HHSearch:||DPBB_1 Cerato-platanin|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001153
Barwin is a basic protein isolated from aqueous extracts of barley seeds. It is 125 amino acids in length, and contains six cysteine residues that combine to form three disulphide bridges [PUBMED:1390663, PUBMED:1390664]. Comparative analysis shows the sequence to be highly similar to a 122 amino acid stretch in the C-terminal of the products of two wound-induced genes (win1 and win2) from potato, the product of the hevein gene of rubber trees, and pathogenesis-related protein 4 from tobacco. The high levels of similarity to these proteins, and their ability to bind saccharides, suggest that the barwin domain may be involved in a common defence mechanism in plants.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Biological process||defense response to fungus (GO:0050832)|
|defense response to bacterium (GO:0042742)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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The DPBB fold is often an enzymatic domain. The members of this family are quite diverse, and if catalytic this family may contain several different functions [1,2]. This clan represents the barwin like barrels.
The clan contains the following 5 members:3D Barwin Cerato-platanin DPBB_1 Glyco_hydro_45
We make a range of alignments for each Pfam-A family:
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
|Seed source:||Sarah Teichmann|
|Number in seed:||8|
|Number in full:||153|
|Average length of the domain:||108.50 aa|
|Average identity of full alignment:||60 %|
|Average coverage of the sequence by the domain:||69.81 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||12|
|Download:||download the raw HMM for this family|
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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 Barwin domain has been found. There are 2 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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