Summary: Barstar (barnase inhibitor)
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Barstar Edit Wikipedia article
Barstar (barnase inhibitor) | |||||||||
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Identifiers | |||||||||
Symbol | Barstar | ||||||||
Pfam | PF01337 | ||||||||
InterPro | IPR000468 | ||||||||
SCOP | 1brs | ||||||||
SUPERFAMILY | 1brs | ||||||||
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Barstar is a small protein synthesized by the bacterium Bacillus amyloliquefaciens. Its function is to inhibit the ribonuclease activity of its binding partner barnase, with which it forms an extraordinarily tightly bound complex within the cell until barnase is secreted.[2][3] Expression of barstar is necessary to counter the lethal effect of expressed active barnase. The structure of the barnase-barstar complex is known.[4]
References
- ^ PDB: 1BRS; Buckle AM, Schreiber G, Fersht AR (August 1994). "Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-A resolution". Biochemistry. 33 (30): 8878–89. doi:10.1021/bi00196a004. PMID 8043575.
- ^ Hartley RW (1989). "Barnase and barstar: two small proteins to fold and fit together". Trends Biochem. Sci. 14 (11): 450–454. doi:10.1016/0968-0004(89)90104-7. PMID 2696173.
- ^ Hartley RW (1988). "Barnase and barstar. Expression of its cloned inhibitor permits expression of a cloned ribonuclease". J. Mol. Biol. 202 (4): 913–915. doi:10.1016/0022-2836(88)90568-2. PMID 3050134.
- ^ Fersht AR, Buckle AM, Schreiber G (1994). "Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-A resolution". Biochemistry. 33 (30): 8878–8889. doi:10.1021/bi00196a004. PMID 8043575.
This article incorporates text from the public domain Pfam and InterPro IPR000468
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Literature references
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Buckle AM, Schreiber G, Fersht AR; , Biochemistry 1994;33:8878-8889.: Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-A resolution. PUBMED:8043575 EPMC:8043575
External database links
SCOP: | 1brs |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000468
Barstar is a small single chain protein. Barnase is the extracellular ribonuclease INTERPRO of Bacillus amyloliquefaciens, and barstar its specific intracellular inhibitor [PUBMED:2696173, PUBMED:3050134]. Expression of barstar is necessary to counter the lethal effect of expressed active barnase.The structure of the barstar consists of two layers of parallel beta-sheet of three strands. Barstar inhibits barnase by statically blocking the active site with a helix and adjacent loop segment [PUBMED:8043575].
Domain organisation
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Alignments
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Seed (102) |
Full (1995) |
Representative proteomes | UniProt (5555) |
NCBI (8392) |
Meta (27) |
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RP15 (318) |
RP35 (1146) |
RP55 (2036) |
RP75 (3172) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (102) |
Full (1995) |
Representative proteomes | UniProt (5555) |
NCBI (8392) |
Meta (27) |
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---|---|---|---|---|---|---|---|---|---|
RP15 (318) |
RP35 (1146) |
RP55 (2036) |
RP75 (3172) |
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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.
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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: | Sarah Teichmann |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Finn RD |
Number in seed: | 102 |
Number in full: | 1995 |
Average length of the domain: | 83.10 aa |
Average identity of full alignment: | 22 % |
Average coverage of the sequence by the domain: | 58.94 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 79 | ||||||||||||
Family (HMM) version: | 18 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Interactions
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 Barstar domain has been found. There are 47 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 sequence.
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