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47  structures 1143  species 2  interactions 1251  sequences 10  architectures

Family: Barstar (PF01337)

Summary: Barstar (barnase inhibitor)

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

Barstar Edit Wikipedia article

Barstar (barnase inhibitor)
Barstar-barnase-1brs.png
The tightly bound complex between barstar and barnase, the ribonuclease barstar inhibits. Barstar is colored by secondary structure and barnase is colored in blue.[1]
Identifiers
Symbol Barstar
Pfam PF01337
InterPro IPR000468
SCOP 1brs
SUPERFAMILY 1brs

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[edit]

  1. ^ 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. 
  2. ^ 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. 
  3. ^ 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. 
  4. ^ 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


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.

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No Pfam abstract.

Literature references

  1. 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

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 barnase-barstar complex is known [PUBMED:8043575].

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
(52)
Full
(1251)
Representative proteomes NCBI
(726)
Meta
(26)
RP15
(59)
RP35
(152)
RP55
(209)
RP75
(253)
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  Seed
(52)
Full
(1251)
Representative proteomes NCBI
(726)
Meta
(26)
RP15
(59)
RP35
(152)
RP55
(209)
RP75
(253)
Alignment:
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  Seed
(52)
Full
(1251)
Representative proteomes NCBI
(726)
Meta
(26)
RP15
(59)
RP35
(152)
RP55
(209)
RP75
(253)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
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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.

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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

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Seed source: Sarah Teichmann
Previous IDs: none
Type: Domain
Author: Finn RD, Bateman A
Number in seed: 52
Number in full: 1251
Average length of the domain: 85.60 aa
Average identity of full alignment: 29 %
Average coverage of the sequence by the domain: 72.31 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.0 21.0
Trusted cut-off 21.3 21.2
Noise cut-off 20.8 20.6
Model length: 90
Family (HMM) version: 13
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 2 interactions for this family. More...

Ribonuclease Barstar

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 seqence.

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