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2  structures 42  species 0  interactions 371  sequences 5  architectures

Family: AvrRpt-cleavage (PF05627)

Summary: Cleavage site for pathogenic type III effector avirulence factor Avr

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Cleavage site for pathogenic type III effector avirulence factor Avr Provide feedback

This domain is conserved in small families of otherwise unrelated proteins in both mono-cots and di-cots, suggesting that it has a conserved, plant-specific function. It is found both in the plant RIN4 (resistance R membrane-bound host-target protein) where it appears to contribute to the binding of the protein to both RCS (AvrRpt2 auto-cleavage site) and AvrB, the virulence factor from the infecting bacterium [1]. The cleavage site for the AvrRpt2 avirulence protein would appear to be the sequence motifs VPQFGDW and LPKFGEW, both of which are highly conserved within the domain [3].

Literature references

  1. Kim HS, Desveaux D, Singer AU, Patel P, Sondek J, Dangl JL; , Proc Natl Acad Sci U S A. 2005;102:6496-6501.: The Pseudomonas syringae effector AvrRpt2 cleaves its C-terminally acylated target, RIN4, from Arabidopsis membranes to block RPM1 activation. PUBMED:15845764 EPMC:15845764

  2. Kottapalli KR, Sarla N, Kikuchi S; , Biotechnol Adv. 2006;24:561-589.: In silico insight into two rice chromosomal regions associated with submergence tolerance and resistance to bacterial leaf blight and gall midge. PUBMED:16887318 EPMC:16887318

  3. Takemoto D, Jones DA; , Mol Plant Microbe Interact. 2005;18:1258-1268.: Membrane release and destabilization of Arabidopsis RIN4 following cleavage by Pseudomonas syringae AvrRpt2. PUBMED:16478045 EPMC:16478045


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR008700

This domain is conserved in small families of otherwise unrelated proteins in both mono-cots and di-cots, suggesting that it has a conserved, plant-specific function. It is found both in the plant RIN4 (resistance R membrane-bound host-target protein) where it appears to contribute to the binding of the protein to both RCS (AvrRpt2 auto-cleavage site) and AvrB, the virulence factor from the infecting bacterium [PUBMED:15845764]. The cleavage site for the AvrRpt2 avirulence protein would appear to be the sequence motifs VPQFGDW and LPKFGEW, both of which are highly conserved within the domain [PUBMED:16478045].

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

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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics 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.

  Seed
(22)
Full
(371)
Representative proteomes NCBI
(352)
Meta
(0)
RP15
(22)
RP35
(94)
RP55
(132)
RP75
(166)
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Format an alignment

  Seed
(22)
Full
(371)
Representative proteomes NCBI
(352)
Meta
(0)
RP15
(22)
RP35
(94)
RP55
(132)
RP75
(166)
Alignment:
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Sequence:
Gaps:
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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
(22)
Full
(371)
Representative proteomes NCBI
(352)
Meta
(0)
RP15
(22)
RP35
(94)
RP55
(132)
RP75
(166)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download    
Gzipped Download   Download   Download   Download   Download   Download   Download    

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.

Pfam alignments:

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 View help on the curation process

Seed source: Pfam-B_9342 (release 8.0)
Previous IDs: NOI;
Type: Domain
Author: Moxon SJ, Coggill P
Number in seed: 22
Number in full: 371
Average length of the domain: 36.90 aa
Average identity of full alignment: 43 %
Average coverage of the sequence by the domain: 27.04 %

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 20.3 20.3
Trusted cut-off 20.8 20.3
Noise cut-off 20.1 19.9
Model length: 39
Family (HMM) version: 6
Download: download the raw HMM for this family

Species distribution

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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 AvrRpt-cleavage 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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