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40  structures 91  species 1  interaction 140  sequences 7  architectures

Family: FB_lectin (PF07367)

Summary: Fungal fruit body lectin

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This is the Wikipedia entry entitled "Fungal fruit body lectin family". More...

Fungal fruit body lectin family Edit Wikipedia article

Fungal fruit body lectin
PDB 1y2u EBI.jpg
crystal structure of the common edible mushroom (Agaricus bisporus) lectin in complex with lacto-N-biose
Identifiers
Symbol FB_lectin
Pfam PF07367
InterPro IPR009960

In molecular biology, the fungal fruit body lectin family consists of several fungal fruit body lectin proteins. Fruit body lectins are thought to have insecticidal activity [1] and may also function in capturing nematodes.[2] One member of this family, the lectin XCL from Boletus chrysenteron (formerly Xerocomus chrysenteron), induces drastic changes in the actin cytoskeleton after sugar binding at the cell surface and internalisation, and has potent insecticidal activity. The fold of lectin XCL is not related to any of several other lectin folds, but shows significant structural similarity to cytolysins.[3]

References

  1. ^ Trigueros V, Lougarre A, Ali-Ahmed D, Rahbe Y, Guillot J, Chavant L, Fournier D, Paquereau L (June 2003). "Xerocomus chrysenteron lectin: identification of a new pesticidal protein". Biochim. Biophys. Acta. 1621 (3): 292–8. doi:10.1016/s0304-4165(03)00098-9. PMID 12787928. 
  2. ^ Iijima N, Yoshino H, Ten LC, Ando A, Watanabe K, Nagata Y (October 2002). "Two genes encoding fruit body lectins of Pleurotus cornucopiae: sequence similarity with the lectin of a nematode-trapping fungus". Biosci. Biotechnol. Biochem. 66 (10): 2083–9. doi:10.1271/bbb.66.2083. PMID 12450118. 
  3. ^ Birck C, Damian L, Marty-Detraves C, Lougarre A, Schulze-Briese C, Koehl P, Fournier D, Paquereau L, Samama JP (December 2004). "A new lectin family with structure similarity to actinoporins revealed by the crystal structure of Xerocomus chrysenteron lectin XCL". J. Mol. Biol. 344 (5): 1409–20. doi:10.1016/j.jmb.2004.10.007. PMID 15561152. 

This article incorporates text from the public domain Pfam and InterPro IPR009960

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.

Fungal fruit body lectin Provide feedback

This family consists of several fungal fruit body lectin proteins. Fruit body lectins are thought to have insecticidal activity [1,2] and may also function in capturing nematodes [3].

Literature references

  1. Wang M, Trigueros V, Paquereau L, Chavant L, Fournier D; , J Econ Entomol 2002;95:603-607.: Proteins as active compounds involved in insecticidal activity of mushroom fruitbodies. PUBMED:12076007 EPMC:12076007

  2. Trigueros V, Lougarre A, Ali-Ahmed D, Rahbe Y, Guillot J, Chavant L, Fournier D, Paquereau L; , Biochim Biophys Acta 2003;1621:292-298.: Xerocomus chrysenteron lectin: identification of a new pesticidal protein. PUBMED:12787928 EPMC:12787928

  3. Iijima N, Yoshino H, Ten LC, Ando A, Watanabe K, Nagata Y; , Biosci Biotechnol Biochem 2002;66:2083-2089.: Two genes encoding fruit body lectins of Pleurotus cornucopiae: sequence similarity with the lectin of a nematode-trapping fungus. PUBMED:12450118 EPMC:12450118


This tab holds annotation information from the InterPro database.

InterPro entry IPR009960

This family consists of several fungal fruit body lectin proteins. Fruit body lectins are thought to have insecticidal activity [PUBMED:12787928] and may also function in capturing nematodes [PUBMED:12450118]. One member of this family, the lectin XCL from Xerocomus chrysenteron, induces drastic changes in the actin cytoskeleton after sugar binding at the cell surface and internalization, and has potent insecticidal activity. The fold of lectin xcl is not related to any of several lectin folds, but but shows significant structural similarity to cytolysins [PUBMED:15561152].

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

This family is a member of clan CDC (CL0293), which has the following description:

This superfamily includes the MACPF domain as well as the Cholesterol-dependent cytolysins [1].

The clan contains the following 8 members:

Aegerolysin Anemone_cytotox FB_lectin Gasdermin MACPF TDH Thaumatin Thiol_cytolysin

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, the UniProtKB sequence database, 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
(14)
Full
(140)
Representative proteomes UniProt
(199)
NCBI
(235)
Meta
(0)
RP15
(34)
RP35
(88)
RP55
(108)
RP75
(141)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

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  Seed
(14)
Full
(140)
Representative proteomes UniProt
(199)
NCBI
(235)
Meta
(0)
RP15
(34)
RP35
(88)
RP55
(108)
RP75
(141)
Alignment:
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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
(14)
Full
(140)
Representative proteomes UniProt
(199)
NCBI
(235)
Meta
(0)
RP15
(34)
RP35
(88)
RP55
(108)
RP75
(141)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download    
Gzipped Download   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.

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_20370 (release 10.0)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Moxon SJ
Number in seed: 14
Number in full: 140
Average length of the domain: 129.40 aa
Average identity of full alignment: 35 %
Average coverage of the sequence by the domain: 69.59 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 28.2 27.1
Noise cut-off 24.0 21.7
Model length: 140
Family (HMM) version: 11
Download: download the raw HMM for this family

Species distribution

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Selections

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Interactions

There is 1 interaction for this family. More...

FB_lectin

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 FB_lectin domain has been found. There are 40 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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