Summary
CNF1/YfiH-like putative cysteine hydrolases
Members of this clan are structurally similar. Families are a class of deamidases with a common fold consisting of three-layered alpha/beta/beta sandwich, wherein two mixed 5-stranded beta sheets are flanked by a layer of two alpha helices. In a shallow cavity at the top of the alpha/beta/beta sandwich, an invariant Cys-His pair forms a catalytic dyad that is required by the toxins for deamidation activity [1]. Deamidation is used by some bacterial virulance factors to modulate eukaryotic host cell signaling systems [2].
This clan contains 4 families and the total number of domains in the clan is 9647. The clan was built by S El-Gebali.
Literature references
- Chao X, Muff TJ, Park SY, Zhang S, Pollard AM, Ordal GW, Bilwes AM, Crane BR;, Cell. 2006;124:561-571.: A receptor-modifying deamidase in complex with a signaling phosphatase reveals reciprocal regulation. PUBMED:16469702 EPMC:16469702
- Washington EJ, Banfield MJ, Dangl JL;, Microbiol Mol Biol Rev. 2013;77:527-539.: What a difference a Dalton makes: bacterial virulence factors modulate eukaryotic host cell signaling systems via deamidation. PUBMED:24006474 EPMC:24006474
Members
This clan contains the following 4 member families:
BLF1 CheD CNF1 Cu-oxidase_4Domain organisation
Below is a listing of the unique domain organisations or architectures from this clan. More...
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Alignments
The table below shows the number of occurrences of each domain throughout the sequence database. More...
Pfam family | Num. domains | Alignment |
---|---|---|
Cu-oxidase_4 (PF02578) | 6621 (68.6%) | View |
CheD (PF03975) | 2999 (31.1%) | View |
CNF1 (PF05785) | 25 (0.3%) | View |
BLF1 (PF17752) | 2 (0.0%) | View |
Total: 4 | Total: 9647 | Clan alignment |
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Family relationships
This diagram shows the relationships between members of this clan. More...
Species distribution
Tree controls
HideThis tree shows the occurrence of the domains in this clan across different species. More...
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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 MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.
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