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381  structures 8877  species 6  interactions 61449  sequences 552  architectures

Clan: His_phosphatase (CL0071)


Histidine phosphatase superfamily Add an annotation

The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches [1].

This clan contains 2 families and the total number of domains in the clan is 61449. The clan was built by RD Finn and DJ Rigden.

Literature references

  1. Rigden DJ;, Biochem J. 2008;409:333-348.: The histidine phosphatase superfamily: structure and function. PUBMED:18092946 EPMC:18092946


This clan contains the following 2 member families:

His_Phos_1 His_Phos_2

External database links

Domain organisation

Below is a listing of the unique domain organisations or architectures from this clan. More...

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The table below shows the number of occurrences of each domain throughout the sequence database. More...

Pfam family Num. domains Alignment
His_Phos_1 (PF00300) 51823 (84.3%) View
His_Phos_2 (PF00328) 9626 (15.7%) View
Total: 2 Total: 61449 Clan alignment

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Family relationships

This diagram shows the relationships between members of this clan. More...

Species distribution

Tree controls


This tree shows the occurrence of the domains in this clan across different species. More...



There are 6 interactions for this clan. More...

Interacting families
6PF2K His_Phos_1
His_Phos_1 6PF2K
His_Phos_2 His_Phos_2
NUDIX His_Phos_1


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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