Summary: Calcineurin-like phosphoesterase
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Calcineurin-like phosphoesterase Provide feedback
This family includes a diverse range of phosphoesterases [1] including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD P13457 or yeast MRE11 P32829. The most conserved regions in this superfamily centre around the metal chelating residues.
Literature references
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Aravind L, Koonin EV; , Nucleic Acids Res 1998;26:3746-3752.: Phosphoesterase domains associated with DNA polymerases of diverse origins. PUBMED:9685491 EPMC:9685491
Internal database links
SCOOP: | DNA_pol_E_B FBPase_2 Glyco_hydro_65N Metallophos_2 Metallophos_3 Metallophos_C PGA_cap PhoD YmdB |
Similarity to PfamA using HHSearch: | Metallophos_2 YmdB Metallophos_3 |
External database links
HOMSTRAD: | stpp |
SCOP: | 1fjm |
This tab holds annotation information from the InterPro database.
InterPro entry IPR004843
This domain is found in a diverse range of phosphoesterases [PUBMED:9685491], including bis(5'-nucleosyl)-tetraphosphatase (apaH), nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases, as well as nucleases such as bacterial SbcD or archaeal/yeast Mre11. The most conserved regions in this domain centre around the metal chelating residues.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | hydrolase activity (GO:0016787) |
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 Calcineurin (CL0163), which has the following description:
This clan contains the calcineurin-like phosphoesterases. This clan also includes the apparently inactive homologues from the small DNA polymerase subunits [1].
The clan contains the following 9 members:
DNA_pol_E_B FBPase_2 Metallophos Metallophos_2 Metallophos_3 PGA_cap PhoD PhoD_2 YmdBAlignments
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...
View options
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 (324) |
Full (91934) |
Representative proteomes | UniProt (305295) |
NCBI (476632) |
Meta (6666) |
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RP15 (13471) |
RP35 (42190) |
RP55 (81693) |
RP75 (133855) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
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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 (324) |
Full (91934) |
Representative proteomes | UniProt (305295) |
NCBI (476632) |
Meta (6666) |
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---|---|---|---|---|---|---|---|---|---|
RP15 (13471) |
RP35 (42190) |
RP55 (81693) |
RP75 (133855) |
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Raw Stockholm | |||||||||
Gzipped |
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
Seed source: | Dlakic M |
Previous IDs: | STphosphatase; |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Dlakic M |
Number in seed: | 324 |
Number in full: | 91934 |
Average length of the domain: | 210.00 aa |
Average identity of full alignment: | 13 % |
Average coverage of the sequence by the domain: | 48.07 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 205 | ||||||||||||
Family (HMM) version: | 29 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Selections
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
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Interactions
There are 25 interactions for this family. More...
Metallophos B56 EF-hand_7 PPP5 TPR_1 Shugoshin_N Rb_C FKBP_C PDZ Pro_isomerase Mre11_DNA_bind HEAT_2 5_nucleotid_C LCM 5_nucleotid_C EF-hand_1 Metallophos_C PPP5 SbcCD_C Abhydrolase_6 IPP-2 Metallophos_C SbcD_C Ank_2 EF-hand_7Structures
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 Metallophos domain has been found. There are 506 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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