Summary: Apyrase
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Apyrase Edit Wikipedia article
Apyrase | |||||||||
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![]() structure and protein design of human apyrase
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Identifiers | |||||||||
Symbol | Apyrase | ||||||||
Pfam | PF06079 | ||||||||
InterPro | IPR009283 | ||||||||
SCOP | 1s1d | ||||||||
SUPERFAMILY | 1s1d | ||||||||
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Apyrase (EC 3.6.1.5, ATP-diphosphatase, adenosine diphosphatase, ADPase, ATP diphosphohydrolase) is a calcium-activated plasma membrane-bound enzyme (magnesium can also activate it) (EC 3.6.1.5) that catalyses the hydrolysis of ATP to yield AMP and inorganic phosphate. Two isoenzymes are found in commercial preparations from S. tuberosum. One with a higher ratio of substrate selectivity for ATP:ADP (approx 10) and another with no selectivity (ratio 1).
It can also act on ADP and other nucleoside triphosphates and diphosphates with the general reaction being NTP -> NDP + Pi -> NMP + 2Pi. This is the same activity that has been employed in the degradation of unincorporated nucleosides during pyrosequencing.
The salivary apyrases of blood-feeding arthropods are nucleotide hydrolysing enzymes that are implicated in the inhibition of host platelet aggregation through the hydrolysis of extracellular adenosine diphosphate.[1]
References
- ^ Smith TM, Hicks-Berger CA, Kim S, Kirley TL (October 2002). "Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases". Arch. Biochem. Biophys. 406 (1): 105–15. PMID 12234496. doi:10.1016/S0003-9861(02)00420-4.
External links
- Apyrase at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the public domain Pfam and InterPro IPR009283
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This family consists of several eukaryotic apyrase proteins ( EC:3.6.1.5). The salivary apyrases of blood-feeding arthropods are nucleotide hydrolysing enzymes implicated in the inhibition of host platelet aggregation through the hydrolysis of extracellular adenosine diphosphate. [1].
Literature references
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Smith TM, Hicks-Berger CA, Kim S, Kirley TL; , Arch Biochem Biophys 2002;406:105-115.: Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. PUBMED:12234496 EPMC:12234496
External database links
SCOP: | 1s1d |
This tab holds annotation information from the InterPro database.
InterPro entry IPR009283
This family consists of several eukaryotic apyrase (or adenosine diphosphatase) proteins (EC), and related nucleoside diphosphatases (EC). The salivary apyrases of blood-feeding arthropods are nucleotide hydrolysing enzymes implicated in the inhibition of host platelet aggregation through the hydrolysis of extracellular adenosine diphosphate [PUBMED:9804829, PUBMED:12234496]. Soluble calcium-activated nucleotidase 1 (CANT1) is the human homologue [PUBMED:15248776].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | calcium ion binding (GO:0005509) |
nucleoside-diphosphatase activity (GO:0017110) |
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 B_Fructosidase (CL0143), which has the following description:
This beta fructosidase superfamily [4] is composed of glycosyl hydrolase families. The members of this clan adopt a five-bladed beta-propeller fold [2-3]. The beta-fructosidase superfamily is also known as furanosidase superfamily [4].
The clan contains the following 9 members:
Apyrase DUF1861 DUF5005 Glyco_hydro_130 Glyco_hydro_32N Glyco_hydro_43 Glyco_hydro_62 Glyco_hydro_68 TachylectinAlignments
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 (55) |
Full (657) |
Representative proteomes | UniProt (1170) |
NCBI (1294) |
Meta (2) |
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RP15 (310) |
RP35 (433) |
RP55 (546) |
RP75 (597) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
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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 (55) |
Full (657) |
Representative proteomes | UniProt (1170) |
NCBI (1294) |
Meta (2) |
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RP15 (310) |
RP35 (433) |
RP55 (546) |
RP75 (597) |
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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: | Pfam-B_7593 (release 9.0) |
Previous IDs: | SHAPY; |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Moxon SJ |
Number in seed: | 55 |
Number in full: | 657 |
Average length of the domain: | 244.60 aa |
Average identity of full alignment: | 41 % |
Average coverage of the sequence by the domain: | 69.06 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 294 | ||||||||||||
Family (HMM) version: | 11 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
ApyraseStructures
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 Apyrase domain has been found. There are 8 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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