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8  structures 129  species 1  interaction 238  sequences 4  architectures

Family: Apyrase (PF06079)

Summary: Apyrase

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This is the Wikipedia entry entitled "Apyrase". More...

Apyrase Edit Wikipedia article

Apyrase
PDB 1s18 EBI.jpg
structure and protein design of human apyrase
Identifiers
Symbol Apyrase
Pfam PF06079
InterPro IPR009283
SCOP 1s1d
SUPERFAMILY 1s1d

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.

The salivary apyrases of blood-feeding arthropods are nucleotide hydrolysing enzymes are implicated in the inhibition of host platelet aggregation through the hydrolysis of extracellular adenosine diphosphate.[1]


References[edit]

  1. ^ 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. doi:10.1016/S0003-9861(02)00420-4. PMID 12234496. 

External links[edit]

This article incorporates text from the public domain Pfam and InterPro IPR009283

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.

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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

  1. 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

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:12234496].

Gene Ontology

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Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

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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
(20)
Full
(238)
Representative proteomes NCBI
(237)
Meta
(2)
RP15
(48)
RP35
(57)
RP55
(86)
RP75
(104)
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Format an alignment

  Seed
(20)
Full
(238)
Representative proteomes NCBI
(237)
Meta
(2)
RP15
(48)
RP35
(57)
RP55
(86)
RP75
(104)
Alignment:
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Sequence:
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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
(20)
Full
(238)
Representative proteomes NCBI
(237)
Meta
(2)
RP15
(48)
RP35
(57)
RP55
(86)
RP75
(104)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

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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_7593 (release 9.0)
Previous IDs: SHAPY;
Type: Family
Author: Moxon SJ
Number in seed: 20
Number in full: 238
Average length of the domain: 249.00 aa
Average identity of full alignment: 43 %
Average coverage of the sequence by the domain: 77.24 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.3 20.3
Trusted cut-off 20.5 35.5
Noise cut-off 19.7 19.4
Model length: 291
Family (HMM) version: 6
Download: download the raw HMM for this family

Species distribution

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Interactions

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

Apyrase

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 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 seqence.

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