Summary: Type I phosphodiesterase / nucleotide pyrophosphatase
Type I phosphodiesterase / nucleotide pyrophosphatase Provide feedback
This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyse the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars . Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity . The alignment encompasses the active site [3,4]. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum .
Jin-Hua P, Goding JW, Nakamura H, Sano K; , Genomics 1997;45:412-415.: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. PUBMED:9344668 EPMC:9344668
Deissler H, Lottspeich F, Rajewsky MF; , J Biol Chem 1995;270:9849-9855.: Affinity purification and cDNA cloning of rat neural differentiation and tumor cell surface antigen gp130RB13-6 reveals relationship to human and murine PC-1. PUBMED:7730366 EPMC:7730366
Murata J, Lee HY, Clair T, Krutzsch HC, Arestad AA, Sobel ME, Liotta LA, Stracke ML; , J Biol Chem 1994;269:30479-30484.: cDNA cloning of the human tumor motility-stimulating protein, autotaxin, reveals a homology with phosphodiesterases. PUBMED:7982964 EPMC:7982964
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002591
This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase I / nucleotide pyrophosphatase (nppase). These enzymes catalyse the cleavage of phosphodiester and phosphosulphate bonds in NAD, deoxynucleotides and nucleotide sugars [PUBMED:9344668]. Another member of this family is ATX an autotaxin, tumor cell motility-stimulating protein which exhibits type I phosphodiesterases activity [PUBMED:7982964]. The alignment encompasses the active site [PUBMED:7730366, PUBMED:7982964]. Also present within this family is 60 kDa Ca2+-ATPase from Myroides odoratus [PUBMED:8617788].
This signature also hits a number of ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
|Molecular function||catalytic activity (GO:0003824)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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The members of this clan all share a common structure of their catalytic domains, which contain conserved metal binding residues .
The clan contains the following 9 members:Alk_phosphatase DUF1501 DUF229 Metalloenzyme PglZ Phosphodiest Phosphoesterase Sulfatase Sulfatase_C
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Curation and family details
|Seed source:||Pfam-B_994 (release 4.1) & Pfam-B_6150 (Release 8.0)|
|Author:||Bashton M, Bateman A|
|Number in seed:||70|
|Number in full:||4764|
|Average length of the domain:||283.30 aa|
|Average identity of full alignment:||14 %|
|Average coverage of the sequence by the domain:||54.15 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||17|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 Phosphodiest domain has been found. There are 34 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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