Summary: Protein-arginine deiminase (PAD)
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Protein-arginine deiminase (PAD) Provide feedback
Members of this family are found in mammals. In the presence of calcium ions, PAD enzymes EC:3.5.3.15 catalyse the post-translational modification reaction responsible for the formation of citrulline residues: Protein L-arginine + H2O <=> Protein L-citrulline + NH3. Several types are recognised (and included in the family) on the basis of molecular mass, substrate specificity, and tissue localisation. The expression of type I PAD is known to be under the control of oestrogen [3].
Literature references
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Rogers G, Winter B, McLaughlan C, Powell B, Nesci T; , J Invest Dermatol 1997;108:700-707.: Peptidylarginine deiminase of the hair follicle: characterization, localization, and function in keratinizing tissues. PUBMED:9129218 EPMC:9129218
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Asaga H, Ishigami A; , Neurosci Lett 2001;299:5-8.: Protein deimination in the rat brain after kainate administration: citrulline-containing proteins as a novel marker of neurodegeneration. PUBMED:11166924 EPMC:11166924
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Rus'd AA, Ikejiri Y, Ono H, Yonekawa T, Shiraiwa M, Kawada A, Takahara H; , Eur J Biochem 1999;259:660-669.: Molecular cloning of cDNAs of mouse peptidylarginine deiminase type I, type III and type IV, and the expression pattern of type I in mouse. PUBMED:10092850 EPMC:10092850
This tab holds annotation information from the InterPro database.
InterPro entry IPR013530
In the presence of calcium ions, Protein-arginine deiminase (PAD) enzymes EC catalyse the post-translational modification reaction responsible for the formation of citrulline residues from protein-bound arginine residues [ PUBMED:10092850 ]. Four PAD isotypes of PAD have been identified in mammals, a fifth may also exist. Non-mammalian vertebrates appear to have only a single PAD enzyme. All known natural substrates of PAD are proteins known to have an important structural function, such as keratin (PAD1), intermediate filaments or proteins associated with intermediate filaments. Citrulination may have consequences for the structural integrity and interactions of these proteins. Physiological levels of calcium appear to be too low to activate these enzymes suggesting a role between PAD activation and loss of calcium homeostasis during terminal differentiation and cell death (apoptosis).
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Cellular component | cytoplasm (GO:0005737) |
Molecular function | calcium ion binding (GO:0005509) |
protein-arginine deiminase activity (GO:0004668) |
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 GME (CL0197), which has the following description:
This superfamily contains a number of related enzymes such as AstB, peptidyl-arginine deiminase, arginine deiminase and amidinotransferase [1,2].
The clan contains the following 6 members:
ADI AstB DDAH_eukar eIF-6 PAD PAD_porphAlignments
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 and the UniProtKB 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 (53) |
Full (1659) |
Representative proteomes | UniProt (3215) |
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RP15 (111) |
RP35 (468) |
RP55 (1248) |
RP75 (1847) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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Seed (53) |
Full (1659) |
Representative proteomes | UniProt (3215) |
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RP15 (111) |
RP35 (468) |
RP55 (1248) |
RP75 (1847) |
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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_2195 (release 6.4) |
Previous IDs: | none |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Mifsud W |
Number in seed: | 53 |
Number in full: | 1659 |
Average length of the domain: | 329.1 aa |
Average identity of full alignment: | 45 % |
Average coverage of the sequence by the domain: | 59.47 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 393 | ||||||||||||
Family (HMM) version: | 18 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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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 PAD domain has been found. There are 55 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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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.