Summary: Protein-arginine deiminase (PAD) N-terminal domain
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Protein-arginine deiminase (PAD) N-terminal domain Provide feedback
This family represents the N-terminal non-catalytic domain of protein-arginine deiminase. This domain has a cupredoxin-like fold.
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
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
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
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR013732
This entry represents the N-terminal non-catalytic domain of protein-arginine deiminase. This domain has a cupredoxin-like fold.
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)|
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This example describes an architecture with one
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Curation and family details
|Seed source:||Pfam-B_2195 (release 6.4)|
|Author:||Mifsud W, Bateman A|
|Number in seed:||15|
|Number in full:||190|
|Average length of the domain:||106.60 aa|
|Average identity of full alignment:||38 %|
|Average coverage of the sequence by the domain:||17.47 %|
|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:||5|
|Download:||download the raw HMM for this family|
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There are 2 interactions 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 PAD_N domain has been found. There are 12 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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