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47  structures 2865  species 0  interactions 4271  sequences 32  architectures

Family: PAD_porph (PF04371)

Summary: Porphyromonas-type peptidyl-arginine deiminase

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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.

Porphyromonas-type peptidyl-arginine deiminase Provide feedback

Peptidyl-arginine deiminase (PAD) enzymes catalyse the deimination of the guanidino group from carboxy-terminal arginine residues of various peptides to produce ammonia. PAD from Porphyromonas gingivalis (PPAD) appears to be evolutionarily unrelated to mammalian PAD (PF03068), which is a metalloenzyme. PPAD is thought to belong to the same superfamily as aminotransferase and arginine deiminase, and to form an alpha/beta propeller structure. This family has previously been named PPADH (Porphyromonas peptidyl-arginine deiminase homologues) [1]. The predicted catalytic residues in PPAD (Q9RQJ2) are Asp130, Asp187, His236, Asp238 and Cys351 [1]. These are absolutely conserved with the exception of Asp187 which is absent in two family members. PPAD is also able to catalyse the deimination of free L-arginine, but has primarily peptidyl-arginine specificity. It may have a FMN cofactor [2].

Literature references

  1. Shirai H, Blundell TL, Mizuguchi K; , Trends Biochem Sci 2001;26:465-468.: A novel superfamily of enzymes that catalyze the modification of guanidino groups. PUBMED:11504612 EPMC:11504612

  2. McGraw WT, Potempa J, Farley D, Travis J; , Infect Immun 1999;67:3248-3256.: Purification, characterization, and sequence analysis of a potential virulence factor from Porphyromonas gingivalis, peptidylarginine deiminase. PUBMED:10377098 EPMC:10377098


Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR007466

Peptidyl-arginine deiminase (PAD) enzymes catalyse the deimination of the guanidino group from carboxy-terminal arginine residues of various peptides to produce ammonia. PAD from Porphyromonas gingivalis (Bacteroides gingivalis) (PPAD) appears to be evolutionarily unrelated to mammalian PAD ( INTERPRO ), which is a metalloenzyme. PPAD is thought to belong to the same superfamily as aminotransferase and arginine deiminase, and to form an alpha/beta propeller structure. This family has previously been named PPADH (Porphyromonas peptidyl-arginine deiminase homologues) [ PUBMED:11504612 ]. The predicted catalytic residues in PPAD ( SWISSPROT ) are Asp130, Asp187, His236, Asp238 and Cys351 [ PUBMED:11504612 ]. These are absolutely conserved with the exception of Asp187 which is absent in two family members. PPAD is also able to catalyse the deimination of free L-arginine, but has primarily peptidyl-arginine specificity. It may have a FMN cofactor [ PUBMED:10377098 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

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_porph

Alignments

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
(359)
Full
(4271)
Representative proteomes UniProt
(21967)
RP15
(507)
RP35
(1903)
RP55
(4241)
RP75
(7660)
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HTML View  View           
PP/heatmap 1 View           

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(359)
Full
(4271)
Representative proteomes UniProt
(21967)
RP15
(507)
RP35
(1903)
RP55
(4241)
RP75
(7660)
Alignment:
Format:
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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
(359)
Full
(4271)
Representative proteomes UniProt
(21967)
RP15
(507)
RP35
(1903)
RP55
(4241)
RP75
(7660)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

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 View help on the curation process

Seed source: COG2957
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Kerrison ND
Number in seed: 359
Number in full: 4271
Average length of the domain: 322.6 aa
Average identity of full alignment: 32 %
Average coverage of the sequence by the domain: 92.05 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 25.2 25.4
Noise cut-off 24.5 24.6
Model length: 319
Family (HMM) version: 18
Download: download the raw HMM for this family

Species distribution

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Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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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_porph domain has been found. There are 47 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.

Protein Predicted structure External Information
A0A044VH89 View 3D Structure Click here
A0A0D2GZ52 View 3D Structure Click here
A0A1C1C7M6 View 3D Structure Click here
A0A1D6J8B5 View 3D Structure Click here
A4VFL7 View 3D Structure Click here
A4XP44 View 3D Structure Click here
B7FA89 View 3D Structure Click here
C3K5U8 View 3D Structure Click here
G7JT50 View 3D Structure Click here
I1MTB1 View 3D Structure Click here
K0EGS5 View 3D Structure Click here
K0EQ78 View 3D Structure Click here
K0EY57 View 3D Structure Click here
O24890 View 3D Structure Click here
O86509 View 3D Structure Click here
Q083U9 View 3D Structure Click here
Q0P9V0 View 3D Structure Click here
Q4KJX9 View 3D Structure Click here
Q5ZZK4 View 3D Structure Click here
Q6CZ80 View 3D Structure Click here
Q6LG16 View 3D Structure Click here
Q6MSR8 View 3D Structure Click here
Q82JP0 View 3D Structure Click here
Q837U5 View 3D Structure Click here
Q87NU5 View 3D Structure Click here
Q87UB2 View 3D Structure Click here
Q88R68 View 3D Structure Click here
Q8DQ68 View 3D Structure Click here
Q8DW17 View 3D Structure Click here
Q8EIF2 View 3D Structure Click here
Q8GWW7 View 3D Structure Click here
Q8RPX2 View 3D Structure Click here
Q8YAS3 View 3D Structure Click here
Q8YAS5 View 3D Structure Click here
Q8ZHG0 View 3D Structure Click here
Q9CEY6 View 3D Structure Click here
Q9I6J9 View 3D Structure Click here
Q9RQJ2 View 3D Structure Click here