The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Protein-arginine deiminase, N-terminal domain
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.

Superfamily: Protein-arginine deiminase, N-terminal domain

Structural domains comprising this superfamily share the structure of the N-terminal, non-catalytic, domain of the protein-arginine deiminase (PAD), a calcium-dependent histone-modifying enzyme that uses a nucleophilic cysteine to hydrolyze guanidinium groups on arginine residues to form citrulline. This reaction, termed citrullination or deimination, results in the loss of positive charge, thereby affecting protein function and altering protein-protein and protein-nucleic acid interactions. PADs are dysregulated in inflammatory diseases and cancer PMID:25621824.

GO Diversity

Unique GO annotations
43 Unique GO terms

EC Diversity

Unique EC annotations
1 Unique EC terms

Species Diversity

Unique species annotations
180 Unique species

Sequence/Structure Diversity

Overview of the sequence / structure diversity of this superfamily compared to other superfamilies in CATH. Click on the chart to view the data in more detail.

Superfamily Summary

A general summary of information for this superfamily.
Structures
Domains: 40
Domain clusters (>95% seq id): 4
Domain clusters (>35% seq id): 3
Unique PDBs: 39
Alignments
Structural Clusters (5A): 1
Structural Clusters (9A): 1
FunFam Clusters: 13
Function
Unique EC: 1
Unique GO: 43
Taxonomy
Unique Species: 180