SUPERFAMILY 1.73 HMM library and genome assignments server


cAMP-binding domain-like superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   All beta proteins [ 48724] (165)
Fold:   Double-stranded beta-helix [ 51181] (7)
  one turn of helix is made by two pairs of antiparallel strands linked with short turns
has appearance of a sandwich of distinct architecture and jelly-roll topology
Superfamily:   cAMP-binding domain-like [ 51206] (3)
Families:   CO-sensing protein CooA, N-terminal domain [ 51207]
  heme-binding domain
  Listeriolysin regulatory protein PrfA, N-terminal domain [ 89419]
  cAMP-binding domain [ 51210] (10)
  Pfam 00027


Superfamily statistics
Genomes (1,034) UniProt 15.0 PDB chains (SCOP 1.73)
Domains 13,180 10,661 29
Proteins 10,468 9,257 25


Functional annotation
General category Regulation
Detailed category Signal transduction

Function annotation of SCOP domain superfamilies
InterPro annotation
Cross references IPR000595 SSF51206 Protein matches
Abstract Proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues [PubMed14638413, PubMed10550204, PubMed1710853]. The best studied of these proteins is the prokaryotic catabolite gene activator (also known as the cAMP receptor protein) (gene crp) where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure. There are six invariant amino acids in this domain, three of which are glycine residues that are thought to be essential for maintenance of the structural integrity of the beta-barrel. cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain. The cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain. The cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section. Vertebrate cyclic nucleotide-gated ion-channels also contain this domain. Two such cations channels have been fully characterised, one is found in rod cells where it plays a role in visual signal transduction.

InterPro database

PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation ]

Internal database links

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level.


Alignments of sequences to 16 models in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.


Browse and view proteins in genomes which have different domain combinations including a cAMP-binding domain-like domain.


Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.


Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

There are 16 hidden Markov models representing the cAMP-binding domain-like superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.


Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Internal database links ]