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C-terminal domain of adenylylcyclase associated protein superfamily
|General category ||Metabolism|
|Detailed category ||Other enzymes|
Document: Function annotation of SCOP domain superfamilies
Xenopus Anatomy (XA)(show details)
Highlighted in gray are those with FDR_all>0.001
Document: XA annotation of SCOP domains
|Cross references ||IPR013912 SSF69340 Protein matches|
Cyclase-associated protein (CAP) is a conserved two-domain protein that helps to activate the catalytic activity of adenylyl cyclase in the cyclase-bound state through interaction with Ras, which binds to the cyclase in a different region. With its other domain, CAP can bind monomeric actin and therefore also carries a cytoskeletal function. The protein is thus involved in Ras/cAMP-dependent signal transduction and most likely serves as an adapter protein translocating the adenylyl cyclase complex to the actin cytoskeleton. [1550959, 7962207].
Structurally, CAP is a protein of 474 to 551 residues. The N- and C-terminal domains of CAP are connected by an intermediate section which contains a proline-rich region. In the yeast protein, this domain has
been further divided into the P1 and P2 regions. While the P1 region is constituted by a 14 amino-acid sequence of unknown function, the P2 region exhibits a consensus SH3-binding motif (PXXP) and is necessary to target CAP to cortical actin patches. Dictyostelium CAP is a phosphatidylinositol 4,5-biphosphate (PIP2) regulated G-actin sequestering protein, which is present in the cytosol and shows enrichment at plasma-membrane regions. The cortical translocation is mediated by the N-terminal domain .
The CARP domain has been found as a tandem repeat in the C-terminal of many CAPs and also in the X-linked retinitis
pigmentosa 2 gene product.
PDBeMotif information about ligands, sequence and structure motifs
Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Xenopus Anatomy (XA) ]
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 3 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 C-terminal domain of adenylylcyclase associated protein 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 3 hidden Markov models representing the C-terminal domain of adenylylcyclase associated protein 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 · Xenopus Anatomy (XA) · Internal database links ]