Summary: Cyclic-di-AMP receptor
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CdAMP is a family of bacterial cyclic-di-AMP receptor proteins. Cyclic-di-AMP (c-di-AMP) is a bacterial secondary messenger involved in various processes, including sensing of DNA-integrity, cell wall metabolism and potassium transport. CdAMP_rec has a ferredoxin-like fold and is structurally related to Pii-signal transduction proteins .
Internal database links
|Similarity to PfamA using HHSearch:||P-II|
This tab holds annotation information from the InterPro database.
InterPro entry IPR010375
CdAMP is a family of bacterial cyclic-di-AMP receptor proteins. Cyclic-di-AMP (c-di-AMP) is a bacterial secondary messenger involved in various processes, including sensing of DNA-integrity, cell wall metabolism and potassium transport. CdAMP_rec has a ferredoxin-like fold and is structurally related to Pii-signal transduction proteins [PUBMED:25435171].
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The members of this clan are characterised by the fact the domains, each comprised of four beta-strand and two alpha helices, tend to form tetrameric structures .
The clan contains the following 12 members:Amidase02_C CdAMP_rec CutA1 DUF190 DUF2007 DUF2179 DUF3240 HisG_C Nit_Regul_Hom NRho P-II Rhomboid_N
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Curation and family details
|Seed source:||Pfam-B_9915 (release 9.0)|
|Number in seed:||10|
|Number in full:||711|
|Average length of the domain:||105.90 aa|
|Average identity of full alignment:||45 %|
|Average coverage of the sequence by the domain:||97.39 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||10|
|Download:||download the raw HMM for this family|
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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 CdAMP_rec domain has been found. There are 16 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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