Summary: Microtubule-binding calmodulin-regulated spectrin-associated
This is the Wikipedia entry entitled "Calmodulin-regulated spectrin-associated CKK domain". More...
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Calmodulin-regulated spectrin-associated CKK domain Edit Wikipedia article
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solution structure of a murine hypothetical protein from riken cdna 2310057j16
In molecular biology, the calmodulin-regulated spectrin-associated CKK domain (also known as the CKK domain) is a domain which occurs at the C-terminus of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal. This domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a this domain in murine hypothetical protein has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin.
- Baines, A. J.; Bignone, P. A.; King, M. D. A.; Maggs, A. M.; Bennett, P. M.; Pinder, J. C.; Phillips, G. W. (2009). "The CKK Domain (DUF1781) Binds Microtubules and Defines the CAMSAP/ssp4 Family of Animal Proteins". Molecular Biology and Evolution 26 (9): 2005–2014. doi:10.1093/molbev/msp115. PMID 19508979.
Microtubule-binding calmodulin-regulated spectrin-associated Provide feedback
This is the C-terminal domain of a family of eumetazoan proteins collectively defined as calmodulin-regulated spectrin-associated, or CAMSAP, proteins. CAMSAP proteins carry an N-terminal region that includes the CH domain, a central region including a predicted coiled-coil and this C-terminal, or CKK, domain - defined as being present in CAMSAP, KIAA1078 and KIAA1543, The C-terminal domain is the part of the CAMSAP proteins that binds to microtubules. The domain appears to act by producing inhibition of neurite extension, probably by blocking microtubule function. CKK represents a domain that has evolved with the metazoa. The structure of a murine hypothetical protein from RIKEN cDNA has shown the domain to adopt a mainly beta barrel structure with an associated alpha-helical hairpin.
Baines AJ, Bignone PA, King MD, Maggs AM, Bennett PM, Pinder JC, Phillips GW;, Mol Biol Evol. 2009 Jun 9. [Epub ahead of print]: The CKK domain (DUF1781) domain binds microtubules and defines the CAMSAP/ssp4 family of animal proteins. PUBMED:19508979 EPMC:19508979
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR014797
The CKK domain occurs at the C terminus of a family of proteins collectively defined as calmodulin-regulated spectrin-associated (or CAMSAP) proteins. CAMSAP proteins carry an N-terminal region that includes a CH domain, a central region including a predicted coiled-coil, and this C-terminal CKK domain which is involved in binding CAMSAP proteins to microtubules [PUBMED:19508979].
The structure of the CKK domain is a beta-barrel with an associated alpha-helical hairpin. Characteristically, the CKK domain has a single invariant tryptophan residue within the core of the predicted beta-barrel. Residues that interact with this Trp to form part of this core are highly conserved too.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||microtubule binding (GO:0008017)|
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This example describes an architecture with one
Gladomain, followed by two consecutive
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Curation and family details
|Previous IDs:||DUF1781; CKK;|
|Author:||Mistry J, Baines A|
|Number in seed:||14|
|Number in full:||287|
|Average length of the domain:||125.80 aa|
|Average identity of full alignment:||57 %|
|Average coverage of the sequence by the domain:||10.32 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
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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 CAMSAP_CKK domain has been found. There are 1 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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