Summary: Microtubule-binding calmodulin-regulated spectrin-associated
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This is the Wikipedia entry entitled "Calmodulin-regulated spectrin-associated CKK domain". More...
Calmodulin-regulated spectrin-associated CKK domain Edit Wikipedia article
| solution structure of a murine hypothetical protein from riken cdna 2310057j16 | |||||||||
| Identifiers | |||||||||
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| Symbol | CAMSAP_CKK | ||||||||
| Pfam | PF08683 | ||||||||
| Pfam clan | CL0350 | ||||||||
| InterPro | IPR014797 | ||||||||
| SCOP | 1ugj | ||||||||
| SUPERFAMILY | 1ugj | ||||||||
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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. [1]
[edit] References
- ^ 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): 20052014. doi:10.1093/molbev/msp115. PMID 19508979.
This article incorporates text from the public domain Pfam and InterPro IPR014797
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
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.
Literature references
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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
| PANDIT: | PF08683 |
| Pseudofam: | PF08683 |
| SCOP: | 1ugj |
| SYSTERS: | CAMSAP_CKK |
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.
Gene Ontology
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) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan PRC-barrel (CL0350), which contains the following 3 members:
CAMSAP_CKK DUF2171 PRCAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (14) |
Full (287) |
Representative proteomes | NCBI (255) |
Meta (3) |
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| RP15 (44) |
RP35 (60) |
RP55 (101) |
RP75 (153) |
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| Jalview | ||||||||
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| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (14) |
Full (287) |
Representative proteomes | NCBI (255) |
Meta (3) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (44) |
RP35 (60) |
RP55 (101) |
RP75 (153) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | pdb_1ugj |
| Previous IDs: | DUF1781; CKK; |
| Type: | Domain |
| 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 information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 124 | ||||||||||||
| Family (HMM) version: | 6 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Structures
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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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence