Summary: Calcium/calmodulin dependent protein kinase II association domain
This is the Wikipedia entry entitled "Ca2+/calmodulin-dependent protein kinase". More...
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Calcium/calmodulin dependent protein kinase II association domain Provide feedback
This domain is found at the C-terminus of the Calcium/calmodulin dependent protein kinases II (CaMKII). These proteins also have a Ser/Thr protein kinase domain (PF00069) at their N-terminus . The function of the CaMKII association domain is the assembly of the single proteins into large (8 to 14 subunits) multimers .
Gangopadhyay SS, Barber AL, Gallant C, Grabarek Z, Smith JL, Morgan KG; , Biochem J 2003;372:347-357.: Differential functional properties of calmodulin-dependent protein kinase IIgamma variants isolated from smooth muscle. PUBMED:12603201 EPMC:12603201
Internal database links
|SCOOP:||DUF3225 DUF4440 NTF2 SnoaL SnoaL_2 SnoaL_3 SnoaL_4|
|Similarity to PfamA using HHSearch:||DUF3225 SnoaL_2 SnoaL_3 SnoaL_4 DUF4440|
This tab holds annotation information from the InterPro database.
InterPro entry IPR013543
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity [PUBMED:3291115]:
- Serine/threonine-protein kinases
- Tyrosine-protein kinases
- Dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)
Protein kinase function is evolutionarily conserved from Escherichia coli to human [PUBMED:12471243]. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation [PUBMED:12368087]. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [PUBMED:15078142], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [PUBMED:15320712].
This domain is found at the C terminus of the Calcium/calmodulin dependent protein kinases II (CaMKII). These proteins also have a Ser/Thr protein kinase domain (INTERPRO) at their N terminus [PUBMED:12603201]. The function of the CaMKII association domain is the assembly of the single proteins into large (8 to 14 subunits) multimers [PUBMED:14993460] and is a prominent kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||calmodulin-dependent protein kinase activity (GO:0004683)|
|calmodulin binding (GO:0005516)|
|Biological process||protein phosphorylation (GO:0006468)|
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This superfamily contains a variety of enzymes such as Scytalone dehydratase, Delta-5-3-ketosteroid isomerase, Limonene-1,2-epoxide hydrolase among others. The family also includes presumed non-enzymatic homologues such as NTF2.
The clan contains the following 38 members:CaMKII_AD DUF1348 DUF2358 DUF3225 DUF3804 DUF3828 DUF3887 DUF4348 DUF4440 DUF4467 DUF4518 DUF4783 DUF4829 DUF4864 DUF4878 DUF4904 DUF5104 DUF5105 Endopep_inhib LEH Lumazine_bd_2 MBA1 MecA_N MlaC Mtr2 NTF2 PHZA_PHZB Ring_hydroxyl_B Scytalone_dh SnoaL SnoaL_2 SnoaL_3 SnoaL_4 T4BSS_DotI_IcmL Tim44 TpcC VirB8 WI12
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the UniProtKB sequence database using the family HMM
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
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Curation and family details
|Seed source:||Pfam-B_1025 (release 18.0)|
|Number in seed:||5|
|Number in full:||941|
|Average length of the domain:||120.60 aa|
|Average identity of full alignment:||49 %|
|Average coverage of the sequence by the domain:||31.47 %|
|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:||9|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 CaMKII_AD domain has been found. There are 65 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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