Summary: Protein kinase domain
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This is the Wikipedia entry entitled "Protein kinase domain". More...
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Protein kinase domain Provide feedback
No Pfam abstract.
Literature references
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Hanks SK, Quinn AM; , Methods Enzymol 1991;200:38-62.: Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. PUBMED:1956325 EPMC:1956325
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Hanks SK, Hunter T; , FASEB J 1995;9:576-596.: Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. PUBMED:7768349 EPMC:7768349
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Hunter T, Plowman GD; , Trends Biochem Sci 1997;22:18-22.: The protein kinases of budding yeast: six score and more. PUBMED:9020587 EPMC:9020587
Internal database links
External database links
HOMSTRAD: | kinase TyrKc |
PRINTS: | PR00109 |
PROSITE: | PDOC00100 PDOC00212 PDOC00213 PDOC00629 |
PROSITE profile: | PS50011 |
SCOP: | 1apm |
SMART: | STYKc S_TKc TyrKc |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000719
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].
Eukaryotic protein kinases [PUBMED:12734000, PUBMED:7768349, PUBMED:1835513, PUBMED:1956325, PUBMED:3291115] are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. There are a number of conserved regions in the catalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is a glycine-rich stretch of residues in the vicinity of a lysine residue, which has been shown to be involved in ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residue which is important for the catalytic activity of the enzyme [PUBMED:1862342].
This entry represents the protein kinase domain containing the catalytic function of protein kinases [PUBMED:1956325]. This domain is found in serine/threonine-protein kinases, tyrosine-protein kinases and dual specificity protein kinases.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | ATP binding (GO:0005524) |
protein kinase activity (GO:0004672) | |
Biological process | protein phosphorylation (GO:0006468) |
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 PKinase (CL0016), which has the following description:
This superfamily includes the Serine/Threonine- and Tyrosine- protein kinases as well as related kinases that act on non-protein substrates.
The clan contains the following 38 members:
ABC1 AceK Act-Frag_cataly Alpha_kinase APH APH_6_hur Choline_kinase CotH DUF1679 DUF2252 DUF4135 EcKinase Fam20C Fructosamin_kin FTA2 Haspin_kinase HipA_C Ins_P5_2-kin IPK IucA_IucC Kdo Kinase-like Kinase-PolyVal KIND Pan3_PK PI3_PI4_kinase PIP49_C PIP5K PK_Tyr_Ser-Thr Pkinase Pkinase_fungal Pox_ser-thr_kin RIO1 Seadorna_VP7 UL97 WaaY YrbL-PhoP_reg YukCAlignments
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 (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...
View options
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 (38) |
Full (424548) |
Representative proteomes | UniProt (795002) |
NCBI (1410719) |
Meta (4445) |
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RP15 (64507) |
RP35 (190240) |
RP55 (328341) |
RP75 (462263) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
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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 (38) |
Full (424548) |
Representative proteomes | UniProt (795002) |
NCBI (1410719) |
Meta (4445) |
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---|---|---|---|---|---|---|---|---|---|
RP15 (64507) |
RP35 (190240) |
RP55 (328341) |
RP75 (462263) |
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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.
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: | Unknown |
Previous IDs: | pkinase; |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Sonnhammer ELL |
Number in seed: | 38 |
Number in full: | 424548 |
Average length of the domain: | 242.40 aa |
Average identity of full alignment: | 21 % |
Average coverage of the sequence by the domain: | 37.99 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 264 | ||||||||||||
Family (HMM) version: | 26 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Colour assignments
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Selections
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
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Interactions
There are 73 interactions for this family. More...
TsaD FHA PK_Tyr_Ser-Thr PKI fn3 TGF_beta_GS TGF_beta_GS PBD CDKN3 CK1gamma_C CKS CagA cNMP_binding Pkinase_C C1_1 CaM-KIIN S1 Ribonuc_2-5A TsaD Mo25 EF-hand_6 PBD INCENP_ARK-bind Pkinase_C EF-hand_7 GSK-3_bind SAM_1 Ank_2 Cyclin FKBP_C RGS DED Cyclin_C CaMKII_AD CaM-KIIN Herp-Cyclin RIIa CGI-121 EF-hand_8 K-cyclin_vir_C CDI POLO_box UBA_2 Rhodanese cNMP_binding I-set Ras PB1 Ank Cyclin_N PH RRM_1 Ribonuc_2-5A CK_II_beta CK_II_beta Aurora-A_bind EF-hand_1 EF-hand_5 Cyclin_C FHA Haspin_kinase FKBP_C Cyclin_N Ank_4 Tat PP2C CDK5_activator Cyclin PKI Pkinase Phospholamban zf-DBF AMPKBIStructures
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 Pkinase domain has been found. There are 5366 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 sequence.
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