Summary
Protein kinase domain
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
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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
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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
InterPro entry IPR017442
Protein kinases are a group of enzymes that possess a catalytic subunit which transfers 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. The enzymes fall into two broad classes, characterised with respect to substrate specificity: serine/threonine specific and tyrosine specific PUBMED:3291115.
Protein kinase function has been evolutionarily conserved from Escherichia coli to human. 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 includes protein kinases from eukaryotes and viruses and may include some bacterial hits too.Clan
This family is a member of clan PKinase (CL0016), which contains the following 17 members:
ABC1 APH APH_6_hur Choline_kinase DUF1679 DUF2252 DUF227 Fructosamin_kin Kdo Pkinase Pkinase_Tyr Pox_ser-thr_kin RIO1 Seadorna_VP7 UL97 WaaY YrbL-PhoP_regGene Ontology
| Molecular function | ATP binding (GO:0005524) |
| protein kinase activity (GO:0004672) | |
| Biological process | protein amino acid phosphorylation (GO:0006468) |
External database links
| HOMSTRAD: | kinase TyrKc |
| PANDIT: | PF00069 |
| PRINTS: | PR00109 |
| PROSITE: | PDOC00100 PDOC00212 PDOC00213 PDOC00629 |
| PROSITE profile: | PS50011 |
| SCOP: | 1apm |
| SMART: | STYKc S_TKc TyrKc |
| SYSTERS: | Pkinase |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
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 HMMER2.
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. 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 or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
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 |
| Author: | Sonnhammer ELL |
| Number in seed: | 54 |
| Number in full: | 51174 |
| Average length of the domain: | 238.20 aa |
| Average identity of full alignment: | 20 % |
| Average coverage of the sequence by the domain: | 38.93 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 260 | ||||||||||||
| Family (HMM) version: | 18 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Interactions
There are 21 interactions for this family. More...
Ank Pkinase cNMP_binding Cyclin_N FKBP_C Pkinase_C S1 RGS UBA PBD CKS CK_II_beta CDI Cyclin_C CDKN3 Ribonuc_2-5A I-set TGF_beta_GS Cyclin K-cyclin_vir_C Herp-CyclinStructures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD 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.
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