Summary: Protein kinase domain
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Protein kinase domain Edit Wikipedia article
| Protein kinase domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of the catalytic subunit of cAMP-dependent protein kinase.[1] | |||||||||
| Identifiers | |||||||||
| Symbol | Pkinase | ||||||||
| Pfam | PF00069 | ||||||||
| InterPro | IPR000719 | ||||||||
| SMART | TyrKc | ||||||||
| PROSITE | PDOC00100 | ||||||||
| SCOP2 | 1apm / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 186 | ||||||||
| CDD | cd00180 | ||||||||
| Membranome | 3 | ||||||||
| |||||||||
The protein kinase domain is a structurally conserved protein domain containing the catalytic function of protein kinases.[2][3][4] Protein kinases are a group of enzymes that move a phosphate group onto proteins, in a process called phosphorylation. This functions as an on/off switch for many cellular processes, including metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. They also function in embryonic development, physiological responses, and in the nervous and immune system. Abnormal phosphorylation causes many human diseases, including cancer, and drugs that affect phosphorylation can treat those diseases.[5]
Protein kinases possess a catalytic subunit which transfers the gamma phosphate from nucleoside triphosphates (almost always ATP) to the side chain of an amino acid in a protein, resulting in a conformational and/or dynamic changes affecting protein function. These enzymes fall into two broad classes, characterised with respect to substrate specificity: serine/threonine specific and tyrosine specific.[6]
Function
Protein kinase function has been evolutionarily conserved from Escherichia coli to Homo sapiens. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation.[7] Phosphorylation usually results in a functional change of the target protein by changing structure, dynamics, enzyme activity, cellular location, or association with other proteins.
Structure
The catalytic subunits of protein kinases are highly conserved, and the structures of over 270 of the approximately 500 human kinase domains have been determined,[8] leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases.[9]
Eukaryotic protein kinases[2][3][10][11] 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. The domain consists of two sub-domains referred to as the N- and C-terminal domains. The N-terminal domain consists of five beta sheet strands and an alpha helix called the C-helix, and the C-terminal domain usually consists of six alpha helices (labeled D, E, F, G, H, and I). The C-terminal domain contains two long loops, called the catalytic loop and the activation loop, which are essential for catalytic activity. The catalytic loop includes the "HRD motif" (for the amino acid sequence His-Arg-Asp), whose aspartic acid residue interacts directly with the hydroxyl group of the target serine, threonine, or tyrosine residue that is phosphorylated.[12]
The activation loop starts with the DFG motif (for the amino acid sequence Asp-Phe-Gly), which helps to bind ATP and magnesium in the active site. Broadly, the state or conformation of the kinase may be classified as DFGin or DFGout, depending on whether the Asp residue of the DFG motif is in or out of the active site. In the active form, the first few residues of the activation loop adopt a specific form of the DFGin conformation. Some inactive structures may adopt one of several other DFGin conformations, while other inactive structures are DFGout.[13]
Examples
The following is a list of human proteins containing the protein kinase domain:[14]
AAK1Â ; AATKÂ ; ABL1Â ; ABL2Â ; ACVR1Â ; ACVR1BÂ ; ACVR1CÂ ; ACVR2AÂ ; ACVR2BÂ ; ACVRL1Â ; AKT1Â ; AKT2Â ; AKT3Â ; ALKÂ ; AMHR2Â ; ANKK1Â ; ARAFÂ ; AURKAÂ ; AURKBÂ ; AURKCÂ ; AXLÂ ; BLKÂ ; BMP2KÂ ; BMPR1AÂ ; BMPR1BÂ ; BMPR2Â ; BMXÂ ; BRAFÂ ; BRSK1Â ; BRSK2Â ; BTKÂ ; BUB1Â ; BUB1BÂ ; CAMK1Â ; CAMK1DÂ ; CAMK1GÂ ; CAMK2AÂ ; CAMK2BÂ ; CAMK2DÂ ; CAMK2GÂ ; CAMK4Â ; CAMKK1Â ; CAMKK2Â ; CAMKVÂ ; CASKÂ ; CDC42BPAÂ ; CDC42BPBÂ ; CDC42BPGÂ ; CDC7Â ; CDK1Â ; CDK10Â ; CDK11AÂ ; CDK11BÂ ; CDK12Â ; CDK13Â ; CDK14Â ; CDK15Â ; CDK16Â ; CDK17Â ; CDK18Â ; CDK19Â ; CDK2Â ; CDK20Â ; CDK3Â ; CDK4Â ; CDK5Â ; CDK6Â ; CDK7Â ; CDK8Â ; CDK9Â ; CDKL1Â ; CDKL2Â ; CDKL3Â ; CDKL4Â ; CDKL5Â ; CHEK1Â ; CHEK2Â ; CHUKÂ ; CITÂ ; CLK1Â ; CLK2Â ; CLK3Â ; CLK4Â ; CSF1RÂ ; CSKÂ ; CSNK1A1Â ; CSNK1A1LÂ ; CSNK1DÂ ; CSNK1EÂ ; CSNK1G1Â ; CSNK1G2Â ; CSNK1G3Â ; CSNK2A1Â ; CSNK2A2Â ; CSNK2A3Â ; DAPK1Â ; DAPK2Â ; DAPK3Â ; DCLK1Â ; DCLK2Â ; DCLK3Â ; DDR1Â ; DDR2Â ; DMPKÂ ; DSTYKÂ ; DYRK1AÂ ; DYRK1BÂ ; DYRK2Â ; DYRK3Â ; DYRK4Â ; EGFRÂ ; EIF2AK1Â ; EIF2AK2Â ; EIF2AK3Â ; EIF2AK4Â ; EPHA1Â ; EPHA10Â ; EPHA2Â ; EPHA3Â ; EPHA4Â ; EPHA5Â ; EPHA6Â ; EPHA7Â ; EPHA8Â ; EPHB1Â ; EPHB2Â ; EPHB3Â ; EPHB4Â ; EPHB6Â ; ERBB2Â ; ERBB3Â ; ERBB4Â ; ERN1Â ; ERN2Â ; FERÂ ; FESÂ ; FGFR1Â ; FGFR2Â ; FGFR3Â ; FGFR4Â ; FGRÂ ; FLT1Â ; FLT3Â ; FLT4Â ; FRKÂ ; FYNÂ ; GAKÂ ; GRK1Â ; GRK2Â ; GRK3Â ; GRK4Â ; GRK5Â ; GRK6Â ; GRK7Â ; GSG2Â ; GSK3AÂ ; GSK3BÂ ; GUCY2CÂ ; GUCY2DÂ ; GUCY2FÂ ; HCKÂ ; HIPK1Â ; HIPK2Â ; HIPK3Â ; HIPK4Â ; HUNKÂ ; ICKÂ ; IGF1RÂ ; IKBKBÂ ; IKBKEÂ ; ILKÂ ; INSRÂ ; INSRRÂ ; IRAK1Â ; IRAK2Â ; IRAK3Â ; IRAK4Â ; ITKÂ ; JAK1Â ; JAK2Â ; JAK3Â ; KALRNÂ ; KDRÂ ; KITÂ ; KSR1Â ; KSR2Â ; LATS1Â ; LATS2Â ; LCKÂ ; LIMK1Â ; LIMK2Â ; LMTK2Â ; LMTK3Â ; LRRK1Â ; LRRK2Â ; LTKÂ ; LYNÂ ; MAKÂ ; MAP2K1Â ; MAP2K2Â ; MAP2K3Â ; MAP2K4Â ; MAP2K5Â ; MAP2K6Â ; MAP2K7Â ; MAP3K1Â ; MAP3K10Â ; MAP3K11Â ; MAP3K12Â ; MAP3K13Â ; MAP3K14Â ; MAP3K15Â ; MAP3K19Â ; MAP3K2Â ; MAP3K20Â ; MAP3K21Â ; MAP3K3Â ; MAP3K4Â ; MAP3K5Â ; MAP3K6Â ; MAP3K7Â ; MAP3K8Â ; MAP3K9Â ; MAP4K1Â ; MAP4K2Â ; MAP4K3Â ; MAP4K4Â ; MAP4K5Â ; MAPK1Â ; MAPK10Â ; MAPK11Â ; MAPK12Â ; MAPK13Â ; MAPK14Â ; MAPK15Â ; MAPK3Â ; MAPK4Â ; MAPK6Â ; MAPK7Â ; MAPK8Â ; MAPK9Â ; MAPKAPK2Â ; MAPKAPK3Â ; MAPKAPK5Â ; MARK1Â ; MARK2Â ; MARK3Â ; MARK4Â ; MAST1Â ; MAST2Â ; MAST3Â ; MAST4Â ; MASTLÂ ; MATKÂ ; MELKÂ ; MERTKÂ ; METÂ ; MINK1Â ; MKNK1Â ; MKNK2Â ; MLKLÂ ; MOKÂ ; MOSÂ ; MST1RÂ ; MUSKÂ ; MYLKÂ ; MYLK2Â ; MYLK3Â ; MYLK4Â ; MYO3AÂ ; MYO3BÂ ; NEK1Â ; NEK10Â ; NEK11Â ; NEK2Â ; NEK3Â ; NEK4Â ; NEK5Â ; NEK6Â ; NEK7Â ; NEK8Â ; NEK9Â ; NIM1KÂ ; NLKÂ ; NPR1Â ; NPR2Â ; NRBP1Â ; NRBP2Â ; NRKÂ ; NTRK1Â ; NTRK2Â ; NTRK3Â ; NUAK1Â ; NUAK2Â ; OBSCNÂ ; OXSR1Â ; PAK1Â ; PAK2Â ; PAK3Â ; PAK4Â ; PAK5Â ; PAK6Â ; PAN3Â ; PASKÂ ; PBKÂ ; PDGFRAÂ ; PDGFRBÂ ; PDIK1LÂ ; PDPK1Â ; PDPK2PÂ ; PEAK1Â ; PEAK3Â ; PHKG1Â ; PHKG2Â ; PIK3R4Â ; PIM1Â ; PIM2Â ; PIM3Â ; PINK1Â ; PKDCCÂ ; PKMYT1Â ; PKN1Â ; PKN2Â ; PKN3Â ; PLK1Â ; PLK2Â ; PLK3Â ; PLK4Â ; PLK5Â ; PNCKÂ ; POMKÂ ; PRKAA1Â ; PRKAA2Â ; PRKACAÂ ; PRKACBÂ ; PRKACGÂ ; PRKCAÂ ; PRKCBÂ ; PRKCDÂ ; PRKCEÂ ; PRKCGÂ ; PRKCHÂ ; PRKCIÂ ; PRKCQÂ ; PRKCZÂ ; PRKD1Â ; PRKD2Â ; PRKD3Â ; PRKG1Â ; PRKG2Â ; PRKXÂ ; PRKYÂ ; PRPF4BÂ ; PSKH1Â ; PSKH2Â ; PTK2Â ; PTK2BÂ ; PTK6Â ; PTK7Â ; PXKÂ ; RAF1Â ; RETÂ ; RIOK1Â ; RIOK2Â ; RIOK3Â ; RIPK1Â ; RIPK2Â ; RIPK3Â ; RIPK4Â ; RNASELÂ ; ROCK1Â ; ROCK2Â ; ROR1Â ; ROR2Â ; ROS1Â ; RPS6KA1Â ; RPS6KA2Â ; RPS6KA3Â ; RPS6KA4Â ; RPS6KA5Â ; RPS6KA6Â ; RPS6KB1Â ; RPS6KB2Â ; RPS6KC1Â ; RPS6KL1Â ; RSKRÂ ; RYKÂ ; SBK1Â ; SBK2Â ; SBK3Â ; SCYL1Â ; SCYL2Â ; SCYL3Â ; SGK1Â ; SGK2Â ; SGK223Â ; SGK3Â ; SIK1Â ; SIK1BÂ ; SIK2Â ; SIK3Â ; SLKÂ ; SNRKÂ ; SPEGÂ ; SRCÂ ; SRMSÂ ; SRPK1Â ; SRPK2Â ; SRPK3Â ; STK10Â ; STK11Â ; STK16Â ; STK17AÂ ; STK17BÂ ; STK24Â ; STK25Â ; STK26Â ; STK3Â ; STK31Â ; STK32AÂ ; STK32BÂ ; STK32CÂ ; STK33Â ; STK35Â ; STK36Â ; STK38Â ; STK38LÂ ; STK39Â ; STK4Â ; STK40Â ; STKLD1Â ; STRADAÂ ; STRADBÂ ; STYK1Â ; SYKÂ ; TAOK1Â ; TAOK2Â ; TAOK3Â ; TBCKÂ ; TBK1Â ; TECÂ ; TEKÂ ; TESK1Â ; TESK2Â ; TEX14Â ; TGFBR1Â ; TGFBR2Â ; TIE1Â ; TLK1Â ; TLK2Â ; TNIKÂ ; TNK1Â ; TNK2Â ; TNNI3KÂ ; TP53RKÂ ; TRIB1Â ; TRIB2Â ; TRIB3Â ; TRIOÂ ; TSSK1BÂ ; TSSK2Â ; TSSK3Â ; TSSK4Â ; TSSK6Â ; TTBK1Â ; TTBK2Â ; TTKÂ ; TTNÂ ; TXKÂ ; TYK2Â ; TYRO3Â ; UHMK1Â ; ULK1Â ; ULK2Â ; ULK3Â ; ULK4Â ; VRK1Â ; VRK2Â ; VRK3Â ; WEE1Â ; WEE2Â ; WNK1Â ; WNK2Â ; WNK3Â ; WNK4Â ; YES1Â ; ZAP70
References
- ^ Knighton DR, Bell SM, Zheng J, et al. (May 1993). "2.0 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with a peptide inhibitor and detergent". Acta Crystallogr. D. 49 (Pt 3): 357–61. doi:10.1107/S0907444993000502. PMID 15299526.
- ^ a b Hanks SK, Quinn AM (1991). "Protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members". Meth. Enzymol. Methods in Enzymology. 200: 38–62. doi:10.1016/0076-6879(91)00126-H. ISBN 978-0-12-182101-2. PMID 1956325.
- ^ a b Hanks SK, Hunter T (May 1995). "Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification". FASEB J. 9 (8): 576–96. doi:10.1096/fasebj.9.8.7768349. PMID 7768349. S2CID 21377422.
- ^ Scheeff ED, Bourne PE (October 2005). "Structural evolution of the protein kinase-like superfamily". PLOS Comput. Biol. 1 (5): e49. Bibcode:2005PLSCB...1...49S. doi:10.1371/journal.pcbi.0010049. PMCÂ 1261164. PMIDÂ 16244704.
- ^ Manning G, Whyte DB, Martinez R, Hunter T, Sudarsanam S (December 2002). "The Protein Kinase Complement of the Human Genome". Science. 298 (5600): 1912–1934. Bibcode:2002Sci...298.1912M. doi:10.1126/science.1075762. PMID 12471243. S2CID 26554314.
- ^ Hunter T, Hanks SK, Quinn AM (1988). "The protein kinase family: conserved features and deduced phylogeny of the catalytic domains". Science. 241 (4861): 42–51. Bibcode:1988Sci...241...42H. doi:10.1126/science.3291115. PMID 3291115.
- ^ Manning G, Plowman GD, Hunter T, Sudarsanam S (October 2002). "Evolution of protein kinase signaling from yeast to man". Trends Biochem. Sci. 27 (10): 514–20. doi:10.1016/S0968-0004(02)02179-5. PMID 12368087.
- ^ Modi, V; Dunbrack, RL (24 December 2019). "A Structurally-Validated Multiple Sequence Alignment of 497 Human Protein Kinase Domains". Scientific Reports. 9 (1): 19790. Bibcode:2019NatSR...919790M. doi:10.1038/s41598-019-56499-4. PMCÂ 6930252. PMIDÂ 31875044.
- ^ Li B, Liu Y, Uno T, Gray N (August 2004). "Creating chemical diversity to target protein kinases". Comb. Chem. High Throughput Screen. 7 (5): 453–72. doi:10.2174/1386207043328580. PMID 15320712. Archived from the original on 14 April 2013.
- ^ Hanks SK (2003). "Genomic analysis of the eukaryotic protein kinase superfamily: a perspective". Genome Biol. 4 (5): 111. doi:10.1186/gb-2003-4-5-111. PMCÂ 156577. PMIDÂ 12734000.
- ^ Hunter T (1991). "Protein kinase classification". Meth. Enzymol. Methods in Enzymology. 200: 3–37. doi:10.1016/0076-6879(91)00125-G. ISBN 978-0-12-182101-2. PMID 1835513.
- ^ Knighton DR, Zheng JH, Ten Eyck LF, Ashford VA, Xuong NH, Taylor SS, Sowadski JM (July 1991). "Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase". Science. 253 (5018): 407–14. Bibcode:1991Sci...253..407K. doi:10.1126/science.1862342. PMID 1862342.
- ^ Modi, V; Dunbrack, RL (2 April 2019). "Defining a new nomenclature for the structures of active and inactive kinases". Proceedings of the National Academy of Sciences of the United States of America. 116 (14): 6818–6827. doi:10.1073/pnas.1814279116. PMC 6452665. PMID 30867294.
- ^ "Human and mouse protein kinases: classification and index". pkinfam.txt. UniProt Consortium. Retrieved 10 June 2019.
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Protein kinase domain Provide feedback
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Literature references
-
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
-
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
-
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:3291115 , PUBMED:12734000 , PUBMED:7768349 , PUBMED:1835513 , PUBMED:1956325 ] 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 40 members:
ABC1 AceK_kinase Act-Frag_cataly Alpha_kinase APH APH_6_hur Choline_kinase CotH DUF1679 DUF2252 DUF4135 DUF5898 EcKL 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 TCAD9 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 and the UniProtKB 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 (38) |
Full (636438) |
Representative proteomes | UniProt (1154676) |
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|---|---|---|---|---|---|---|---|
| RP15 (112033) |
RP35 (280166) |
RP55 (517261) |
RP75 (703019) |
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| Jalview | |||||||
| HTML | |||||||
| PP/heatmap | 1 | ||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data 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 (636438) |
Representative proteomes | UniProt (1154676) |
||||
|---|---|---|---|---|---|---|---|
| RP15 (112033) |
RP35 (280166) |
RP55 (517261) |
RP75 (703019) |
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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 
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| Number in seed: | 38 |
| Number in full: | 636438 |
| Average length of the domain: | 241.40 aa |
| Average identity of full alignment: | 21 % |
| Average coverage of the sequence by the domain: | 36.71 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 264 | ||||||||||||
| Family (HMM) version: | 28 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Colour assignments
Archea
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Eukaryota
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Bacteria
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Other sequences
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Viruses
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Unclassified
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Viroids
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Unclassified sequence
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Selections
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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 Pkinase domain has been found. There are 6176 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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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.
