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Conserved domains on  [gi|442620344|ref|NP_001262811|]
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CASK, isoform H [Drosophila melanogaster]

Protein Classification

peripheral plasma membrane protein CASK( domain architecture ID 11602698)

peripheral plasma membrane protein CASK (calcium/calmodulin-dependent serine protein kinase) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and also functions as an adaptor protein through its multiple protein-protein interaction modules, PDZ, SH3, and inactive guanylate kinase (GuK) domains

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
8-308 0e+00

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 586.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGML 87
Cdd:cd14094    1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGML 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLCFEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSAI 167
Cdd:cd14094   81 YMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLPGTreTIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWKSI 247
Cdd:cd14094  161 QLGES--GLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHI 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 248 SANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRD-KLQRTHLADTVEELKRYNARRKLKGA 308
Cdd:cd14094  239 SESAKDLVRRMLMLDPAERITVYEALNHPWIKERDrYAYRIHLPETVEQLRKFNARRKLKGA 300
Guanylate_kin pfam00625
Guanylate kinase;
710-883 1.04e-68

Guanylate kinase;


:

Pssm-ID: 395500  Cd Length: 182  Bit Score: 226.49  E-value: 1.04e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  710 QRKTLVLLGAHGVGRRHIKNTLISKYPDKYAYPIPHTTRPAKPEEENGRSYYFVSHDEMMADIGANEYLEYGTHEDAMYG 789
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  790 TKLDTIRRIHTEGKMAILDVEPQALKILRTAEFTPYVVFIAAPSLQ-----NIADYDGSLERLAKESEMLRQLYGHF-FD 863
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKvlqrrLKGRGKEQEEKINKRMAAAEQEFQHYeFD 160
                         170       180
                  ....*....|....*....|
gi 442620344  864 LTIVNNDISETIATLETAID 883
Cdd:pfam00625 161 VIIVNDDLEEAYKKLKEALE 180
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
494-574 8.96e-55

PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CASK, Caenorhabditis elegans Lin-2, and related domains. CASK and Lin-2 are membrane-associated guanylate kinase (MAGUK)-like proteins. CASK (also known as Calcium/calmodulin-dependent protein kinase, CAKI, and Camguk) has a role in synaptic transmembrane protein anchoring and ion channel trafficking. CASK may regulate transmembrane proteins that bind calcium, calmodulin, or nucleotides; it regulates the Drosophila ether a go-go (eag) potassium channel, and also regulates autophosphorylation of CaMKII. CASK binding partners include the transcription factor TBR1, and cell-surface proteins, including amyloid precursor protein, neurexins, and syndecans. Lin-2, as a component of the CLin-10-Lin-2-Lin-7 complex, plays a role in controlling the basolateral localization of the EGF receptor Let-23; this complex also associates with the neuron-specific motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor 2B along microtubules. CASK may also function in targeting or scaffolding of the protein parkin which is selectively truncated by a Parkinson's disease-causing mutation; the C-terminus of parkin functions as a class II PDZ-binding motif that binds CASK. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP6-MPP2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


:

Pssm-ID: 467267 [Multi-domain]  Cd Length: 81  Bit Score: 183.84  E-value: 8.96e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 494 RLVQFQKNTDEPMGITLKMTEDGRCIVARIMHGGMIHRQATLHVGDEIREINGQPVQHQSVGQLQRMLREARGSVTFKIV 573
Cdd:cd10831    1 RLVQFQKNTDEPMGITLKMNEDGRCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREARGSITFKIV 80

                 .
gi 442620344 574 P 574
Cdd:cd10831   81 P 81
SH3_CASK cd12081
Src Homology 3 domain of Calcium/calmodulin-dependent Serine protein Kinase; CASK is a ...
586-646 4.54e-37

Src Homology 3 domain of Calcium/calmodulin-dependent Serine protein Kinase; CASK is a scaffolding protein that is highly expressed in the mammalian nervous system and plays roles in synaptic protein targeting, neural development, and gene expression regulation. CASK interacts with many different binding partners including parkin, neurexin, syndecans, calcium channel proteins, caskin, among others, to perform specific functions in different subcellular locations. Disruption of the CASK gene in mice results in neonatal lethality while mutations in the human gene have been associated with X-linked mental retardation. Drosophila CASK is associated with both pre- and postsynaptic membranes and is crucial in synaptic transmission and vesicle cycling. CASK contains an N-terminal calmodulin-dependent kinase (CaMK)-like domain, two L27 domains, followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


:

Pssm-ID: 213014  Cd Length: 62  Bit Score: 133.10  E-value: 4.54e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 586 FVRAQFDYNPLDDELIPCAQAGISFQVGDILQIISKDDHHWWQARLDT-VGGSAGLIPSPEL 646
Cdd:cd12081    1 YVRAQFEYDPLKDDLIPCKQAGIRFRVGDILQIISKDDHNWWQAKLENsKNGTAGLIPSPEL 62
L27 pfam02828
L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.
347-396 4.76e-10

L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.


:

Pssm-ID: 460717  Cd Length: 52  Bit Score: 55.89  E-value: 4.76e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 442620344  347 VQRILDCLDDIYSLQDAHVDADVLRDMLRDNRLHQFLQLFDRIAATVVTS 396
Cdd:pfam02828   1 VELVLELLEDLQPLSEASEDLAELQKLLQSPHLQALLEAHDKVAQKVYEP 50
L27 pfam02828
L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.
406-462 2.42e-09

L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.


:

Pssm-ID: 460717  Cd Length: 52  Bit Score: 53.58  E-value: 2.42e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344  406 VGRCRDVLEQLSSTSGGNSlggkyAKEELMRLLAAPHMQALLHSHDVVARDVYGEEA 462
Cdd:pfam02828   1 VELVLELLEDLQPLSEASE-----DLAELQKLLQSPHLQALLEAHDKVAQKVYEPPS 52
 
Name Accession Description Interval E-value
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
8-308 0e+00

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 586.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGML 87
Cdd:cd14094    1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGML 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLCFEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSAI 167
Cdd:cd14094   81 YMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLPGTreTIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWKSI 247
Cdd:cd14094  161 QLGES--GLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHI 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 248 SANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRD-KLQRTHLADTVEELKRYNARRKLKGA 308
Cdd:cd14094  239 SESAKDLVRRMLMLDPAERITVYEALNHPWIKERDrYAYRIHLPETVEQLRKFNARRKLKGA 300
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-278 6.09e-82

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 264.78  E-value: 6.09e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344    12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPglstADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDR----ERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344    92 EFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLpg 171
Cdd:smart00220  77 EYCEGGDL-FDLLKKRGR---LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL---DEDGHVKLADFGLARQL-- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   172 tRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG--VRLQQSVARGRLSFEAPEWKsISA 249
Cdd:smart00220 148 -DPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDqlLELFKKIGKPKPPFPPPEWD-ISP 225
                          250       260
                   ....*....|....*....|....*....
gi 442620344   250 NAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:smart00220 226 EAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
Guanylate_kin pfam00625
Guanylate kinase;
710-883 1.04e-68

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 226.49  E-value: 1.04e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  710 QRKTLVLLGAHGVGRRHIKNTLISKYPDKYAYPIPHTTRPAKPEEENGRSYYFVSHDEMMADIGANEYLEYGTHEDAMYG 789
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  790 TKLDTIRRIHTEGKMAILDVEPQALKILRTAEFTPYVVFIAAPSLQ-----NIADYDGSLERLAKESEMLRQLYGHF-FD 863
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKvlqrrLKGRGKEQEEKINKRMAAAEQEFQHYeFD 160
                         170       180
                  ....*....|....*....|
gi 442620344  864 LTIVNNDISETIATLETAID 883
Cdd:pfam00625 161 VIIVNDDLEEAYKKLKEALE 180
Pkinase pfam00069
Protein kinase domain;
12-278 3.71e-56

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 192.84  E-value: 3.71e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKK---KDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   92 EFMEGSDLcFEVVRRavaGFVYSEAVACHYMRQILEALRYCHEndilhrdvrpacallatvdnsapvklggfgsaiqlpg 171
Cdd:pfam00069  78 EYVEGGSL-FDLLSE---KGAFSEREAKFIMKQILEGLESGSS------------------------------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  172 tretieTHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWKSISANA 251
Cdd:pfam00069 117 ------LTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLSEEA 190
                         250       260
                  ....*....|....*....|....*..
gi 442620344  252 KDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:pfam00069 191 KDLLKKLLKKDPSKRLTATQALQHPWF 217
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
494-574 8.96e-55

PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CASK, Caenorhabditis elegans Lin-2, and related domains. CASK and Lin-2 are membrane-associated guanylate kinase (MAGUK)-like proteins. CASK (also known as Calcium/calmodulin-dependent protein kinase, CAKI, and Camguk) has a role in synaptic transmembrane protein anchoring and ion channel trafficking. CASK may regulate transmembrane proteins that bind calcium, calmodulin, or nucleotides; it regulates the Drosophila ether a go-go (eag) potassium channel, and also regulates autophosphorylation of CaMKII. CASK binding partners include the transcription factor TBR1, and cell-surface proteins, including amyloid precursor protein, neurexins, and syndecans. Lin-2, as a component of the CLin-10-Lin-2-Lin-7 complex, plays a role in controlling the basolateral localization of the EGF receptor Let-23; this complex also associates with the neuron-specific motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor 2B along microtubules. CASK may also function in targeting or scaffolding of the protein parkin which is selectively truncated by a Parkinson's disease-causing mutation; the C-terminus of parkin functions as a class II PDZ-binding motif that binds CASK. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP6-MPP2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467267 [Multi-domain]  Cd Length: 81  Bit Score: 183.84  E-value: 8.96e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 494 RLVQFQKNTDEPMGITLKMTEDGRCIVARIMHGGMIHRQATLHVGDEIREINGQPVQHQSVGQLQRMLREARGSVTFKIV 573
Cdd:cd10831    1 RLVQFQKNTDEPMGITLKMNEDGRCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREARGSITFKIV 80

                 .
gi 442620344 574 P 574
Cdd:cd10831   81 P 81
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
720-883 4.92e-54

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 185.57  E-value: 4.92e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   720 HGVGRRHIKNTLISKYPDKYAYPIPHTTRPAKPEEENGRSYYFVSHDEMMADIGANEYLEYGTHEDAMYGTKLDTIRRIH 799
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   800 TEGKMAILDVEPQALKILRTAEFTPYVVFIAAPSLQNIAD-----YDGSLERLAKESEMLRQLYG--HFFDLTIVNNDIS 872
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERrlrqrGTETSERIQKRLAAAQKEAQeyHLFDYVIVNDDLE 160
                          170
                   ....*....|.
gi 442620344   873 ETIATLETAID 883
Cdd:smart00072 161 DAYEELKEILE 171
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
12-496 5.69e-47

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 175.59  E-value: 5.69e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvAKFTASPGLStADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLR-PELAADPEAR-ERFRREARALARLNHPNIVRVYDVGEEDGRPYLVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCfEVVRRavaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLPG 171
Cdd:COG0515   87 EYVEGESLA-DLLRR---RGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANIL---LTPDGRVKLIDFGIARALGG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETiETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEWKSISAN 250
Cdd:COG0515  160 ATLT-QTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGdSPAELLRAHLREPPPPPSELRPDLPPA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 251 AKDLVMKMLAANPHHRL-SITEVLDHpwirdrdkLQRTHLADTVEELKRYNARRKLKGAVQAIAGGTNMDPLYATDADMP 329
Cdd:COG0515  239 LDAIVLRALAKDPEERYqSAAELAAA--------LRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 330 ITGATDEWADEEAGIEAVQRILDCLDDIYSLQDAHVDADVLRDMLRDNRLHQFLQLFDRIAATVVTsnGRAPAAEAVGRC 409
Cdd:COG0515  311 AAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAA--AAAAAAAALAAA 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 410 RDVLEQLSSTSGGNSLGGKYAKEELMRLLAAPHMQALLHSHDVVARDVYGEEALRVTPPPMVPYLNGDELDNVEGGELQH 489
Cdd:COG0515  389 AAAAAAAAAAALAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAA 468

                 ....*..
gi 442620344 490 VTRVRLV 496
Cdd:COG0515  469 ALAAAAA 475
SH3_CASK cd12081
Src Homology 3 domain of Calcium/calmodulin-dependent Serine protein Kinase; CASK is a ...
586-646 4.54e-37

Src Homology 3 domain of Calcium/calmodulin-dependent Serine protein Kinase; CASK is a scaffolding protein that is highly expressed in the mammalian nervous system and plays roles in synaptic protein targeting, neural development, and gene expression regulation. CASK interacts with many different binding partners including parkin, neurexin, syndecans, calcium channel proteins, caskin, among others, to perform specific functions in different subcellular locations. Disruption of the CASK gene in mice results in neonatal lethality while mutations in the human gene have been associated with X-linked mental retardation. Drosophila CASK is associated with both pre- and postsynaptic membranes and is crucial in synaptic transmission and vesicle cycling. CASK contains an N-terminal calmodulin-dependent kinase (CaMK)-like domain, two L27 domains, followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 213014  Cd Length: 62  Bit Score: 133.10  E-value: 4.54e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 586 FVRAQFDYNPLDDELIPCAQAGISFQVGDILQIISKDDHHWWQARLDT-VGGSAGLIPSPEL 646
Cdd:cd12081    1 YVRAQFEYDPLKDDLIPCKQAGIRFRVGDILQIISKDDHNWWQAKLENsKNGTAGLIPSPEL 62
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
12-284 3.70e-33

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 131.09  E-value: 3.70e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIV---DVAKFTaspglSTADLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLkkrEILKMK-----QVQHVAQEKSILMELSHPFIVNMMCSFQDENRVY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAiq 168
Cdd:PTZ00263  95 FLLEFVVGGEL-FTHLRKAGR---FPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLL---DNKGHVKVTDFGFA-- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 lpgTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFeaPEWksI 247
Cdd:PTZ00263 166 ---KKVPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDdTPFRIYEKILAGRLKF--PNW--F 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 442620344 248 SANAKDLVMKMLAANPHHRL-----SITEVLDHPWIR--DRDKL 284
Cdd:PTZ00263 239 DGRARDLVKGLLQTDHTKRLgtlkgGVADVKNHPYFHgaNWDKL 282
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
714-879 1.99e-26

Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.


Pssm-ID: 238026  Cd Length: 137  Bit Score: 105.31  E-value: 1.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 714 LVLLGAHGVGRRHIKNTLISKYPDKYAYPIPHTTRPAKPEEENGRSYYFVSHDEMMADIGANEYLEYGTHEDAMYGTKLD 793
Cdd:cd00071    2 IVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSKA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 794 TIRRIHTEGKMAILDVEPQALKILRTAEFTPYVVFIAAPslqniadydgslerlakesemlrqlyghffDLTIVNNDISE 873
Cdd:cd00071   82 AVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP------------------------------DYVIVNDDLEK 131

                 ....*.
gi 442620344 874 TIATLE 879
Cdd:cd00071  132 AYEELK 137
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
714-882 4.20e-25

guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 213788  Cd Length: 179  Bit Score: 102.96  E-value: 4.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  714 LVLLGAHGVGrrhiKNTLIS---KYPDKYAYPIPHTTRPAKPEEENGRSYYFVSHDEMMADIGANEYLEYGTHEDAMYGT 790
Cdd:TIGR03263   3 IVISGPSGAG----KSTLVKallEEDPNLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  791 KLDTIRRIHTEGKMAILDVEPQ-ALKILRTaeFTPYV-VFIAAPSLQNIA--------DYDGSLE-RLAK-ESEMlrqLY 858
Cdd:TIGR03263  79 PKSPVEEALAAGKDVLLEIDVQgARQVKKK--FPDAVsIFILPPSLEELErrlrkrgtDSEEVIErRLAKaKKEI---AH 153
                         170       180
                  ....*....|....*....|....
gi 442620344  859 GHFFDLTIVNNDISETIATLETAI 882
Cdd:TIGR03263 154 ADEFDYVIVNDDLEKAVEELKSII 177
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
714-882 1.21e-24

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 102.07  E-value: 1.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 714 LVLLGAHGVGRRHIKNTLISKYPDkYAYPIPHTTRPAKPEEENGRSYYFVSHDEMMADIGANEYLEYGTHEDAMYGTKLD 793
Cdd:COG0194    5 IVLSGPSGAGKTTLVKALLERDPD-LRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGTPKA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 794 TIRRIHTEGKMAILDVEPQ-ALKILRTAeftPYVV--FIAAPSLQ---------------NIAdydgslERLAK-ESEML 854
Cdd:COG0194   84 EVEEALAAGKDVLLEIDVQgARQVKKKF---PDAVsiFILPPSLEelerrlrgrgtdseeVIE------RRLAKaREELA 154
                        170       180
                 ....*....|....*....|....*...
gi 442620344 855 RQlygHFFDLTIVNNDISETIATLETAI 882
Cdd:COG0194  155 HA---DEFDYVVVNDDLDRAVEELKAII 179
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
7-266 4.62e-22

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 101.41  E-value: 4.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   7 LFDDVYELCEVIGKGPFSIVRR--CI--HREsnqqFAVKIVD---------VAKFtaspglstadlKREATICHMLKHPH 73
Cdd:NF033483   4 LLGGRYEIGERIGRGGMAEVYLakDTrlDRD----VAVKVLRpdlardpefVARF-----------RREAQSAASLSHPN 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  74 IVELLETYSSEGMLYMVFEFMEGSDLcFEVVRRavaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvD 153
Cdd:NF033483  69 IVSVYDVGEDGGIPYIVMEYVDGRTL-KDYIRE---HGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILI---T 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 154 NSAPVKLGGFGSAIQLPGTRETiETHGRVGCPHYMAPE-----VVTRRlygkgCDVWGAGVMLHVLLSGRLPFLG-SGVr 227
Cdd:NF033483 142 KDGRVKVTDFGIARALSSTTMT-QTNSVLGTVHYLSPEqarggTVDAR-----SDIYSLGIVLYEMLTGRPPFDGdSPV- 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442620344 228 lqqSVARGRLSFEAP---EW-KSISANAKDLVMKMLAANPHHR 266
Cdd:NF033483 215 ---SVAYKHVQEDPPppsELnPGIPQSLDAVVLKATAKDPDDR 254
gmk PRK00300
guanylate kinase; Provisional
714-882 4.57e-21

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 92.07  E-value: 4.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 714 LVLLGAHGVGrrhiKNTLIS---KYPDKYAYPIPHTTRPAKPEEENGRSYYFVSHDEMMADIGANEYLEYGTHEDAMYGT 790
Cdd:PRK00300   8 IVLSGPSGAG----KSTLVKallERDPNLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYYGT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 791 KLDTIRRIHTEGKMAILDVEPQ-ALKILRTAeftPYVV--FIAAPSLQN---------------IAdydgslERLAK-ES 851
Cdd:PRK00300  84 PRSPVEEALAAGKDVLLEIDWQgARQVKKKM---PDAVsiFILPPSLEElerrlrgrgtdseevIA------RRLAKaRE 154
                        170       180       190
                 ....*....|....*....|....*....|.
gi 442620344 852 EMLRQlygHFFDLTIVNNDISETIATLETAI 882
Cdd:PRK00300 155 EIAHA---SEYDYVIVNDDLDTALEELKAII 182
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
495-572 1.23e-15

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 72.70  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  495 LVQFQKNTDEPMGITLKMTEDGR---CIVARIMHGGMIHRQAtLHVGDEIREINGQPVQHQSVGQLQRMLREARGSVTFK 571
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGdpgIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                  .
gi 442620344  572 I 572
Cdd:pfam00595  80 I 80
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
492-574 6.53e-12

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 62.01  E-value: 6.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   492 RVRLVQFQKNTdEPMGITLKM--TEDGRCIVARIMHGGMIHRqATLHVGDEIREINGQPVQHQSVGQLQRMLREARGSVT 569
Cdd:smart00228   1 EPRLVELEKGG-GGLGFSLVGgkDEGGGVVVSSVVPGSPAAK-AGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVT 78

                   ....*
gi 442620344   570 FKIVP 574
Cdd:smart00228  79 LTVLR 83
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
586-643 1.69e-11

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 59.86  E-value: 1.69e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344   586 FVRAQFDYNP-LDDELipcaqagiSFQVGDILQIISKDDHHWWQARLDtvGGSAGLIPS 643
Cdd:smart00326   4 QVRALYDYTAqDPDEL--------SFKKGDIITVLEKSDDGWWKGRLG--RGKEGLFPS 52
L27 pfam02828
L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.
347-396 4.76e-10

L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.


Pssm-ID: 460717  Cd Length: 52  Bit Score: 55.89  E-value: 4.76e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 442620344  347 VQRILDCLDDIYSLQDAHVDADVLRDMLRDNRLHQFLQLFDRIAATVVTS 396
Cdd:pfam02828   1 VELVLELLEDLQPLSEASEDLAELQKLLQSPHLQALLEAHDKVAQKVYEP 50
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
348-397 9.71e-10

domain in receptor targeting proteins Lin-2 and Lin-7;


Pssm-ID: 197794  Cd Length: 53  Bit Score: 54.82  E-value: 9.71e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 442620344   348 QRILDCLDDIYSLQDAHVDADVLRDMLRDNRLHQFLQLFDRIAATVVTSN 397
Cdd:smart00569   1 QRLLELLEELQSLLSPSEDLQELRRLLQSPHLQALLKIHDKVAETELDPP 50
L27 pfam02828
L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.
406-462 2.42e-09

L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.


Pssm-ID: 460717  Cd Length: 52  Bit Score: 53.58  E-value: 2.42e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344  406 VGRCRDVLEQLSSTSGGNSlggkyAKEELMRLLAAPHMQALLHSHDVVARDVYGEEA 462
Cdd:pfam02828   1 VELVLELLEDLQPLSEASE-----DLAELQKLLQSPHLQALLEAHDKVAQKVYEPPS 52
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
408-458 2.99e-09

domain in receptor targeting proteins Lin-2 and Lin-7;


Pssm-ID: 197794  Cd Length: 53  Bit Score: 53.67  E-value: 2.99e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 442620344   408 RCRDVLEQLSSTSGGNSLggkyaKEELMRLLAAPHMQALLHSHDVVARDVY 458
Cdd:smart00569   2 RLLELLEELQSLLSPSED-----LQELRRLLQSPHLQALLKIHDKVAETEL 47
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
588-643 3.37e-09

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 53.36  E-value: 3.37e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344  588 RAQFDYNPLD-DELipcaqagiSFQVGDILQIISKDDHHWWQARLDtvGGSAGLIPS 643
Cdd:pfam00018   1 VALYDYTAQEpDEL--------SFKKGDIIIVLEKSEDGWWKGRNK--GGKEGLIPS 47
 
Name Accession Description Interval E-value
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
8-308 0e+00

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 586.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGML 87
Cdd:cd14094    1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGML 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLCFEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSAI 167
Cdd:cd14094   81 YMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLPGTreTIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWKSI 247
Cdd:cd14094  161 QLGES--GLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHI 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 248 SANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRD-KLQRTHLADTVEELKRYNARRKLKGA 308
Cdd:cd14094  239 SESAKDLVRRMLMLDPAERITVYEALNHPWIKERDrYAYRIHLPETVEQLRKFNARRKLKGA 300
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
11-277 7.99e-100

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 312.49  E-value: 7.99e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  11 VYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSE---DEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLCFEVVRRavagFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSAIQLp 170
Cdd:cd05117   78 MELCTGGELFDRIVKK----GSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIF- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 gtRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGRLSFEAPEWKSISA 249
Cdd:cd05117  153 --EEGEKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQeLFEKILKGKYSFDSPEWKNVSE 230
                        250       260
                 ....*....|....*....|....*...
gi 442620344 250 NAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd05117  231 EAKDLIKRLLVVDPKKRLTAAEALNHPW 258
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-308 9.46e-95

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 300.49  E-value: 9.46e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd14086    1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSAR---DHQKLEREARICRLLKHPNIVRLHDSISEEGFHYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSAIQL 169
Cdd:cd14086   78 VFDLVTGGELFEDIVAREF----YSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PGTRETieTHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRLSFEAPEWKSIS 248
Cdd:cd14086  154 QGDQQA--WFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQhRLYAQIKAGAYDYPSPEWDTVT 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKLQRT-HLADTVEELKRYNARRKLKGA 308
Cdd:cd14086  232 PEAKDLINQMLTVNPAKRITAAEALKHPWICQRDRVASMvHRQETVDCLKKFNARRKLKGA 292
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-278 6.09e-82

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 264.78  E-value: 6.09e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344    12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPglstADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDR----ERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344    92 EFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLpg 171
Cdd:smart00220  77 EYCEGGDL-FDLLKKRGR---LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL---DEDGHVKLADFGLARQL-- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   172 tRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG--VRLQQSVARGRLSFEAPEWKsISA 249
Cdd:smart00220 148 -DPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDqlLELFKKIGKPKPPFPPPEWD-ISP 225
                          250       260
                   ....*....|....*....|....*....
gi 442620344   250 NAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:smart00220 226 EAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
Guanylate_kin pfam00625
Guanylate kinase;
710-883 1.04e-68

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 226.49  E-value: 1.04e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  710 QRKTLVLLGAHGVGRRHIKNTLISKYPDKYAYPIPHTTRPAKPEEENGRSYYFVSHDEMMADIGANEYLEYGTHEDAMYG 789
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  790 TKLDTIRRIHTEGKMAILDVEPQALKILRTAEFTPYVVFIAAPSLQ-----NIADYDGSLERLAKESEMLRQLYGHF-FD 863
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKvlqrrLKGRGKEQEEKINKRMAAAEQEFQHYeFD 160
                         170       180
                  ....*....|....*....|
gi 442620344  864 LTIVNNDISETIATLETAID 883
Cdd:pfam00625 161 VIIVNDDLEEAYKKLKEALE 180
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
12-277 2.54e-65

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 219.70  E-value: 2.54e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14003    2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEE---IEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFG-SAIQLP 170
Cdd:cd14003   79 EYASGGEL-FDYIVNNGR---LSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILL---DKNGNLKIIDFGlSNEFRG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRetieTHGRVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGRLsfeaPEWKSIS 248
Cdd:cd14003  152 GSL----LKTFCGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSkLFRKILKGKY----PIPSHLS 223
                        250       260
                 ....*....|....*....|....*....
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14003  224 PDARDLIRRMLVVDPSKRITIEEILNHPW 252
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
12-312 2.23e-63

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 215.96  E-value: 2.23e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFtaspglstaDLKREATIchMLK---HPHIVELLETYSSEGMLY 88
Cdd:cd14091    2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKR---------DPSEEIEI--LLRygqHPNIITLRDVYDDGNSVY 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAP-VKLGGFGSAI 167
Cdd:cd14091   71 LVTELLRGGELLDRILRQKF----FSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDPEsLRICDFGFAK 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLpgtRETietHGRVGCPHY----MAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-----VRLQQsVARGRLS 238
Cdd:cd14091  147 QL---RAE---NGLLMTPCYtanfVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASGPndtpeVILAR-IGSGKID 219
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620344 239 FEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKLQRTHLADTveelkryNARRKLKGAVQAI 312
Cdd:cd14091  220 LSGGNWDHVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRDSLPQRQLTDP-------QDAALVKGAVAAT 286
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
8-277 2.70e-59

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 203.74  E-value: 2.70e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADL---KREATICHML-KHPHIVELLETYSS 83
Cdd:cd14093    1 FYAKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSENEAEELReatRREIEILRQVsGHPNIIELHDVFES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGMLYMVFEFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGF 163
Cdd:cd14093   81 PTFIFLVFELCRKGEL-FDYLTEVVT---LSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILL---DDNLNVKISDF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 164 GSAIQLPGTRETIEThgrVGCPHYMAPEVVTRRL------YGKGCDVWGAGVMLHVLLSGRLPFLGsgvRLQQSVAR--- 234
Cdd:cd14093  154 GFATRLDEGEKLREL---CGTPGYLAPEVLKCSMydnapgYGKEVDMWACGVIMYTLLAGCPPFWH---RKQMVMLRnim 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 442620344 235 -GRLSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14093  228 eGKYEFGSPEWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
12-277 1.25e-58

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 201.40  E-value: 1.25e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLstadLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14095    2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHM----IENEVAILRRVKHPNIVQLIEEYDTDTELYLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATV-DNSAPVKLGGFGSAIQLP 170
Cdd:cd14095   78 ELVKGGDL-FDAITSSTK---FTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHeDGSKSLKLADFGLATEVK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRETIethgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGvRLQQS----VARGRLSFEAPEWKS 246
Cdd:cd14095  154 EPLFTV-----CGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPD-RDQEElfdlILAGEFEFLSPYWDN 227
                        250       260       270
                 ....*....|....*....|....*....|.
gi 442620344 247 ISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14095  228 ISDSAKDLISRMLVVDPEKRYSAGQVLDHPW 258
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
8-289 3.74e-57

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 199.06  E-value: 3.74e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYEL---CEVIGKGPFSIVRRCIHRESNQQFAVKIVDvakftaspglSTADLKREATICHMLK-HPHIVELLETYSS 83
Cdd:cd14092    1 FFQNYELdlrEEALGDGSFSVCRKCVHKKTGQEFAVKIVS----------RRLDTSREVQLLRLCQgHPNIVKLHEVFQD 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGMLYMVFEFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGF 163
Cdd:cd14092   71 ELHTYLVMELLRGGEL-LERIRKKKR---FTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAEIKIVDF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 164 GSAIQLPGTrETIEThgrvgcP----HYMAPEVVTRRLYGKG----CDVWGAGVMLHVLLSGRLPFLGSGVRLQ-----Q 230
Cdd:cd14092  147 GFARLKPEN-QPLKT------PcftlPYAAPEVLKQALSTQGydesCDLWSLGVILYTMLSGQVPFQSPSRNESaaeimK 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 231 SVARGRLSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKLQRTHL 289
Cdd:cd14092  220 RIKSGDFSFDGEEWKNVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSSPSSTPL 278
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
8-278 1.18e-56

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 196.46  E-value: 1.18e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTA---SPGLSTADLKREATICHMLKHPHIVELLETYSSE 84
Cdd:cd14084    4 LRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIgsrREINKPRNIETEIEILKKLSHPCIIKIEDFFDAE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  85 GMLYMVFEFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFG 164
Cdd:cd14084   84 DDYYIVLELMEGGEL-FDRVVSNKR---LKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECLIKITDFG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 SAiQLPGTRETIEThgRVGCPHYMAPEVVT---RRLYGKGCDVWGAGVMLHVLLSGRLPFLG--SGVRLQQSVARGRLSF 239
Cdd:cd14084  160 LS-KILGETSLMKT--LCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEeyTQMSLKEQILSGKYTF 236
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 442620344 240 EAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14084  237 IPKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
Pkinase pfam00069
Protein kinase domain;
12-278 3.71e-56

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 192.84  E-value: 3.71e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKK---KDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   92 EFMEGSDLcFEVVRRavaGFVYSEAVACHYMRQILEALRYCHEndilhrdvrpacallatvdnsapvklggfgsaiqlpg 171
Cdd:pfam00069  78 EYVEGGSL-FDLLSE---KGAFSEREAKFIMKQILEGLESGSS------------------------------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  172 tretieTHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWKSISANA 251
Cdd:pfam00069 117 ------LTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLSEEA 190
                         250       260
                  ....*....|....*....|....*..
gi 442620344  252 KDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:pfam00069 191 KDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
18-277 4.66e-56

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 194.02  E-value: 4.66e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVakftasPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFIPK------RDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLcfevVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSApVKLGGFGSAIQL-PGTreti 176
Cdd:cd14006   75 EL----LDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQ-IKIIDFGLARKLnPGE---- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 177 ETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGRLSFEAPEWKSISANAKDLV 255
Cdd:cd14006  146 ELKEIFGTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQeTLANISACRVDFSEEYFSSVSQEAKDFI 225
                        250       260
                 ....*....|....*....|..
gi 442620344 256 MKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14006  226 RKLLVKEPRKRPTAQEALQHPW 247
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
8-312 5.05e-56

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 195.43  E-value: 5.05e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvakftaspglSTADLK---REATICHMLKHPHIVELLETYSSE 84
Cdd:cd14085    1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLK----------KTVDKKivrTEIGVLLRLSHPNIIKLKEIFETP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  85 GMLYMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFG 164
Cdd:cd14085   71 TEISLVLELVTGGELFDRIVEKGY----YSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 SAIQLPgtrETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQ--QSVARGRLSFEAP 242
Cdd:cd14085  147 LSKIVD---QQVTMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYmfKRILNCDYDFVSP 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 243 EWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKlQRTHLADTVEELKRYNARRKLKGAVQAI 312
Cdd:cd14085  224 WWDDVSLNAKDLVKKLIVLDPKKRLTTQQALQHPWVTGKAA-NFAHMDTAQKKLQEFNARRKLKAAVKAV 292
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
494-574 8.96e-55

PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CASK, Caenorhabditis elegans Lin-2, and related domains. CASK and Lin-2 are membrane-associated guanylate kinase (MAGUK)-like proteins. CASK (also known as Calcium/calmodulin-dependent protein kinase, CAKI, and Camguk) has a role in synaptic transmembrane protein anchoring and ion channel trafficking. CASK may regulate transmembrane proteins that bind calcium, calmodulin, or nucleotides; it regulates the Drosophila ether a go-go (eag) potassium channel, and also regulates autophosphorylation of CaMKII. CASK binding partners include the transcription factor TBR1, and cell-surface proteins, including amyloid precursor protein, neurexins, and syndecans. Lin-2, as a component of the CLin-10-Lin-2-Lin-7 complex, plays a role in controlling the basolateral localization of the EGF receptor Let-23; this complex also associates with the neuron-specific motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor 2B along microtubules. CASK may also function in targeting or scaffolding of the protein parkin which is selectively truncated by a Parkinson's disease-causing mutation; the C-terminus of parkin functions as a class II PDZ-binding motif that binds CASK. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP6-MPP2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467267 [Multi-domain]  Cd Length: 81  Bit Score: 183.84  E-value: 8.96e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 494 RLVQFQKNTDEPMGITLKMTEDGRCIVARIMHGGMIHRQATLHVGDEIREINGQPVQHQSVGQLQRMLREARGSVTFKIV 573
Cdd:cd10831    1 RLVQFQKNTDEPMGITLKMNEDGRCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREARGSITFKIV 80

                 .
gi 442620344 574 P 574
Cdd:cd10831   81 P 81
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
720-883 4.92e-54

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 185.57  E-value: 4.92e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   720 HGVGRRHIKNTLISKYPDKYAYPIPHTTRPAKPEEENGRSYYFVSHDEMMADIGANEYLEYGTHEDAMYGTKLDTIRRIH 799
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   800 TEGKMAILDVEPQALKILRTAEFTPYVVFIAAPSLQNIAD-----YDGSLERLAKESEMLRQLYG--HFFDLTIVNNDIS 872
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERrlrqrGTETSERIQKRLAAAQKEAQeyHLFDYVIVNDDLE 160
                          170
                   ....*....|.
gi 442620344   873 ETIATLETAID 883
Cdd:smart00072 161 DAYEELKEILE 171
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
11-278 7.52e-54

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 187.85  E-value: 7.52e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  11 VYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLstADLKREATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd14081    2 PYRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVL--MKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFG-SAIQL 169
Cdd:cd14081   80 LEYVSGGELFDYLVKKGR----LTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLL---DEKNNIKIADFGmASLQP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PGTRetIETHgrVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGRlsFEAPEwkSI 247
Cdd:cd14081  153 EGSL--LETS--CGSPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRqLLEKVKRGV--FHIPH--FI 224
                        250       260       270
                 ....*....|....*....|....*....|.
gi 442620344 248 SANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14081  225 SPDAQDLLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
12-277 2.49e-53

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 186.46  E-value: 2.49e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKfTASPGLsTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14663    2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQ-VAREGM-VEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEvvrRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFG-SAIQLP 170
Cdd:cd14663   80 ELVTGGEL-FS---KIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLL---DEDGNLKISDFGlSALSEQ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRETIeTHGRVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRlsFEAPEWksIS 248
Cdd:cd14663  153 FRQDGL-LHTTCGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFDDENLmALYRKIMKGE--FEYPRW--FS 227
                        250       260
                 ....*....|....*....|....*....
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14663  228 PGAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
12-277 1.42e-52

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 184.38  E-value: 1.42e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLstadLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14185    2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDM----IESEILIIKSLSHPNIVKLFEVYETEKEIYLIL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLA-TVDNSAPVKLGGFGSAIQLP 170
Cdd:cd14185   78 EYVRGGDL-FDAIIESVK---FTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQhNPDKSTTLKLADFGLAKYVT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRETIethgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLgSGVRLQ----QSVARGRLSFEAPEWKS 246
Cdd:cd14185  154 GPIFTV-----CGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFR-SPERDQeelfQIIQLGHYEFLPPYWDN 227
                        250       260       270
                 ....*....|....*....|....*....|.
gi 442620344 247 ISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14185  228 ISEAAKDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
18-278 2.00e-51

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 181.60  E-value: 2.00e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAK-------FTASPGLSTA--DLKREATICHMLKHPHIVELLET--YSSEGM 86
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRlrkrregKNDRGKIKNAldDVRREIAIMKKLDHPNIVRLYEVidDPESDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEGSDLcfEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSA 166
Cdd:cd14008   81 LYLVLEYCEGGPV--MELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGT---VKISDFGVS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLPGTRETIEthGRVGCPHYMAPEV--VTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAP 242
Cdd:cd14008  156 EMFEDGNDTLQ--KTAGTPAFLAPELcdGDSKTYsGKAADIWALGVTLYCLVFGRLPFNGdNILELYEAIQNQNDEFPIP 233
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 442620344 243 ewKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14008  234 --PELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
10-278 2.30e-51

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 182.23  E-value: 2.30e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELC-EVIGKGPFSIVRRCIHRESNQQFAVKIVDvakftASPGLSTADLKREATICHMLK-HPHIVELLETYSSEGML 87
Cdd:cd14090    1 DLYKLTgELLGEGAYASVQTCINLYTGKEYAVKIIE-----KHPGHSRSRVFREVETLHQCQgHPNILQLIEYFEDDERF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGF--GS 165
Cdd:cd14090   76 YLVFEKMRGGPLLSHIEKRVH----FTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSPVKICDFdlGS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 166 AIQLPGTR----ETIETHGRVGCPHYMAPEVV-----TRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR--------- 227
Cdd:cd14090  152 GIKLSSTSmtpvTTPELLTPVGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGRCGEdcgwdrgea 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 228 -------LQQSVARGRLSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14090  232 cqdcqelLFHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
10-317 6.00e-51

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 180.99  E-value: 6.00e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvaKFTASPGLSTADLKREAtichmlKHPHIVELLETYSSEGMLYM 89
Cdd:cd14175    1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVID--KSKRDPSEEIEILLRYG------QHPNIITLKDVYDDGKHVYL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatVDNSA---PVKLGGFGSA 166
Cdd:cd14175   73 VTELMRGGELLDKILRQKF----FSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILY--VDESGnpeSLRICDFGFA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLPGTRETIETHGRVGcpHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFL-GSGVRLQQSVAR---GRLSFEAP 242
Cdd:cd14175  147 KQLRAENGLLMTPCYTA--NFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFAnGPSDTPEEILTRigsGKFTLSGG 224
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620344 243 EWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKLQRTHLadtveelkRYNARRKLKGAVQAIAGGTN 317
Cdd:cd14175  225 NWNTVSDAAKDLVSKMLHVDPHQRLTAKQVLQHPWITQKDKLPQSQL--------NHQDVQLVKGAMAATYSALN 291
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
9-277 1.95e-50

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 178.33  E-value: 1.95e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   9 DDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvaKFTASPGLSTadLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd14083    2 RDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCID--KKALKGKEDS--LENEIAVLRKIKHPNIVQLLDIYESKSHLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLcFEvvrRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFG-SAI 167
Cdd:cd14083   78 LVMELVTGGEL-FD---RIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISDFGlSKM 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLPGTRETIethgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEWKS 246
Cdd:cd14083  154 EDSGVMSTA-----CGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDeNDSKLFAQILKAEYEFDSPYWDD 228
                        250       260       270
                 ....*....|....*....|....*....|.
gi 442620344 247 ISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14083  229 ISDSAKDFIRHLMEKDPNKRYTCEQALEHPW 259
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
8-277 2.27e-50

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 179.01  E-value: 2.27e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPG----LSTADLKREATICHMLKHPHIVELLETYSS 83
Cdd:cd14181    8 FYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTAERLSPEqleeVRSSTLKEIHILRQVSGHPSIITLIDSYES 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGMLYMVFEFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGF 163
Cdd:cd14181   88 STFIFLVFDLMRRGEL-FDYLTEKVT---LSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILL---DDQLHIKLSDF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 164 GSAIQL-PGT--RETiethgrVGCPHYMAPEVV------TRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQ-QSVA 233
Cdd:cd14181  161 GFSCHLePGEklREL------CGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMlRMIM 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 442620344 234 RGRLSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14181  235 EGRYQFSSPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPF 278
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
16-277 4.10e-50

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 177.87  E-value: 4.10e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIV-DVAKftaspglstadLKREATIcHML--KHPHIVELLE----TYSSEGMLY 88
Cdd:cd14089    7 QVLGLGINGKVLECFHKKTGEKFALKVLrDNPK-----------ARREVEL-HWRasGCPHIVRIIDvyenTYQGRKCLL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLCFEVVRRAVAGFVYSEAVacHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSAiQ 168
Cdd:cd14089   75 VVMECMEGGELFSRIQERADSAFTEREAA--EIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGFA-K 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPGTRETIEThgrvGC--PHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGS-GVRL----QQSVARGRLSFEA 241
Cdd:cd14089  152 ETTTKKSLQT----PCytPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNhGLAIspgmKKRIRNGQYEFPN 227
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 442620344 242 PEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14089  228 PEWSNVSEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
18-276 1.25e-49

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 174.77  E-value: 1.25e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGlstaDLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLE----ELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLcFEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPGTRETIE 177
Cdd:cd00180   77 SL-KDLLKENKGPL--SEEEALSILRQLLSALEYLHSNGIIHRDLKPENILL---DSDGTVKLADFGLAKDLDSDDSLLK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 178 THGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLlsgrlpflgsgvrlqqsvargrlsfeapewksisANAKDLVMK 257
Cdd:cd00180  151 TTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL----------------------------------EELKDLIRR 196
                        250
                 ....*....|....*....
gi 442620344 258 MLAANPHHRLSITEVLDHP 276
Cdd:cd00180  197 MLQYDPKKRPSAKELLEHL 215
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
12-279 1.35e-49

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 175.74  E-value: 1.35e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpGLSTaDLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14007    2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKS-GLEH-QLRREIEIQSHLRHPNILRLYGYFEDKKRIYLIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEVVRRAVagfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLP- 170
Cdd:cd14007   80 EYAPNGEL-YKELKKQK---RFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILL---GSNGELKLADFGWSVHAPs 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRETIethgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGRLSFeapeWKSISA 249
Cdd:cd14007  153 NRRKTF-----CGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQeTYKRIQNVDIKF----PSSVSP 223
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 250 NAKDLVMKMLAANPHHRLSITEVLDHPWIR 279
Cdd:cd14007  224 EAKDLISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
12-278 2.87e-49

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 174.96  E-value: 2.87e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd08215    2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEK---EREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSAIQLPG 171
Cdd:cd08215   79 EYADGGDLAQKIKKQKKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGV---VKLGDFGISKVLES 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIEThgRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGRlsFEAPEwKSISAN 250
Cdd:cd08215  156 TTDLAKT--VVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPaLVYKIVKGQ--YPPIP-SQYSSE 230
                        250       260
                 ....*....|....*....|....*...
gi 442620344 251 AKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd08215  231 LRDLVNSMLQKDPEKRPSANEILSSPFI 258
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-304 2.92e-49

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 175.95  E-value: 2.92e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVdvakfTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd14166    3 ETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCI-----KKSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFG-SAIQ 168
Cdd:cd14166   78 VMQLVSGGELFDRILERGV----YTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMITDFGlSKME 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPGTRETIethgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEWKSI 247
Cdd:cd14166  154 QNGIMSTA-----CGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEeTESRLFEKIKEGYYEFESPFWDDI 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344 248 SANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKLQRTHLADTVEELKRYNARRK 304
Cdd:cd14166  229 SESAKDFIRHLLEKNPSKRYTCEKALSHPWIIGNTALHRDIYPSVSEQIQKNFAKSK 285
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
10-277 3.52e-49

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 174.83  E-value: 3.52e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLstadLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd14184    1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHL----IENEVSILRRVKHPNIIMLIEEMDTPAELYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATV-DNSAPVKLGGFGSAIQ 168
Cdd:cd14184   77 VMELVKGGDL-FDAITSSTK---YTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYpDGTKSLKLGDFGLATV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPGTRETIethgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLgSGVRLQQ----SVARGRLSFEAPEW 244
Cdd:cd14184  153 VEGPLYTV-----CGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFR-SENNLQEdlfdQILLGKLEFPSPYW 226
                        250       260       270
                 ....*....|....*....|....*....|...
gi 442620344 245 KSISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14184  227 DNITDSAKELISHMLQVNVEARYTAEQILSHPW 259
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
4-320 5.41e-49

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 177.13  E-value: 5.41e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   4 DEILFDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftASPGLSTADLKREAtichmlKHPHIVELLETYSS 83
Cdd:cd14176   13 NSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK--RDPTEEIEILLRYG------QHPNIITLKDVYDD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGMLYMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatVD---NSAPVKL 160
Cdd:cd14176   85 GKYVYVVTELMKGGELLDKILRQKF----FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILY--VDesgNPESIRI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 161 GGFGSAIQLPGTRETIETHGRVGcpHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFL-GSGVRLQQSVAR---GR 236
Cdd:cd14176  159 CDFGFAKQLRAENGLLMTPCYTA--NFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFAnGPDDTPEEILARigsGK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 237 LSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKLQRThladtveELKRYNARRKLKGAVQAIAGGT 316
Cdd:cd14176  237 FSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQY-------QLNRQDAPHLVKGAMAATYSAL 309

                 ....
gi 442620344 317 NMDP 320
Cdd:cd14176  310 NRNQ 313
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
12-278 8.31e-49

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 175.32  E-value: 8.31e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQF-AVKIVDVAKFTASP--GLSTADLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd14096    3 YRLINKIGEGAFSNVYKAVPLRNTGKPvAIKVVRKADLSSDNlkGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVD--------NSAP--- 157
Cdd:cd14096   83 IVLELADGGEIFHQIVRLTY----FSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPIPfipsivklRKADdde 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 158 -------------------VKLGGFGSAIQLpGTRETIETHGRVGcphYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGR 218
Cdd:cd14096  159 tkvdegefipgvggggigiVKLADFGLSKQV-WDSNTKTPCGTVG---YTAPEVVKDERYSKKVDMWALGCVLYTLLCGF 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620344 219 LPFLGSGVR-LQQSVARGRLSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14096  235 PPFYDESIEtLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
18-277 1.77e-48

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 172.79  E-value: 1.77e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKK---LQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLCFEVVRRavagFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSA--IQLPGTRET 175
Cdd:cd14009   78 DLSQYIRKR----GRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVLKIADFGFArsLQPASMAET 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 176 IethgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGRLSFEAPEWKSISANAKDL 254
Cdd:cd14009  154 L-----CGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNhVQLLRNIERSDAVIPFPIAAQLSPDCKDL 228
                        250       260
                 ....*....|....*....|...
gi 442620344 255 VMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14009  229 LRRLLRRDPAERISFEEFFAHPF 251
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
12-274 1.94e-48

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 172.77  E-value: 1.94e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAkfTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14014    2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPE--LAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEVVRRavaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSAIQLPG 171
Cdd:cd14014   80 EYVEGGSL-ADLLRE---RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGR---VKLTDFGIARALGD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETiETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEWKSISAN 250
Cdd:cd14014  153 SGLT-QTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGdSPAAVLAKHLQEAPPPPSPLNPDVPPA 231
                        250       260
                 ....*....|....*....|....*
gi 442620344 251 AKDLVMKMLAANPHHRL-SITEVLD 274
Cdd:cd14014  232 LDAIILRALAKDPEERPqSAAELLA 256
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
8-317 2.35e-48

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 174.05  E-value: 2.35e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftASPGLSTADLKREAtichmlKHPHIVELLETYSSEGML 87
Cdd:cd14177    2 FTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSK--RDPSEEIEILMRYG------QHPNIITLKDVYDDGRYV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLCFEVVRRAvagfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACAL-LATVDNSAPVKLGGFGSA 166
Cdd:cd14177   74 YLVTELMKGGELLDRILRQK----FFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANADSIRICDFGFA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLPGTRETIETHGRVGcpHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG----SGVRLQQSVARGRLSFEAP 242
Cdd:cd14177  150 KQLRGENGLLLTPCYTA--NFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANgpndTPEEILLRIGSGKFSLSGG 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620344 243 EWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKLQRthladtvEELKRYNARRKLKGAVQAIAGGTN 317
Cdd:cd14177  228 NWDTVSDAAKDLLSHMLHVDPHQRYTAEQVLKHSWIACRDQLPH-------YQLNRQDAPHLVKGAMAATYSALN 295
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
8-290 2.67e-48

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 173.66  E-value: 2.67e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftASPGLSTADLKREAtichmlKHPHIVELLETYSSEGML 87
Cdd:cd14178    1 FTDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSK--RDPSEEIEILLRYG------QHPNIITLKDVYDDGKFV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACAL-LATVDNSAPVKLGGFGSA 166
Cdd:cd14178   73 YLVMELMRGGELLDRILRQKC----FSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNPESIRICDFGFA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLPGTRETIETHGRVGcpHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFL-GSGVRLQQSVAR---GRLSFEAP 242
Cdd:cd14178  149 KQLRAENGLLMTPCYTA--NFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFAnGPDDTPEEILARigsGKYALSGG 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 442620344 243 EWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKLQRTHLA 290
Cdd:cd14178  227 NWDSISDAAKDIVSKMLHVDPHQRLTAPQVLRHPWIVNREYLSQNQLS 274
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
16-278 5.49e-48

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 171.55  E-value: 5.49e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglsTAD-LKREATICHMLKHPHIVELLETYSSEGMLYMVFEFM 94
Cdd:cd06606    6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEE----ELEaLEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  95 EG---SDLCfevvrRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLPG 171
Cdd:cd06606   82 PGgslASLL-----KKFGKL--PEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANIL---VDSDGVVKLADFGCAKRLAE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF--LGSGVRLQQSVARGRLSFEAPEWksISA 249
Cdd:cd06606  152 IATGEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWseLGNPVAALFKIGSSGEPPPIPEH--LSE 229
                        250       260
                 ....*....|....*....|....*....
gi 442620344 250 NAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06606  230 EAKDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
8-279 1.85e-47

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 170.48  E-value: 1.85e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVakfTASPGLSTADLK--REATI--CHMLK----HPHIVELLE 79
Cdd:cd14182    1 FYEKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDI---TGGGSFSPEEVQelREATLkeIDILRkvsgHPNIIQLKD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  80 TYSSEGMLYMVFEFMEGSDLcFEVVRRAVagfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVK 159
Cdd:cd14182   78 TYETNTFFFLVFDLMKKGEL-FDYLTEKV---TLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILL---DDDMNIK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 160 LGGFGSAIQLPGTRETIEThgrVGCPHYMAPEVVTRRL------YGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQ-QSV 232
Cdd:cd14182  151 LTDFGFSCQLDPGEKLREV---CGTPGYLAPEIIECSMddnhpgYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMlRMI 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 442620344 233 ARGRLSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIR 279
Cdd:cd14182  228 MSGNYQFGSPEWDDRSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQ 274
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
12-496 5.69e-47

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 175.59  E-value: 5.69e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvAKFTASPGLStADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLR-PELAADPEAR-ERFRREARALARLNHPNIVRVYDVGEEDGRPYLVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCfEVVRRavaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLPG 171
Cdd:COG0515   87 EYVEGESLA-DLLRR---RGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANIL---LTPDGRVKLIDFGIARALGG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETiETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEWKSISAN 250
Cdd:COG0515  160 ATLT-QTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGdSPAELLRAHLREPPPPPSELRPDLPPA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 251 AKDLVMKMLAANPHHRL-SITEVLDHpwirdrdkLQRTHLADTVEELKRYNARRKLKGAVQAIAGGTNMDPLYATDADMP 329
Cdd:COG0515  239 LDAIVLRALAKDPEERYqSAAELAAA--------LRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 330 ITGATDEWADEEAGIEAVQRILDCLDDIYSLQDAHVDADVLRDMLRDNRLHQFLQLFDRIAATVVTsnGRAPAAEAVGRC 409
Cdd:COG0515  311 AAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAA--AAAAAAAALAAA 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 410 RDVLEQLSSTSGGNSLGGKYAKEELMRLLAAPHMQALLHSHDVVARDVYGEEALRVTPPPMVPYLNGDELDNVEGGELQH 489
Cdd:COG0515  389 AAAAAAAAAAALAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAAAARLLAAAAAAAAAAAAAPLLAALLAAA 468

                 ....*..
gi 442620344 490 VTRVRLV 496
Cdd:COG0515  469 ALAAAAA 475
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
18-278 1.15e-46

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 167.40  E-value: 1.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTaspglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAK-----DREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLcFEvvrRAVA-GFVYSEAVACHYMRQILEALRYCHENDILHRDVRPAcALLATVDNSAPVKLGGFGSAIQLPGTRETi 176
Cdd:cd14103   76 EL-FE---RVVDdDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPE-NILCVSRTGNQIKIIDFGLARKYDPDKKL- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 177 ethgRV--GCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEWKSISANAKD 253
Cdd:cd14103  150 ----KVlfGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGdNDAETLANVTRAKWDFDDEAFDDISDEAKD 225
                        250       260
                 ....*....|....*....|....*
gi 442620344 254 LVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14103  226 FISKLLVKDPRKRMSAAQCLQHPWL 250
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
10-278 2.63e-46

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 167.90  E-value: 2.63e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELC-EVIGKGPFSIVRRCIHRESNQQFAVKIVDvakftASPGLSTADLKREATICHMLK-HPHIVELLETYSSEGML 87
Cdd:cd14173    1 DVYQLQeEVLGEGAYARVQTCINLITNKEYAVKIIE-----KRPGHSRSRVFREVEMLYQCQgHRNVLELIEFFEEEDKF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGF--GS 165
Cdd:cd14173   76 YLVFEKMRGGSILSHIHRRRH----FNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKICDFdlGS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 166 AIQLPGTRETIETHGRV---GCPHYMAPEVVTR-----RLYGKGCDVWGAGVMLHVLLSGRLPFLGS------------- 224
Cdd:cd14173  152 GIKLNSDCSPISTPELLtpcGSAEYMAPEVVEAfneeaSIYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdcgwdrgeac 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344 225 ---GVRLQQSVARGRLSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14173  232 pacQNMLFESIQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
12-278 5.16e-46

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 165.82  E-value: 5.16e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQ--FAVKIVDVAKftASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd14080    2 YRLGKTIGEGSYSKVKLAEYTKSGLKekVACKIIDKKK--APKDFLEKFLPRELEILRKLRHPNIIQVYSIFERGSKVFI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLcFEVVRRAvaGFVySEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSAiql 169
Cdd:cd14080   80 FMEYAEHGDL-LEYIQKR--GAL-SESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNN---VKLSDFGFA--- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 pgtRETIETHGRV------GCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSGVR--LQQSVARGrLSFE 240
Cdd:cd14080  150 ---RLCPDDDGDVlsktfcGSAAYAAPEILQGIPYdPKKYDIWSLGVILYIMLCGSMPFDDSNIKkmLKDQQNRK-VRFP 225
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 442620344 241 APEWKsISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14080  226 SSVKK-LSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
16-289 6.24e-46

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 167.52  E-value: 6.24e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIVDvAKFTASPGLSTADLKreatICHmlKHPHIVELLETYSSEGMLYMVFEFME 95
Cdd:cd14179   13 KPLGEGSFSICRKCLHKKTNQEYAVKIVS-KRMEANTQREIAALK----LCE--GHPNIVKLHEVYHDQLHTFLVMELLK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 GSDLcFEVVRRAVagfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSAIQLPGTRET 175
Cdd:cd14179   86 GGEL-LERIKKKQ---HFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSEIKIIDFGFARLKPPDNQP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 176 IEThgrvgcP----HYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF--------LGSGVRLQQSVARGRLSFEAPE 243
Cdd:cd14179  162 LKT------PcftlHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFqchdksltCTSAEEIMKKIKQGDFSFEGEA 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 442620344 244 WKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKLQRTHL 289
Cdd:cd14179  236 WKNVSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQDGSQLSSNPL 281
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-278 6.30e-46

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 165.97  E-value: 6.30e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVrrCIHRESNQQFAVKIVDVAKfTASPGLSTAdLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd14167    3 DIYDFREVLGTGAFSEV--VLAEEKRTQKLVAIKCIAK-KALEGKETS-IENEIAVLHKIKHPNIVALDDIYESGGHLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLCFEVVRRavaGFvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFG-SAIQ 168
Cdd:cd14167   79 IMQLVSGGELFDRIVEK---GF-YTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSKIMISDFGlSKIE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPGTRETIEthgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGRLSFEAPEWKSI 247
Cdd:cd14167  155 GSGSVMSTA----CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENdAKLFEQILKAEYEFDSPYWDDI 230
                        250       260       270
                 ....*....|....*....|....*....|.
gi 442620344 248 SANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14167  231 SDSAKDFIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
10-278 7.44e-46

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 165.45  E-value: 7.44e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAvkivdvAKFTASPGLSTADL-KREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd14114    2 DHYDILEELGTGAFGVVHRCTERATGNNFA------AKFIMTPHESDKETvRKEIQIMNQLHHPKLINLHDAFEDDNEMV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLcFEvvRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPAcALLATVDNSAPVKLGGFGSAIQ 168
Cdd:cd14114   76 LILEFLSGGEL-FE--RIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPE-NIMCTTKRSNEVKLIDFGLATH 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 L-PGTRETIEThgrvGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGRLSFEAPEWKS 246
Cdd:cd14114  152 LdPKESVKVTT----GTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENdDETLRNVKSCDWNFDDSAFSG 227
                        250       260       270
                 ....*....|....*....|....*....|..
gi 442620344 247 ISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14114  228 ISEEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
12-278 1.17e-45

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 165.01  E-value: 1.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvakfTASPGLSTADlkREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14087    3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIE----TKCRGREVCE--SELNVLRRVRHTNIIQLIEVFETKERVYMVM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSdlcfEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSAIQLPG 171
Cdd:cd14087   77 ELATGG----ELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIMITDFGLASTRKK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHgRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGRLSFEAPEWKSISAN 250
Cdd:cd14087  153 GPNCLMKT-TCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNrTRLYRQILRAKYSYSGEPWPSVSNL 231
                        250       260
                 ....*....|....*....|....*...
gi 442620344 251 AKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14087  232 AKDFIDRLLTVNPGERLSATQALKHPWI 259
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
11-279 5.07e-45

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 163.88  E-value: 5.07e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  11 VYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAkftaspGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd14104    1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVK------GADQVLVKKEISILNIARHRNILRLHESFESHEELVMI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLcFEvvRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPAcALLATVDNSAPVKLGGFGSAIQL- 169
Cdd:cd14104   75 FEFISGVDI-FE--RITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPE-NIIYCTRRGSYIKIIEFGQSRQLk 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PGTRETIEthgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEWKSIS 248
Cdd:cd14104  151 PGDKFRLQ----YTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAeTNQQTIENIRNAEYAFDDEAFKNIS 226
                        250       260       270
                 ....*....|....*....|....*....|.
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPWIR 279
Cdd:cd14104  227 IEALDFVDRLLVKERKSRMTAQEALNHPWLK 257
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
11-278 6.03e-45

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 163.10  E-value: 6.03e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  11 VYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd14097    2 IYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSS---AVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALL--ATVDNSAP--VKLGGFGSA 166
Cdd:cd14097   79 MELCEDGELKELLLRKGF----FSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVksSIIDNNDKlnIKVTDFGLS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLPGTRETIETHgRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEWK 245
Cdd:cd14097  155 VQKYGLGEDMLQE-TCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAkSEEKLFEEIRKGDLTFTQSVWQ 233
                        250       260       270
                 ....*....|....*....|....*....|...
gi 442620344 246 SISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14097  234 SVSDAAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
12-277 1.04e-44

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 162.11  E-value: 1.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftaSPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14069    3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKR---APGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSAIQLPG 171
Cdd:cd14069   80 EYASGGEL-FDKIEPDVG---MPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDN---LKISDFGLATVFRY 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHGRVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPF-LGSGVRLQQSVAR-GRLSFEAPeWKSIS 248
Cdd:cd14069  153 KGKERLLNKMCGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELPWdQPSDSCQEYSDWKeNKKTYLTP-WKKID 231
                        250       260
                 ....*....|....*....|....*....
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14069  232 TAALSLLRKILTENPNKRITIEDIKKHPW 260
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
10-280 1.49e-44

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 162.09  E-value: 1.49e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLstadLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd14183    6 ERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHM----IQNEVSILRRVKHPNIVLLIEEMDMPTELYL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALL-ATVDNSAPVKLGGFGSAIQ 168
Cdd:cd14183   82 VMELVKGGDL-FDAITSTNK---YTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyEHQDGSKSLKLGDFGLATV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPGTRETIethgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG---VRLQQSVARGRLSFEAPEWK 245
Cdd:cd14183  158 VDGPLYTV-----CGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGddqEVLFDQILMGQVDFPSPYWD 232
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442620344 246 SISANAKDLVMKMLAANPHHRLSITEVLDHPWIRD 280
Cdd:cd14183  233 NVSDSAKELITMMLQVDVDQRYSALQVLEHPWVND 267
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
12-277 1.82e-44

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 161.28  E-value: 1.82e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14079    4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLD--MEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFG-SAIQLP 170
Cdd:cd14079   82 EYVSGGELFDYIVQKGR----LSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLL---DSNMNVKIADFGlSNIMRD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GtrETIEThgRVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGrlSFEAPEWksIS 248
Cdd:cd14079  155 G--EFLKT--SCGSPNYAAPEVISGKLYaGPEVDVWSCGVILYALLCGSLPFDDEHIpNLFKKIKSG--IYTIPSH--LS 226
                        250       260
                 ....*....|....*....|....*....
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14079  227 PGARDLIKRMLVVDPLKRITIPEIRQHPW 255
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
12-289 6.07e-44

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 161.58  E-value: 6.07e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELC---EVIGKGPFSIVRRCIHRESNQQFAVKIVDvAKFTASPGLSTADLKreatICHmlKHPHIVELLETYSSEGMLY 88
Cdd:cd14180    5 YELDleePALGEGSFSVCRKCRHRQSGQEYAVKIIS-RRMEANTQREVAALR----LCQ--SHPNIVALHEVLHDQYHTY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSAIQ 168
Cdd:cd14180   78 LVMELLRGGELLDRIKKKAR----FSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGAVLKVIDFGFARL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPGTRETIEThgrvgcP----HYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGS--------GVRLQQSVARGR 236
Cdd:cd14180  154 RPQGSRPLQT------PcftlQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKrgkmfhnhAADIMHKIKEGD 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442620344 237 LSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKLQRTHL 289
Cdd:cd14180  228 FSLEGEAWKGVSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQGGSALSSTPL 280
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
8-278 9.00e-43

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 157.13  E-value: 9.00e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYEL-CEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLK-HPHIVELLETYSSEG 85
Cdd:cd14106    5 INEVYTVeSTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQD---CRNEILHEIAVLELCKdCPRVVNLHEVYETRS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 MLYMVFEFMEGSdlcfEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFG- 164
Cdd:cd14106   82 ELILILELAAGG----ELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGDIKLCDFGi 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 SAIQLPGT--RETIethgrvGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVrlQQS---VARGRLSF 239
Cdd:cd14106  158 SRVIGEGEeiREIL------GTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDK--QETflnISQCNLDF 229
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 442620344 240 EAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14106  230 PEELFKDVSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
18-277 1.32e-42

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 155.75  E-value: 1.32e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDvaKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLR--KKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLcFEVVRRAvagFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPGTRETie 177
Cdd:cd05123   79 EL-FSHLSKE---GRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILL---DSDGHIKLTDFGLAKELSSDGDR-- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 178 THGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRLSFeaPEwkSISANAKDLVM 256
Cdd:cd05123  150 TYTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRkEIYEKILKSPLKF--PE--YVSPEAKSLIS 225
                        250       260
                 ....*....|....*....|....
gi 442620344 257 KMLAANPHHRL---SITEVLDHPW 277
Cdd:cd05123  226 GLLQKDPTKRLgsgGAEEIKAHPF 249
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
12-278 2.59e-42

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 155.40  E-value: 2.59e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVdvAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14099    3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVV--PKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EfmegsdLC-----FEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSA 166
Cdd:cd14099   81 E------LCsngslMELLKRRKA---LTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFL---DENMNVKIGDFGLA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQL--PGTRE-TIethgrVGCPHYMAPEVVTRRLyGKGC--DVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARgRLSFEA 241
Cdd:cd14099  149 ARLeyDGERKkTL-----CGTPNYIAPEVLEKKK-GHSFevDIWSLGVILYTLLVGKPPFETSDVKETYKRIK-KNEYSF 221
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 442620344 242 PEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14099  222 PSHLSISDEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
12-277 3.77e-42

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 154.94  E-value: 3.77e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGlSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14098    2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDK-NLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLC-FEVVRRAVAGFVYSEAVachymRQILEALRYCHENDILHRDVRPACALLaTVDNSAPVKLGGFGSAiQLP 170
Cdd:cd14098   81 EYVEGGDLMdFIMAWGAIPEQHARELT-----KQILEAMAYTHSMGITHRDLKPENILI-TQDDPVIVKISDFGLA-KVI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRETIETHgrVGCPHYMAPEVVTRR------LYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGRLSFEAPE 243
Cdd:cd14098  154 HTGTFLVTF--CGTMAYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLTGALPFDGSSqLPVEKRIRKGRYTQPPLV 231
                        250       260       270
                 ....*....|....*....|....*....|....
gi 442620344 244 WKSISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14098  232 DFNISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
10-279 8.73e-42

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 154.80  E-value: 8.73e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELC-EVIGKGPFSIVRRCIHRESNQQFAVKIVDvakftASPGLSTADLKREA-TICHMLKHPHIVELLETYSSEGML 87
Cdd:cd14174    1 DLYRLTdELLGEGAYAKVQGCVSLQNGKEYAVKIIE-----KNAGHSRSRVFREVeTLYQCQGNKNILELIEFFEDDTRF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGF--GS 165
Cdd:cd14174   76 YLVFEKLRGGSILAHIQKRKH----FNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSPVKICDFdlGS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 166 AIQLPGTRETIET---HGRVGCPHYMAPEVV-----TRRLYGKGCDVWGAGVMLHVLLSGRLPFLGS-GV---------- 226
Cdd:cd14174  152 GVKLNSACTPITTpelTTPCGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGHcGTdcgwdrgevc 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 227 -----RLQQSVARGRLSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIR 279
Cdd:cd14174  232 rvcqnKLFESIQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
11-278 9.00e-42

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 153.51  E-value: 9.00e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  11 VYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglstADLKREATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKK-----ESILNEIAILKKCKHPNIVKYYGSYLKKDELWIV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLcfevvRRAVAGFVYS---EAVAChYMRQILEALRYCHENDILHRDVRPACALLATvdnSAPVKLGGFGSAI 167
Cdd:cd05122   76 MEFCSGGSL-----KDLLKNTNKTlteQQIAY-VCKEVLKGLEYLHSHGIIHRDIKAANILLTS---DGEVKLIDFGLSA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLPGTRETIEthgRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGrlsfEAPEWKS 246
Cdd:cd05122  147 QLSDGKTRNT---FVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPpMKALFLIATN----GPPGLRN 219
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442620344 247 I---SANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd05122  220 PkkwSKEFKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
12-278 9.40e-42

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 153.32  E-value: 9.40e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14071    2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEE---NLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFG-SAIQLP 170
Cdd:cd14071   79 EYASNGEI-FDYLAQHGR---MSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLL---DANMNIKIADFGfSNFFKP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GtrETIETHgrVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGRlsFEAPEWksIS 248
Cdd:cd14071  152 G--ELLKTW--CGSPPYAAPEVFEGKEYeGPQLDIWSLGVVLYVLVCGALPFDGSTLQtLRDRVLSGR--FRIPFF--MS 223
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14071  224 TDCEHLIRRMLVLDPSKRLTIEQIKKHKWM 253
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-286 1.60e-41

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 153.51  E-value: 1.60e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  11 VYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLstadLKREATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd14169    4 VYELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAM----VENEIAVLRRINHENIVSLEDIYESPTHLYLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFG-SAIQL 169
Cdd:cd14169   80 MELVTGGELFDRIIERGS----YTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFEDSKIMISDFGlSKIEA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PGTRETIethgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEWKSIS 248
Cdd:cd14169  156 QGMLSTA-----CGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDeNDSELFNQILKAEYEFDSPYWDDIS 230
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKLQR 286
Cdd:cd14169  231 ESAKDFIRHLLERDPEKRFTCEQALQHPWISGDTALDR 268
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
9-278 6.02e-41

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 151.87  E-value: 6.02e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   9 DDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASP-GLSTADLKREATICHMLKHPHIVELLETYSSEGML 87
Cdd:cd14105    4 EDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASRrGVSREDIEREVSILRQVLHPNIITLHDVFENKTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAP-VKLGGFGSA 166
Cdd:cd14105   84 VLILELVAGGEL-FDFLAEKES---LSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPIPrIKLIDFGLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLPGTRETIETHGrvgCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEWK 245
Cdd:cd14105  160 HKIEDGNEFKNIFG---TPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGdTKQETLANITAVNYDFDDEYFS 236
                        250       260       270
                 ....*....|....*....|....*....|...
gi 442620344 246 SISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14105  237 NTSELAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
9-278 9.64e-41

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 151.33  E-value: 9.64e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   9 DDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASP-GLSTADLKREATICHMLKHPHIVELLETYSSEGML 87
Cdd:cd14194    4 DDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRrGVSREDIEREVSILKEIQHPNVITLHEVYENKTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatVDNSAP---VKLGGFG 164
Cdd:cd14194   84 ILILELVAGGEL-FDFLAEKES---LTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIML--LDRNVPkprIKIIDFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 SAIQLPGTRETIEThgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGRLSFEAPE 243
Cdd:cd14194  158 LAHKIDFGNEFKNI---FGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQeTLANVSAVNYEFEDEY 234
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442620344 244 WKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14194  235 FSNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
PDZ_MPP1-like cd10830
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 ...
494-574 1.19e-40

PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1, and related domains. MPP1 (also known as MAGUK p55 subfamily member 1, erythrocyte membrane protein p55, EMP55) is a membrane-associated guanylate kinase (MAGUK)-like protein which forms a complex with protein 4.1 and glycophorin C (GPC) at the cytoplasmic face of the plasma membrane; this complex is essential for cytoskeleton-membrane linkage in erythrocytes and many non-erythroid cells, and participates in the determination of membrane stability and cell shape. MPP1, by interacting with various scaffold proteins and cytoskeletal proteins in the postsynaptic density, also plays an important role in organizing synaptic and non-synaptic structures. MPP1 is also a component of the Crumbs protein complex in the mammalian retina and may link the Usher protein network and the Crumbs protein complex. The MPP1 PDZ domain binding partners include GPC, ABCC4, and CADM1/Necl-2/SynCAM1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467266 [Multi-domain]  Cd Length: 81  Bit Score: 143.85  E-value: 1.19e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 494 RLVQFQKNTDEPMGITLKMTEDGRCIVARIMHGGMIHRQATLHVGDEIREINGQPVQHQSVGQLQRMLREARGSVTFKIV 573
Cdd:cd10830    1 RLVQFEKNTEEPMGITLKLNEKQSCIVARILHGGMIHRQGSLHVGDEILEINGKSVTNHSVDQLQKMLKETKGMVSLKVI 80

                 .
gi 442620344 574 P 574
Cdd:cd10830   81 P 81
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
12-278 4.66e-40

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 148.82  E-value: 4.66e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14072    2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPS---SLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSdlcfEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQL-P 170
Cdd:cd14072   79 EYASGG----EVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLL---DADMNIKIADFGFSNEFtP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRetIETHgrVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGRlsFEAPEWksIS 248
Cdd:cd14072  152 GNK--LDTF--CGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPFDGQNLKeLRERVLRGK--YRIPFY--MS 223
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14072  224 TDCENLLKKFLVLNPSKRGTLEQIMKDRWM 253
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
18-278 6.91e-40

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 149.53  E-value: 6.91e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVdvakftaspgLSTADLKREATIcHML--KHPHIVELLETY----------SSEG 85
Cdd:cd14171   14 LGTGISGPVRVCVKKSTGERFALKIL----------LDRPKARTEVRL-HMMcsGHPNIVQIYDVYansvqfpgesSPRA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 MLYMVFEFMEGSDLCFEVVRRAvaGFVYSEAVAchYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGS 165
Cdd:cd14171   83 RLLIVMELMEGGELFDRISQHR--HFTEKQAAQ--YTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAPIKLCDFGF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 166 AIQLPGTRETIEThgrvgCPHYMAPEVV-----------------TRRLYGKGCDVWGAGVMLHVLLSGRLPFLGS---- 224
Cdd:cd14171  159 AKVDQGDLMTPQF-----TPYYVAPQVLeaqrrhrkersgiptspTPYTYDKSCDMWSLGVIIYIMLCGYPPFYSEhpsr 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442620344 225 --GVRLQQSVARGRLSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14171  234 tiTKDMKRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
10-278 9.57e-40

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 148.21  E-value: 9.57e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELC-EVIGKGPFSIVRRCIHRESNQQFAVKIVdvakFTASPGLSTADLKREATIChmlkhPHIVELLETYS----SE 84
Cdd:cd14172    3 DDYKLSkQVLGLGVNGKVLECFHRRTGQKCALKLL----YDSPKARREVEHHWRASGG-----PHIVHILDVYEnmhhGK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  85 GMLYMVFEFMEGSDLCFEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFG 164
Cdd:cd14172   74 RCLLIIMECMEGGELFSRIQERGDQAF--TEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVLKLTDFG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 SAiqlpgTRETIETHGRVGC--PHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFL---GSGVR--LQQSVARGRL 237
Cdd:cd14172  152 FA-----KETTVQNALQTPCytPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYsntGQAISpgMKRRIRMGQY 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 442620344 238 SFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14172  227 GFPNPEWAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
9-278 1.05e-39

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 148.18  E-value: 1.05e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   9 DDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASP-GLSTADLKREATICHMLKHPHIVELLETYSSEGML 87
Cdd:cd14196    4 EDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrGVSREEIEREVSILRQVLHPNIITLHDVYENRTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatVDNSAP---VKLGGFG 164
Cdd:cd14196   84 VLILELVSGGEL-FDFLAQKES---LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIML--LDKNIPiphIKLIDFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 SAIQLpgtRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQS-VARGRLSFEAPE 243
Cdd:cd14196  158 LAHEI---EDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLAnITAVSYDFDEEF 234
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442620344 244 WKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14196  235 FSHTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
12-278 1.35e-39

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 147.40  E-value: 1.35e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05578    2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKD--SVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPG 171
Cdd:cd05578   80 DLLLGGDLRYHLQQKVK----FSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILL---DEQGHVHITDFNIATKLTD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIEThgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWKSISANA 251
Cdd:cd05578  153 GTLATST---SGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRAKFETASVLYPAGWSEEA 229
                        250       260
                 ....*....|....*....|....*...
gi 442620344 252 KDLVMKMLAANPHHRLS-ITEVLDHPWI 278
Cdd:cd05578  230 IDLINKLLERDPQKRLGdLSDLKNHPYF 257
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
11-278 1.60e-39

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 146.97  E-value: 1.60e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  11 VYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglstaDLKREATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd06614    1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKE------LIINEILIMKECKHPNIVDYYDSYLVGDELWVV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLCfEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLp 170
Cdd:cd06614   75 MEYMDGGSLT-DIITQNPVRM--NESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILL---SKDGSVKLADFGFAAQL- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 gTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVR-LQQSVARGRLSFEAPEwkSIS 248
Cdd:cd06614  148 -TKEKSKRNSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEePPLRaLFLITTKGIPPLKNPE--KWS 224
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06614  225 PEFKDFLNKCLVKDPEKRPSAEELLQHPFL 254
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
18-282 1.85e-39

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 147.36  E-value: 1.85e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIvdvakftaspgLSTADLKR---------EATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd05579    1 ISRGAYGRVYLAKKKSTGDLYAIKV-----------IKKRDMIRknqvdsvlaERNILSQAQNPFVVKLYYSFQGKKNLY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDL--------CFEvvrravagfvysEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKL 160
Cdd:cd05579   70 LVMEYLPGGDLysllenvgALD------------EDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILI---DANGHLKL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 161 GGFG-------------SAIQLPGTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR 227
Cdd:cd05579  135 TDFGlskvglvrrqiklSIQKKSNGAPEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPE 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 228 -LQQSVARGRLSFeaPEWKSISANAKDLVMKMLAANPHHRL---SITEVLDHPWIRDRD 282
Cdd:cd05579  215 eIFQNILNGKIEW--PEDPEVSDEAKDLISKLLTPDPEKRLgakGIEEIKNHPFFKGID 271
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
18-278 5.46e-39

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 146.35  E-value: 5.46e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKF------------------TASPGLSTADLKREATICHMLKHPHIVELLE 79
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLlkqagffrrppprrkpgaLGKPLDPLDRVYREIAILKKLDHPNVVKLVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  80 TYS--SEGMLYMVFEFMEGSDlcfevVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPAcALLATVDNSap 157
Cdd:cd14118   82 VLDdpNEDNLYMVFELVDKGA-----VMEVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPS-NLLLGDDGH-- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 158 VKLGGFGSAIQLPGTRETIEThgRVGCPHYMAPEVVT--RRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVA 233
Cdd:cd14118  154 VKIADFGVSNEFEGDDALLSS--TAGTPAFMAPEALSesRKKFsGKALDIWAMGVTLYCFVFGRCPFEDDHIlGLHEKIK 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 442620344 234 RGRLSFeaPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14118  232 TDPVVF--PDDPVVSEQLKDLILRMLDKNPSERITLPEIKEHPWV 274
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
9-279 6.48e-39

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 145.92  E-value: 6.48e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   9 DDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASP-GLSTADLKREATICHMLKHPHIVELLETYSSEGML 87
Cdd:cd14195    4 EDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRrGVSREEIEREVNILREIQHPNIITLHDIFENKTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatVDNSAP---VKLGGFG 164
Cdd:cd14195   84 VLILELVSGGEL-FDFLAEKES---LTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIML--LDKNVPnprIKLIDFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 SAIQLPGTRETIEThgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPE 243
Cdd:cd14195  158 IAHKIEAGNEFKNI---FGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGeTKQETLTNISAVNYDFDEEY 234
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 442620344 244 WKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIR 279
Cdd:cd14195  235 FSNTSELAKDFIRRLLVKDPKKRMTIAQSLEHSWIK 270
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
12-278 1.22e-38

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 144.83  E-value: 1.22e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFtaspGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14078    5 YELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKAL----GDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEVVrraVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFG-SAIQLP 170
Cdd:cd14078   81 EYCPGGEL-FDYI---VAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLL---DEDQNLKLIDFGlCAKPKG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRETIETHgrVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRlsFEAPEWksIS 248
Cdd:cd14078  154 GMDHHLETC--CGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNVmALYRKIQSGK--YEEPEW--LS 227
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14078  228 PSSKLLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-311 2.53e-38

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 145.19  E-value: 2.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglsTADLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd14168   10 KIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGK----ESSIENEIAVLRKIKHENIVALEDIYESPNHLYL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLCFEVVRRavaGFvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSAiQL 169
Cdd:cd14168   86 VMQLVSGGELFDRIVEK---GF-YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMISDFGLS-KM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PGTRETIEThgRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGRLSFEAPEWKSIS 248
Cdd:cd14168  161 EGKGDVMST--ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENdSKLFEQILKADYEFDSPYWDDIS 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKLQRTHLADTVEELKRYNARRKLKGAVQA 311
Cdd:cd14168  239 DSAKDFIRNLMEKDPNKRYTCEQALRHPWIAGDTALCKNIHESVSAQIRKNFAKSKWRQAFNA 301
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
16-277 2.59e-38

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 143.71  E-value: 2.59e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFtasPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFME 95
Cdd:cd14082    9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRF---PTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 GSDLcfEVVRRAVAGFVySEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSA--IQLPGTR 173
Cdd:cd14082   86 GDML--EMILSSEKGRL-PERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQVKLCDFGFAriIGEKSFR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 174 ETIethgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFlGSGVRLQQSVARGRLSFEAPEWKSISANAKD 253
Cdd:cd14082  163 RSV-----VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-NEDEDINDQIQNAAFMYPPNPWKEISPDAID 236
                        250       260
                 ....*....|....*....|....
gi 442620344 254 LVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14082  237 LINNLLQVKMRKRYSVDKSLSHPW 260
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
12-279 3.93e-38

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 143.89  E-value: 3.93e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTAdlKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05581    3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYV--TIEKEVLSRLAHPGIVKLYYTFQDESKLYFVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPG 171
Cdd:cd05581   81 EYAPNGDL-LEYIRKYGS---LDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILL---DEDMHIKITDFGTAKVLGP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHGR---------------VGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG--VRLQQSVAr 234
Cdd:cd05581  154 DSSPESTKGDadsqiaynqaraasfVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNeyLTFQKIVK- 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 442620344 235 grLSFEAPEwkSISANAKDLVMKMLAANPHHRLSITEVLDHPWIR 279
Cdd:cd05581  233 --LEYEFPE--NFPPDAKDLIQKLLVLDPSKRLGVNENGGYDELK 273
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
12-278 5.03e-38

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 142.76  E-value: 5.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVdVAKFtasPGLSTAD-----LKReatICHMLKHPHIVELLE--TYSSE 84
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKI-KNDF---RHPKAALreiklLKH---LNDVEGHPNIVKLLDvfEHRGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  85 GMLYMVFEFMeGSDLCfEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPAcALLATVDNSApVKLGGFG 164
Cdd:cd05118   74 NHLCLVFELM-GMNLY-ELIKDYPRGL--PLDLIKSYLYQLLQALDFLHSNGIIHRDLKPE-NILINLELGQ-LKLADFG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 SAIQLPGTRETiethGRVGCPHYMAPEV-VTRRLYGKGCDVWGAGVMLHVLLSGRlPFLGSGVRLQQSVARGRLsFEAPE 243
Cdd:cd05118  148 LARSFTSPPYT----PYVATRWYRAPEVlLGAKPYGSSIDIWSLGCILAELLTGR-PLFPGDSEVDQLAKIVRL-LGTPE 221
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442620344 244 wksisanAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd05118  222 -------ALDLLSKMLKYDPAKRITASQALAHPYF 249
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
494-574 1.01e-37

PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1-7 (also known as MAGUK p55 subfamily members 1-7), and related domains. MPPs comprise a subfamily of a larger group of multidomain proteins, namely, membrane-associated guanylate kinases (MAGUKs). MPPs form diverse protein complexes at the cell membranes, which are involved in a wide range of cellular processes, including establishing proper cell structure, polarity and cell adhesion. MPPs have only one PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467208 [Multi-domain]  Cd Length: 80  Bit Score: 135.47  E-value: 1.01e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 494 RLVQFQKNTDEPMGITLKMTEDgRCIVARIMHGGMIHRQATLHVGDEIREINGQPVQHQSVGQLQRMLREARGSVTFKIV 573
Cdd:cd06726    1 RLVEFEKARDEPLGATIKMEED-SVIVARILHGGMAHRSGLLHVGDEILEINGIPVSGKTVDELQKLLSSLSGSVTFKLI 79

                 .
gi 442620344 574 P 574
Cdd:cd06726   80 P 80
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
12-278 1.49e-37

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 142.24  E-value: 1.49e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVdvaKF-TASPGLSTADLkREATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKI---RLdNEEEGIPSTAL-REISLLKELKHPNIVKLLDVIHTENKLYLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEgSDL--CFEVVRRAVagfvySEAVACHYMRQILEALRYCHENDILHRDVRPAcALLATVDNSapVKLGGFGSA-- 166
Cdd:cd07829   77 FEYCD-QDLkkYLDKRPGPL-----PPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQ-NLLINRDGV--LKLADFGLAra 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLPGTRETIEthgrVGCPHYMAPEVVTR-RLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQ---------------- 229
Cdd:cd07829  148 FGIPLRTYTHE----VVTLWYRAPEILLGsKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQlfkifqilgtpteesw 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620344 230 ---QSVARGRLSFeaPEW---------KSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd07829  224 pgvTKLPDYKPTF--PKWpkndlekvlPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
SH3_CASK cd12081
Src Homology 3 domain of Calcium/calmodulin-dependent Serine protein Kinase; CASK is a ...
586-646 4.54e-37

Src Homology 3 domain of Calcium/calmodulin-dependent Serine protein Kinase; CASK is a scaffolding protein that is highly expressed in the mammalian nervous system and plays roles in synaptic protein targeting, neural development, and gene expression regulation. CASK interacts with many different binding partners including parkin, neurexin, syndecans, calcium channel proteins, caskin, among others, to perform specific functions in different subcellular locations. Disruption of the CASK gene in mice results in neonatal lethality while mutations in the human gene have been associated with X-linked mental retardation. Drosophila CASK is associated with both pre- and postsynaptic membranes and is crucial in synaptic transmission and vesicle cycling. CASK contains an N-terminal calmodulin-dependent kinase (CaMK)-like domain, two L27 domains, followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 213014  Cd Length: 62  Bit Score: 133.10  E-value: 4.54e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 586 FVRAQFDYNPLDDELIPCAQAGISFQVGDILQIISKDDHHWWQARLDT-VGGSAGLIPSPEL 646
Cdd:cd12081    1 YVRAQFEYDPLKDDLIPCKQAGIRFRVGDILQIISKDDHNWWQAKLENsKNGTAGLIPSPEL 62
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
12-278 4.83e-37

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 140.27  E-value: 4.83e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvakfTASPGLSTADLK--------------REATICHMLKHPHIVEL 77
Cdd:cd14077    3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIP----RASNAGLKKEREkrlekeisrdirtiREAALSSLLNHPHICRL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  78 LETYSSEGMLYMVFEFMEGSDLCFEVVRRAvagfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsap 157
Cdd:cd14077   79 RDFLRTPNHYYMLFEYVDGGQLLDYIISHG----KLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGN--- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 158 VKLGGFG-SAIQLPGTRetieTHGRVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVAR 234
Cdd:cd14077  152 IKIIDFGlSNLYDPRRL----LRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENMPaLHAKIKK 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 442620344 235 GRLSFeaPEWksISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14077  228 GKVEY--PSY--LSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
12-278 7.25e-37

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 139.61  E-value: 7.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvAKFTASPGLsTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14186    3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMID-KKAMQKAGM-VQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSAIQLPG 171
Cdd:cd14186   81 EMCHNGEMSRYLKNRKKP---FTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMN---IKIADFGLATQLKM 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIEThgRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR--LQQSVARgrlSFEAPEWksISA 249
Cdd:cd14186  155 PHEKHFT--MCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKntLNKVVLA---DYEMPAF--LSR 227
                        250       260
                 ....*....|....*....|....*....
gi 442620344 250 NAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14186  228 EAQDLIHQLLRKNPADRLSLSSVLDHPFM 256
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
12-278 1.03e-36

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 139.09  E-value: 1.03e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTaspGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14074    5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLD---DVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatVDNSAPVKLGGFG-SAIQLP 170
Cdd:cd14074   82 ELGDGGDM-YDYIMKHENGL--NEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVF--FEKQGLVKLTDFGfSNKFQP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GtrETIEThgRVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFlgsgvrlQQSVARGRLS------FEAPE 243
Cdd:cd14074  157 G--EKLET--SCGSLAYSAPEILLGDEYdAPAVDIWSLGVILYMLVCGQPPF-------QEANDSETLTmimdckYTVPA 225
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442620344 244 wkSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14074  226 --HVSPECKDLIRRMLIRDPKKRASLEEIENHPWL 258
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
8-278 1.80e-36

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 138.57  E-value: 1.80e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvAKFtaspgLSTADLKREATICHMLKHPHIVELLETYSSEGML 87
Cdd:cd14113    5 FDSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVN-KKL-----MKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLCFEVVRravAGFVYSEAVAChYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSAI 167
Cdd:cd14113   79 ILVLEMADQGRLLDYVVR---WGNLTEEKIRF-YLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTIKLADFGDAV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLpgtRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRlQQSVARGRLSFEAPE--WK 245
Cdd:cd14113  155 QL---NTTYYIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVE-ETCLNICRLDFSFPDdyFK 230
                        250       260       270
                 ....*....|....*....|....*....|...
gi 442620344 246 SISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14113  231 GVSQKAKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
12-282 3.20e-36

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 138.87  E-value: 3.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFtaspglstADLK------REATICHMLKHPHIVELLETYSSEG 85
Cdd:cd05580    3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKI--------IKLKqvehvlNEKRILSEVRHPFIVNLLGSFQDDR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 MLYMVFEFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGS 165
Cdd:cd05580   75 NLYMVMEYVPGGEL-FSLLRRSGR---FPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLL---DSDGHIKITDFGF 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 166 AIQLPGtretiETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGRLSFeaPEW 244
Cdd:cd05580  148 AKRVKD-----RTYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENpMKIYEKILEGKIRF--PSF 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442620344 245 ksISANAKDLVMKMLAANPHHRL-----SITEVLDHPWIRDRD 282
Cdd:cd05580  221 --FDPDAKDLIKRLLVVDLTKRLgnlknGVEDIKNHPWFAGID 261
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
16-277 3.28e-36

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 137.42  E-value: 3.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQF-AVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFM 94
Cdd:cd14121    1 EKLGSGTYATVYKAYRKSGAREVvAVKCVSKSSLNKA---STENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  95 EGSDLC-FEVVRRAVagfvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsaPV-KLGGFGSAIQLpgt 172
Cdd:cd14121   78 SGGDLSrFIRSRRTL-----PESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYN--PVlKLADFGFAQHL--- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 173 RETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFlgSGVRLQQSVARGRLS--FEAPEWKSISAN 250
Cdd:cd14121  148 KPNDEAHSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPF--ASRSFEELEEKIRSSkpIEIPTRPELSAD 225
                        250       260
                 ....*....|....*....|....*..
gi 442620344 251 AKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14121  226 CRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-278 3.72e-36

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 137.67  E-value: 3.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftaspgLSTAD---LKREATICHMLKHPHIVELLETY--SSEGM 86
Cdd:cd08217    2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGK------MSEKEkqqLVSEVNILRELKHPNIVRYYDRIvdRANTT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEGSDLCfEVVRRAVAGFVY-SEAVACHYMRQILEALRYCH-----ENDILHRDVRPACALLaTVDNSapVKL 160
Cdd:cd08217   76 LYIVMEYCEGGDLA-QLIKKCKKENQYiPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFL-DSDNN--VKL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 161 GGFGSAIQLpgTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGRLsf 239
Cdd:cd08217  152 GDFGLARVL--SHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANqLELAKKIKEGKF-- 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 442620344 240 eaPEWKSI-SANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd08217  228 --PRIPSRySSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
11-278 6.42e-36

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 136.59  E-value: 6.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  11 VYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd06627    1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKS---DLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYII 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLCfEVVRRaVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPAcALLATVDNSapVKLGGFGSAIQLp 170
Cdd:cd06627   78 LEYVENGSLA-SIIKK-FGKF--PESLVAVYIYQVLEGLAYLHEQGVIHRDIKGA-NILTTKDGL--VKLADFGVATKL- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 gTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGsgvrLQQSVARGRLSF--EAPEWKSIS 248
Cdd:cd06627  150 -NEVEKDENSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYD----LQPMAALFRIVQddHPPLPENIS 224
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06627  225 PELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
17-283 8.37e-36

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 136.57  E-value: 8.37e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIVdvakftasPGLSTAD----LKREATICHMLKHPHIVELLETYSSEGMLYMVFE 92
Cdd:cd06623    8 VLGQGSSGVVYKVRHKPTGKIYALKKI--------HVDGDEEfrkqLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  93 FMEGSDLcfEVVRRAVAGFvySEAVaCHYM-RQILEALRYCH-ENDILHRDVRPAcALLATVDNSapVKLGGFGSAIQLP 170
Cdd:cd06623   80 YMDGGSL--ADLLKKVGKI--PEPV-LAYIaRQILKGLDYLHtKRHIIHRDIKPS-NLLINSKGE--VKIADFGISKVLE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRETIETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR----LQQSVargrLSFEAPEWKS 246
Cdd:cd06623  152 NTLDQCNTF--VGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPsffeLMQAI----CDGPPPSLPA 225
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 442620344 247 --ISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDK 283
Cdd:cd06623  226 eeFSPEFRDFISACLQKDPKKRPSAAELLQHPFIKKADN 264
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
11-277 1.73e-35

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 135.79  E-value: 1.73e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  11 VYELCEVIGKGPFSIVRRCIHRESNQQFAvkivdvAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd14107    3 VYEVKEEIGRGTFGFVKRVTHKGNGECCA------AKFIPLRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLCFEVVRRAVAgfvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSaPVKLGGFGSAIQLP 170
Cdd:cd14107   77 LELCSSEELLDRLFLKGVV----TEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRE-DIKICDFGFAQEIT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRETietHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQ-QSVARGRLSFEAPEWKSISA 249
Cdd:cd14107  152 PSEHQ---FSKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATlLNVAEGVVSWDTPEITHLSE 228
                        250       260
                 ....*....|....*....|....*...
gi 442620344 250 NAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14107  229 DAKDFIKRVLQPDPEKRPSASECLSHEW 256
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
9-297 1.83e-35

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 137.09  E-value: 1.83e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   9 DDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIV-DVAKftaspGLSTADLKREATIChmlkhPHIVELLETY----SS 83
Cdd:cd14170    1 DDYKVTSQVLGLGINGKVLQIFNKRTQEKFALKMLqDCPK-----ARREVELHWRASQC-----PHIVRIVDVYenlyAG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGMLYMVFEFMEGSDLCFEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGF 163
Cdd:cd14170   71 RKCLLIVMECLDGGELFSRIQDRGDQAF--TEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDF 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 164 GSAiqlpgtRETIeTHGRVGCP----HYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF-----LGSGVRLQQSVAR 234
Cdd:cd14170  149 GFA------KETT-SHNSLTTPcytpYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFysnhgLAISPGMKTRIRM 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620344 235 GRLSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKLQRT--HLADTVEELK 297
Cdd:cd14170  222 GQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTplHTSRVLKEDK 286
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
17-282 1.87e-35

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 137.54  E-value: 1.87e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFS---IVRRCIHRESNQQFAVKIVDVAKFTASPGlSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEF 93
Cdd:cd05584    3 VLGKGGYGkvfQVRKTTGSDKGKIFAMKVLKKASIVRNQK-DTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLILEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  94 MEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAiqlpgtR 173
Cdd:cd05584   82 LSGGELFMHLEREGI----FMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILL---DAQGHVKLTDFGLC------K 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 174 ETIE----THGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQ-QSVARGRLSFeaPEWksIS 248
Cdd:cd05584  149 ESIHdgtvTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTiDKILKGKLNL--PPY--LT 224
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 442620344 249 ANAKDLVMKMLAANPHHRLSIT-----EVLDHPWIRDRD 282
Cdd:cd05584  225 NEARDLLKKLLKRNVSSRLGSGpgdaeEIKAHPFFRHIN 263
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
10-278 4.22e-35

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 134.70  E-value: 4.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpGLStADLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd14116    5 EDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKA-GVE-HQLRREVEIQSHLRHPNILRLYGYFHDATRVYL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvdnSAPVKLGGFGSAIQL 169
Cdd:cd14116   83 ILEYAPLGTVYRELQKLSK----FDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGS---AGELKIADFGWSVHA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PGTRETIethgRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFlgSGVRLQQSVAR-GRLSFEAPEWksIS 248
Cdd:cd14116  156 PSSRRTT----LCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPF--EANTYQETYKRiSRVEFTFPDF--VT 227
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14116  228 EGARDLISRLLKHNPSQRPMLREVLEHPWI 257
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
12-276 6.84e-35

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 133.67  E-value: 6.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADlkrEATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd08530    2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREDSVN---EIRLLASVNHPNIIRYKEAFLDGNRLCIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSAIQLpg 171
Cdd:cd08530   79 EYAPFGDLSKLISKRKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDL---VKIGDLGISKVL-- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIEThgRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEWksiSAN 250
Cdd:cd08530  154 KKNLAKT--QIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEArTMQELRYKVCRGKFPPIPPVY---SQD 228
                        250       260
                 ....*....|....*....|....*.
gi 442620344 251 AKDLVMKMLAANPHHRLSITEVLDHP 276
Cdd:cd08530  229 LQQIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
12-278 7.30e-35

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 133.67  E-value: 7.30e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLstADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDM--VRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAiQLPG 171
Cdd:cd14073   81 EYASGGELYDYISERRR----LPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILL---DQNGNAKIADFGLS-NLYS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHgrVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRlsFEAPEWKSisa 249
Cdd:cd14073  153 KDKLLQTF--CGSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDFkRLVKQISSGD--YREPTQPS--- 225
                        250       260
                 ....*....|....*....|....*....
gi 442620344 250 NAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14073  226 DASGLIRWMLTVNPKRRATIEDIANHWWV 254
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
18-277 9.66e-35

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 133.54  E-value: 9.66e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGlSTADLKREATICHMLKHPHIVELLETYSSE--GMLYMVFEFME 95
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRIPN-GEANVKREIQILRRLNHRNVIKLVDVLYNEekQKLYMVMEYCV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 GSdLCFEVVRRAVAGFVYSEAVacHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSAIQLPGTRET 175
Cdd:cd14119   80 GG-LQEMLDSAPDKRLPIWQAH--GYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGT---LKISDFGVAEALDLFAED 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 176 IETHGRVGCPHYMAPEVV--TRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGrlSFEAPEWksISANAK 252
Cdd:cd14119  154 DTCTTSQGSPAFQPPEIAngQDSFSGFKVDIWSAGVTLYNMTTGKYPFEGDNIyKLFENIGKG--EYTIPDD--VDPDLQ 229
                        250       260
                 ....*....|....*....|....*
gi 442620344 253 DLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14119  230 DLLRGMLEKDPEKRFTIEQIRQHPW 254
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
10-277 1.22e-34

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 133.10  E-value: 1.22e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAvkivdvAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd14108    2 DYYDIHKEIGRGAFSYLRRVKEKSSDLSFA------AKFIPVRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVII 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEfmegsdLCFE-VVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvDNSAPVKLGGFGSAIQ 168
Cdd:cd14108   76 VTE------LCHEeLLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMAD-QKTDQVRICDFGNAQE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 L-PGTretiETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARG-RLSFEAPEWKS 246
Cdd:cd14108  149 LtPNE----PQYCKYGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNyNVAFEESMFKD 224
                        250       260       270
                 ....*....|....*....|....*....|.
gi 442620344 247 ISANAKDLVMKMLAANpHHRLSITEVLDHPW 277
Cdd:cd14108  225 LCREAKGFIIKVLVSD-RLRPDAEETLEHPW 254
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
10-278 1.42e-34

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 132.76  E-value: 1.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKivdvakFTASPGLSTAD---LKREATICHMLKHPHIVELLETYSSEGM 86
Cdd:cd14002    1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALK------FIPKRGKSEKElrnLRQEIEILRKLNHPNIIEMLDSFETKKE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEG------SD---LCFEVVRRavagfvyseaVAChymrQILEALRYCHENDILHRDVRPACALLatvDNSAP 157
Cdd:cd14002   75 FVVVTEYAQGelfqilEDdgtLPEEEVRS----------IAK----QLVSALHYLHSNRIIHRDMKPQNILI---GKGGV 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 158 VKLGGFGSAIQLpgTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFL-GSGVRLQQSVARGR 236
Cdd:cd14002  138 VKLCDFGFARAM--SCNTLVLTSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYtNSIYQLVQMIVKDP 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 442620344 237 LSFEapewKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14002  216 VKWP----SNMSPEFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
12-278 2.14e-34

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 132.60  E-value: 2.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftASPGLSTADLKREATICHMLKHPHIVELLETY-SSEGMLYMV 90
Cdd:cd14165    3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKK--APDDFVEKFLPRELEILARLNHKSIIKTYEIFeTSDGKVYIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQL- 169
Cdd:cd14165   81 MELGVQGDL-LEFIKLRGA---LPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLL---DKDFNIKLTDFGFSKRCl 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 -PGTRETIETHGRVGCPHYMAPEVVTRRLYG-KGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVA-RGRLSFeaPEWKS 246
Cdd:cd14165  154 rDENGRIVLSKTFCGSAAYAAPEVLQGIPYDpRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQkEHRVRF--PRSKN 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 442620344 247 ISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14165  232 LTSECKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
18-277 2.35e-34

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 132.01  E-value: 2.35e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKivdvakFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVK------FVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLCFEVVRRAVagfVYSEAVAcHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSAIQLPGTRETie 177
Cdd:cd14115   75 RLLDYLMNHDE---LMEEKVA-FYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHRHV-- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 178 tHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEWKSISANAKDLVM 256
Cdd:cd14115  149 -HHLLGNPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDeSKEETCINVCRVDFSFPDEYFGDVSQAARDFIN 227
                        250       260
                 ....*....|....*....|.
gi 442620344 257 KMLAANPHHRLSITEVLDHPW 277
Cdd:cd14115  228 VILQEDPRRRPTAATCLQHPW 248
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
12-277 3.11e-34

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 132.83  E-value: 3.11e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKivdvaKFTASPglSTADLK----REATICHMLKHPHIVELLETYSSEGML 87
Cdd:cd07833    3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIK-----KFKESE--DDEDVKktalREVKVLRQLRHENIVNLKEAFRRKGRL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLcfEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAI 167
Cdd:cd07833   76 YLVFEYVERTLL--ELLEASPGGL--PPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENIL---VSESGVLKLCDFGFAR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLPGTRETIETHgRVGCPHYMAPEV-VTRRLYGKGCDVWGAGVMLHVLLSGRLPF---------------LGSGVRLQQS 231
Cdd:cd07833  149 ALTARPASPLTD-YVATRWYRAPELlVGDTNYGKPVDVWAIGCIMAELLDGEPLFpgdsdidqlyliqkcLGPLPPSHQE 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 232 VARG--------------RLSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07833  228 LFSSnprfagvafpepsqPESLERRYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPY 287
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
12-277 4.70e-34

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 131.65  E-value: 4.70e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvaKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14162    2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVS--KKKAPEDYLQKFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEVVRRAvaGFVySEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSA--IQL 169
Cdd:cd14162   80 ELAENGDL-LDYIRKN--GAL-PEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNN---LKITDFGFArgVMK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PGTRETIETHGRVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARgRLSFeaPEWKSI 247
Cdd:cd14162  153 TKDGKPKLSETYCGSYAYASPEILRGIPYdPFLSDIWSMGVVLYTMVYGRLPFDDSNLKvLLKQVQR-RVVF--PKNPTV 229
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 248 SANAKDLVMKMLAANPhHRLSITEVLDHPW 277
Cdd:cd14162  230 SEECKDLILRMLSPVK-KRITIEEIKRDPW 258
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
18-277 6.16e-34

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 131.19  E-value: 6.16e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVdvAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCV--KKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPGTRETie 177
Cdd:cd05572   79 EL-WTILRDRGL---FDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLL---DSNGYVKLVDFGFAKKLGSGRKT-- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 178 tHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG---VRLQQSVARGRLSFEAPewKSISANAKDL 254
Cdd:cd05572  150 -WTFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDedpMKIYNIILKGIDKIEFP--KYIDKNAKNL 226
                        250       260
                 ....*....|....*....|....*...
gi 442620344 255 VMKMLAANPHHRL-----SITEVLDHPW 277
Cdd:cd05572  227 IKQLLRRNPEERLgylkgGIRDIKKHKW 254
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
18-278 8.05e-34

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 130.89  E-value: 8.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRE--SNQQFAVKIVDVAKFTASPGLSTADLKREATICHMLKHPHIVE---LLETYSSEGMLymVFE 92
Cdd:cd13994    1 IGKGATSVVRIVTKKNprSGVLYAVKEYRRRDDESKRKDYVKRLTSEYIISSKLHHPNIVKvldLCQDLHGKWCL--VME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  93 FMEGSDLCFEVVRRAVAGFvysEAVAChYMRQILEALRYCHENDILHRDVRPACALLaTVDNSapVKLGGFGSAIQL--P 170
Cdd:cd13994   79 YCPGGDLFTLIEKADSLSL---EEKDC-FFKQILRGVAYLHSHGIAHRDLKPENILL-DEDGV--LKLTDFGTAEVFgmP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRETIETHGRVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPF---LGSGVRLQQSVARGRLSFEAPEW-- 244
Cdd:cd13994  152 AEKESPMSAGLCGSEPYMAPEVFTSGSYdGRAVDVWSCGIVLFALFTGRFPWrsaKKSDSAYKAYEKSGDFTNGPYEPie 231
                        250       260       270
                 ....*....|....*....|....*....|....
gi 442620344 245 KSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd13994  232 NLLPSECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
12-278 1.36e-33

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 130.84  E-value: 1.36e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGL------------------STADLKR---EATICHMLK 70
Cdd:cd14200    2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLKQYGFprrppprgskaaqgeqakPLAPLERvyqEIAILKKLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  71 HPHIVELLETYS--SEGMLYMVFEFMEGSDlcfevVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACAL 148
Cdd:cd14200   82 HVNIVKLIEVLDdpAEDNLYMVFDLLRKGP-----VMEVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 149 LAtvdNSAPVKLGGFGSAIQLPGTRETIEThgRVGCPHYMAPEVVT---RRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG 225
Cdd:cd14200  157 LG---DDGHVKIADFGVSNQFEGNDALLSS--TAGTPAFMAPETLSdsgQSFSGKALDVWAMGVTLYCFVYGKCPFIDEF 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442620344 226 V-RLQQSVARGRLSFeaPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14200  232 IlALHNKIKNKPVEF--PEEPEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
12-278 1.61e-33

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 130.86  E-value: 1.61e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKR---------------------EATICHMLK 70
Cdd:cd14199    4 YKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRQAGFPRRPPPRgaraapegctqprgpiervyqEIAILKKLD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  71 HPHIVELLETYS--SEGMLYMVFEfmegsdlcfeVVRRAVAGFV-----YSEAVACHYMRQILEALRYCHENDILHRDVR 143
Cdd:cd14199   84 HPNVVKLVEVLDdpSEDHLYMVFE----------LVKQGPVMEVptlkpLSEDQARFYFQDLIKGIEYLHYQKIIHRDVK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 144 PACALlatVDNSAPVKLGGFGSAIQLPGTRETIEThgRVGCPHYMAPEVV--TRRLY-GKGCDVWGAGVMLHVLLSGRLP 220
Cdd:cd14199  154 PSNLL---VGEDGHIKIADFGVSNEFEGSDALLTN--TVGTPAFMAPETLseTRKIFsGKALDVWAMGVTLYCFVFGQCP 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 221 FLGSGV-RLQQSVARGRLSFeaPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14199  229 FMDERIlSLHSKIKTQPLEF--PDQPDISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
12-277 2.51e-33

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 130.14  E-value: 2.51e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTAdlkREA-TICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd07832    2 YKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQAL---REIkALQACQGHPYVVKLRDVFPHGTGFVLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMeGSDLcFEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLP 170
Cdd:cd07832   79 FEYM-LSSL-SEVLRDEERPL--TEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLL---ISSTGVLKIADFGLARLFS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRETIETHgRVGCPHYMAPEVV-TRRLYGKGCDVWGAGVMLHVLLSGRLPFLGS-------------GVRLQQS---VA 233
Cdd:cd07832  152 EEDPRLYSH-QVATRWYRAPELLyGSRKYDEGVDLWAVGCIFAELLNGSPLFPGEndieqlaivlrtlGTPNEKTwpeLT 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442620344 234 R----GRLSF-EAP--EWKSI----SANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07832  231 SlpdyNKITFpESKgiRLEEIfpdcSPEAIDLLKGLLVYNPKKRLSAEEALRHPY 285
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
12-284 3.70e-33

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 131.09  E-value: 3.70e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIV---DVAKFTaspglSTADLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLkkrEILKMK-----QVQHVAQEKSILMELSHPFIVNMMCSFQDENRVY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAiq 168
Cdd:PTZ00263  95 FLLEFVVGGEL-FTHLRKAGR---FPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLL---DNKGHVKVTDFGFA-- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 lpgTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFeaPEWksI 247
Cdd:PTZ00263 166 ---KKVPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDdTPFRIYEKILAGRLKF--PNW--F 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 442620344 248 SANAKDLVMKMLAANPHHRL-----SITEVLDHPWIR--DRDKL 284
Cdd:PTZ00263 239 DGRARDLVKGLLQTDHTKRLgtlkgGVADVKNHPYFHgaNWDKL 282
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
16-278 4.21e-33

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 128.88  E-value: 4.21e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTaspglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFME 95
Cdd:cd14193   10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQK-----EKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 GSDLcFEvvRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDnSAPVKLGGFGSAIQLPgTRET 175
Cdd:cd14193   85 GGEL-FD--RIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSRE-ANQVKIIDFGLARRYK-PREK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 176 IETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGRLSFEAPEWKSISANAKDL 254
Cdd:cd14193  160 LRVN--FGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDdNETLNNILACQWDFEDEEFADISEEAKDF 237
                        250       260
                 ....*....|....*....|....
gi 442620344 255 VMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14193  238 ISKLLIKEKSWRMSASEALKHPWL 261
SH3_MPP1-like cd12035
Src Homology 3 domain of Membrane Protein, Palmitoylated 1 (or MAGUK p55 subfamily member 1) ...
586-646 4.48e-33

Src Homology 3 domain of Membrane Protein, Palmitoylated 1 (or MAGUK p55 subfamily member 1)-like proteins; This subfamily includes MPP1, CASK (Calcium/calmodulin-dependent Serine protein Kinase), Caenorhabditis elegans lin-2, and similar proteins. MPP1 and CASK are scaffolding proteins from the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). In addition, they also have the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. CASK and lin-2 also contain an N-terminal calmodulin-dependent kinase (CaMK)-like domain and two L27 domains. MPP1 is ubiquitously-expressed and plays roles in regulating neutrophil polarity, cell shape, hair cell development, and neural development and patterning of the retina. CASK is highly expressed in the mammalian nervous system and plays roles in synaptic protein targeting, neural development, and gene expression regulation. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212968  Cd Length: 62  Bit Score: 121.77  E-value: 4.48e-33
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 586 FVRAQFDYNPLDDELIPCAQAGISFQVGDILQIISKDDHHWWQARLDTVG-GSAGLIPSPEL 646
Cdd:cd12035    1 YVRAQFDYDPSKDDLIPCQQAGIAFKTGDILQIISKDDHNWWQARKPGASkEPAGLIPSPEL 62
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
12-278 6.77e-33

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 127.84  E-value: 6.77e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14075    4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQK---TQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvdnSAPVKLGGFG-SAIQLP 170
Cdd:cd14075   81 EYASGGELYTKISTEGK----LSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYAS---NNCVKVGDFGfSTHAKR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GtrETIETHgrVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRLSFeaPEWksIS 248
Cdd:cd14075  154 G--ETLNTF--CGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRAETVaKLKKCILEGTYTI--PSY--VS 225
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14075  226 EPCQELIRGILQPVPSDRYSIDEIKNSEWL 255
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
12-299 7.84e-33

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 128.52  E-value: 7.84e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvakftaspgLSTA-----DLKREATICHMLKHPHIVELLETYSSEGM 86
Cdd:cd06609    3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVID---------LEEAedeieDIQQEIQFLSQCDSPYITKYYGSFLKGSK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEGSDlCFEVVRRAvagfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVKLGGFGSA 166
Cdd:cd06609   74 LWIIMEYCGGGS-VLDLLKPG----PLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLS---EEGDVKLADFGVS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLpgTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFlgsgvrlqQSVARGRLSFEAP---- 242
Cdd:cd06609  146 GQL--TSTMSKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPL--------SDLHPMRVLFLIPknnp 215
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 243 ---EWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKlqRTHLADTVEELKRY 299
Cdd:cd06609  216 pslEGNKFSKPFKDFVELCLNKDPKERPSAKELLKHKFIKKAKK--TSYLTLLIERIKKW 273
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
8-278 8.24e-33

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 127.63  E-value: 8.24e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCE-VIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFtaspglstadLKREATICHMLKHPHIVELLETYSSEGM 86
Cdd:cd14109    1 VRELYEIGEeDEKRAAQGAPFHVTERSTGRNFLAQLRYGDPF----------LMREVDIHNSLDHPNIVQMHDAYDDEKL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVF-EFMEGSDLCFEVVRRAVAgfVYSEAVACHYMRQILEALRYCHENDILHRDVRPAcALLATVDNsapVKLGGFGS 165
Cdd:cd14109   71 AVTVIdNLASTIELVRDNLLPGKD--YYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPE-DILLQDDK---LKLADFGQ 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 166 AIQLpgTRETIETHGRvGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGRLSFEAPEW 244
Cdd:cd14109  145 SRRL--LRGKLTTLIY-GSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDReTLTNVRSGKWSFDSSPL 221
                        250       260       270
                 ....*....|....*....|....*....|....
gi 442620344 245 KSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14109  222 GNISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
12-278 1.22e-32

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 127.63  E-value: 1.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKfTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14070    4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKK-AKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAvagfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFG--SAIQL 169
Cdd:cd14070   83 ELCPGGNLMHRIYDKK----RLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDN---IKLIDFGlsNCAGI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PGTRETIEThgRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFL---GSGVRLQQSVARGRLSfeaPEWKS 246
Cdd:cd14070  156 LGYSDPFST--QCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTvepFSLRALHQKMVDKEMN---PLPTD 230
                        250       260       270
                 ....*....|....*....|....*....|..
gi 442620344 247 ISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14070  231 LSPGAISFLRSLLEPDPLKRPNIKQALANRWL 262
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
18-278 2.93e-32

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 126.65  E-value: 2.93e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVdvaKFTASPGLSTADLKREATICHMLKHPHIVEL--LETYSSEGMLYMvfEFME 95
Cdd:cd06626    8 IGEGTFGKVYTAVNLDTGELMAMKEI---RFQDNDPKTIKEIADEMKVLEGLDHPNLVRYygVEVHREEVYIFM--EYCQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 GSDLcFEVVRRavaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLpGTRET 175
Cdd:cd06626   83 EGTL-EELLRH---GRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFL---DSNGLIKLGDFGSAVKL-KNNTT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 176 IETHGR----VGCPHYMAPEVVTR-RLYGKG--CDVWGAGVMLHVLLSGRLP--FLGSGVRLQQSVARGRLSfEAPEWKS 246
Cdd:cd06626  155 TMAPGEvnslVGTPAYMAPEVITGnKGEGHGraADIWSLGCVVLEMATGKRPwsELDNEWAIMYHVGMGHKP-PIPDSLQ 233
                        250       260       270
                 ....*....|....*....|....*....|..
gi 442620344 247 ISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06626  234 LSPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
12-274 4.35e-32

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 125.85  E-value: 4.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVakFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd08224    2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQI--FEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLaTVDNSapVKLGGFGSAIQLpg 171
Cdd:cd08224   80 ELADAGDLSRLIKHFKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFI-TANGV--VKLGDLGLGRFF-- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARgrlsFEAPEWKSI---- 247
Cdd:cd08224  155 SSKTTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMNLYSLCKK----IEKCEYPPLpadl 230
                        250       260
                 ....*....|....*....|....*...
gi 442620344 248 -SANAKDLVMKMLAANPHHRLSITEVLD 274
Cdd:cd08224  231 ySQELRDLVAACIQPDPEKRPDISYVLD 258
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-278 4.46e-32

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 125.84  E-value: 4.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvakFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd08225    2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEID---LTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAvaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvdNSAPVKLGGFGSAIQLPG 171
Cdd:cd08225   79 EYCDGGDLMKRINRQR--GVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSK--NGMVAKLGDFGIARQLND 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRLsfeAPEWKSISAN 250
Cdd:cd08225  155 SMELAYTC--VGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLhQLVLKICQGYF---APISPNFSRD 229
                        250       260
                 ....*....|....*....|....*...
gi 442620344 251 AKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd08225  230 LRSLISQLFKVSPRDRPSITSILKRPFL 257
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
12-277 5.54e-32

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 126.53  E-value: 5.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASP-GLSTADLkREATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd07841    2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKdGINFTAL-REIKLLQELKHPNIIGLLDVFGHKSNINLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEgSDLcfEVVRRAVAgFVYSEA-VAChYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQL 169
Cdd:cd07841   81 FEFME-TDL--EKVIKDKS-IVLTPAdIKS-YMLMTLRGLEYLHSNWILHRDLKPNNLLI---ASDGVLKLADFGLARSF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 --PGTRetiethgrvgcphyMAPEVVTR-----------RLYGKGCDVWGAGVMLHVLLSgRLPFL-GSG---------- 225
Cdd:cd07841  153 gsPNRK--------------MTHQVVTRwyrapellfgaRHYGVGVDMWSVGCIFAELLL-RVPFLpGDSdidqlgkife 217
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 226 -------------VRLQQSVARGrlSFEAPEWKSI----SANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07841  218 algtpteenwpgvTSLPDYVEFK--PFPPTPLKQIfpaaSDDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
12-278 1.42e-31

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 124.33  E-value: 1.42e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvaKFTASPGLSTADLKREATICHMLKHPHIVELLETY-SSEGMLYMV 90
Cdd:cd14163    2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIID--KSGGPEEFIQRFLPRELQIVERLDHKNIIHVYEMLeSADGKIYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLcFEVVrraVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDnsapVKLGGFGSAIQLP 170
Cdd:cd14163   80 MELAEDGDV-FDCV---LHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFT----LKLTDFGFAKQLP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 -GTRETIETHgrVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFlgSGVRLQQSVARGRLSFEAPEWKSIS 248
Cdd:cd14163  152 kGGRELSQTF--CGSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPF--DDTDIPKMLCQQQKGVSLPGHLGVS 227
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14163  228 RTCQDLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
12-278 1.62e-31

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 124.30  E-value: 1.62e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELC--EVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTaspglSTADLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd14192    4 YAVCphEVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAK-----EREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLcFEvvRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPAcALLATVDNSAPVKLGGFGSAIQL 169
Cdd:cd14192   79 IMEYVDGGEL-FD--RITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPE-NILCVNSTGNQIKIIDFGLARRY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PgTRETIETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEWKSIS 248
Cdd:cd14192  155 K-PREKLKVN--FGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGeTDAETMNNIVNCKWDFDAEAFENLS 231
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14192  232 EEAKDFISRLLVKEKSCRMSATQCLKHEWL 261
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
12-278 4.19e-31

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 122.76  E-value: 4.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHReSNQQFAVKIVDVAKFTASPGLStaDLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14161    5 YEFLETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRIKDEQDLL--HIRREIEIMSSLNHPHIISVYEVFENSSKIVIVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAiQLPG 171
Cdd:cd14161   82 EYASRGDLYDYISERQR----LSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILL---DANGNIKIADFGLS-NLYN 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHgrVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGrlSFEAPEWKSisa 249
Cdd:cd14161  154 QDKFLQTY--CGSPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPFDGHDYKiLVKQISSG--AYREPTKPS--- 226
                        250       260
                 ....*....|....*....|....*....
gi 442620344 250 NAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14161  227 DACGLIRWLLMVNPERRATLEDVASHWWV 255
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
10-278 4.42e-31

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 123.21  E-value: 4.42e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKivdvaKFTASPGLSTADL-KREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd14088    1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCK-----KFLKRDGRKVRKAaKNEINILKMVKHPNILQLVDVFETRKEYF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSdlcfEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSAiq 168
Cdd:cd14088   76 IFLELATGR----EVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSKIVISDFHLA-- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 lpgTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFL---------GSGVRLQQSVARGRLSF 239
Cdd:cd14088  150 ---KLENGLIKEPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYdeaeeddyeNHDKNLFRKILAGDYEF 226
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 442620344 240 EAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14088  227 DSPYWDDISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
12-278 5.57e-31

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 122.62  E-value: 5.57e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLstadlkREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14111    5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVL------QEYEILKSLHHERIMALHEAYITPRYLVLIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRavagFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVKLGGFGSAiQLPG 171
Cdd:cd14111   79 EFCSGKELLHSLIDR----FRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVT---NLNAIKIVDFGSA-QSFN 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQS-VARGRlsFEAPE-WKSISA 249
Cdd:cd14111  151 PLSLRQLGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAkILVAK--FDAFKlYPNVSQ 228
                        250       260
                 ....*....|....*....|....*....
gi 442620344 250 NAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14111  229 SASLFLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
8-278 6.36e-31

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 122.72  E-value: 6.36e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEV-IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLK-HPHIVELLETYSSEG 85
Cdd:cd14198    5 FNNFYILTSKeLGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQD---CRAEILHEIAVLELAKsNPRVVNLHEVYETTS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 MLYMVFEFMEGSDLcFEVVRRAVAGFVySEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGS 165
Cdd:cd14198   82 EIILILEYAAGGEI-FNLCVPDLAEMV-SENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFGM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 166 AIQLPGTRETIEThgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVrlQQS---VARGRLSFEAP 242
Cdd:cd14198  160 SRKIGHACELREI---MGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDN--QETflnISQVNVDYSEE 234
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 442620344 243 EWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14198  235 TFSSVSQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
7-278 6.97e-31

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 122.74  E-value: 6.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   7 LFDDVYELC--EVIGKGPFSIVRRCIHRESNQQFAvkivdvAKFTASpglstadlKREATICHM-LKH-----------P 72
Cdd:cd14197    4 PFQERYSLSpgRELGRGKFAVVRKCVEKDSGKEFA------AKFMRK--------RRKGQDCRMeIIHeiavlelaqanP 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  73 HIVELLETYSSEGMLYMVFEFMEGSDLCFEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLATV 152
Cdd:cd14197   70 WVINLHEVYETASEMILVLEYAAGGEIFNQCVADREEAF--KEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 153 DNSAPVKLGGFGSAIQLPGTRETIEThgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVrlQQS- 231
Cdd:cd14197  148 SPLGDIKIVDFGLSRILKNSEELREI---MGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDK--QETf 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 442620344 232 --VARGRLSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14197  223 lnISQMNVSYSEEEFEHLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
10-278 7.64e-31

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 122.42  E-value: 7.64e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIvdvakFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd14191    2 DFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKF-----FKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLcFEvvRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPAcALLATVDNSAPVKLGGFGSAIQL 169
Cdd:cd14191   77 VLEMVSGGEL-FE--RIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPE-NIMCVNKTGTKIKLIDFGLARRL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 pgtretiETHGRV----GCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGRLSFEAPEW 244
Cdd:cd14191  153 -------ENAGSLkvlfGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNdNETLANVTSATWDFDDEAF 225
                        250       260       270
                 ....*....|....*....|....*....|....
gi 442620344 245 KSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14191  226 DEISDDAKDFISNLLKKDMKARLTCTQCLQHPWL 259
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-273 9.79e-31

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 122.00  E-value: 9.79e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglsTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd08219    2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSA----VEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVvrRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVKLGGFGSAIQLPG 171
Cdd:cd08219   78 EYCDGGDLMQKI--KLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLT---QNGKVKLGDFGSARLLTS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF-LGSGVRLQQSVARGRLSfeaPEWKSISAN 250
Cdd:cd08219  153 PGAYACTY--VGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFqANSWKNLILKVCQGSYK---PLPSHYSYE 227
                        250       260
                 ....*....|....*....|...
gi 442620344 251 AKDLVMKMLAANPHHRLSITEVL 273
Cdd:cd08219  228 LRSLIKQMFKRNPRSRPSATTIL 250
PDZ_MPP6-MPP2-like cd10832
PDZ domain of membrane palmitoylated protein 6 (MPP6), MPP2, and related domains; PDZ (PSD-95 ...
494-574 1.39e-30

PDZ domain of membrane palmitoylated protein 6 (MPP6), MPP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP6, MPP2, and related domains. MPP6 (also known as MAGUK p55 subfamily member, Protein associated with Lin-7, 2 (PALS2), Veli-associated MAGUK 1, and VAM-1) is a membrane-associated guanylate kinase (MAGUK)-like protein. MPP6 is a regulator of Lin-7 expression and localization. MPP6 is also known to bind cell-adhesion protein, nectin-like molecule-2 (Necl-2), and localize to the basolateral plasma membrane in mammalian epithelial cells. MPP2 (also known as MAGUK p55 subfamily member 2) is a postsynaptic protein that links SynCAM1 cell adhesion molecules to core components of the postsynaptic density. Other members of this family include the Drosophila Vari protein, an essential basolateral septate junction protein which interacts with the cell-adhesion protein neurexin IV. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP6-MPP2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467268 [Multi-domain]  Cd Length: 78  Bit Score: 115.02  E-value: 1.39e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 494 RLVQFQKNTDEPMGITLKMtEDGRCIVARIMHGGMIHRQATLHVGDEIREINGQPVqhQSVGQLQRMLREARGSVTFKIV 573
Cdd:cd10832    1 RMVGIRKNPGEPLGVTVRL-EEGELVIARILHGGMIDRQGLLHVGDIIKEVNGVPV--GSPEQLQEMLKNASGSVTLKIL 77

                 .
gi 442620344 574 P 574
Cdd:cd10832   78 P 78
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
12-277 1.39e-30

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 121.41  E-value: 1.39e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTaspglsTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14662    2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKI------DENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEvvRRAVAGfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNS-AP-VKLGGFG---SA 166
Cdd:cd14662   76 EYAAGGEL-FE--RICNAG-RFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLL---DGSpAPrLKICDFGyskSS 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLPGTRETiethgrVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSG--VRLQQSVAR-GRLSFEAP 242
Cdd:cd14662  149 VLHSQPKST------VGTPAYIAPEVLSRKEYdGKVADVWSCGVTLYVMLVGAYPFEDPDdpKNFRKTIQRiMSVQYKIP 222
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442620344 243 EWKSISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14662  223 DYVRVSQDCRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
16-278 2.84e-30

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 120.59  E-value: 2.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFME 95
Cdd:cd06632    6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 GSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLPGTRET 175
Cdd:cd06632   86 GGSI-HKLLQRYGA---FEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANIL---VDTNGVVKLADFGMAKHVEAFSFA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 176 IEThgrVGCPHYMAPEVVTRRL--YGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEwkSISANAK 252
Cdd:cd06632  159 KSF---KGSPYWMAPEVIMQKNsgYGLAVDIWSLGCTVLEMATGKPPWSQyEGVAAIFKIGNSGELPPIPD--HLSPDAK 233
                        250       260
                 ....*....|....*....|....*.
gi 442620344 253 DLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06632  234 DFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
12-277 3.93e-30

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 120.09  E-value: 3.93e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglstaDLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14665    2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDE------NVQREIINHRSLRHPNIVRFKEVILTPTHLAIVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEvvRRAVAGfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNS-AP-VKLGGFG---SA 166
Cdd:cd14665   76 EYAAGGEL-FE--RICNAG-RFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLL---DGSpAPrLKICDFGyskSS 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLPGTRETiethgrVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRL---SFEAP 242
Cdd:cd14665  149 VLHSQPKST------VGTPAYIAPEVLLKKEYdGKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKTIQRIlsvQYSIP 222
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442620344 243 EWKSISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14665  223 DYVHISPECRHLISRIFVADPATRITIPEIRNHEW 257
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
12-277 5.65e-30

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 119.65  E-value: 5.65e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVD---VAKFTASPGLSTADLKreatICHMLK-----HPHIVELLETYSS 83
Cdd:cd14005    2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPksrVTEWAMINGPVPVPLE----IALLLKaskpgVPGVIRLLDWYER 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGMLYMVFEFMEGS-DLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVD-NSAPVKLG 161
Cdd:cd14005   78 PDGFLLIMERPEPCqDL-FDFITERGA---LSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLL---INlRTGEVKLI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 162 GFGSAIQLpgtRETIETHGRvGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFlgsgvRLQQSVARGRLSFe 240
Cdd:cd14005  151 DFGCGALL---KDSVYTDFD-GTRVYSPPEWIRHGRYhGRPATVWSLGILLYDMLCGDIPF-----ENDEQILRGNVLF- 220
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 442620344 241 apeWKSISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14005  221 ---RPRLSKECCDLISRCLQFDPSKRPSLEQILSHPW 254
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
18-274 9.05e-30

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 118.79  E-value: 9.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHResNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd13999    1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDE---LLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLcFEVVRRAvaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPGTRETIE 177
Cdd:cd13999   76 SL-YDLLHKK--KIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILL---DENFTVKIADFGLSRIKNSTTEKMT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 178 thGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFlgSGVRLQQSVARGRLSFEAPEwksISANA----KD 253
Cdd:cd13999  150 --GVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPF--KELSPIQIAAAVVQKGLRPP---IPPDCppelSK 222
                        250       260
                 ....*....|....*....|.
gi 442620344 254 LVMKMLAANPHHRLSITEVLD 274
Cdd:cd13999  223 LIKRCWNEDPEKRPSFSEIVK 243
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
10-278 9.98e-30

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 119.38  E-value: 9.98e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglsTADLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd06610    1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTS----MDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDlCFEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvDNSapVKLGGFGSAIQL 169
Cdd:cd06610   77 VMPLLSGGS-LLDIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGE-DGS--VKIADFGVSASL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 --PGTRETIETHGRVGCPHYMAPEVVTR-RLYGKGCDVWGAGVMLHVLLSGRLPF-----LGSGVRLQQSvARGRLSFEA 241
Cdd:cd06610  153 atGGDRTRKVRKTFVGTPCWMAPEVMEQvRGYDFKADIWSFGITAIELATGAAPYskyppMKVLMLTLQN-DPPSLETGA 231
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 442620344 242 pEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06610  232 -DYKKYSKSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
11-300 1.82e-29

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 118.73  E-value: 1.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  11 VYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAkftaSPGLSTADLKREATICHMLKH---PHIVELLETYSSEGML 87
Cdd:cd06917    2 LYRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLD----TDDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDlcfevVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSAI 167
Cdd:cd06917   78 WIIMDYCEGGS-----IRTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGN---VKLCDFGVAA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLPGTRETIETHgrVGCPHYMAPEVVTR-RLYGKGCDVWGAGVMLHVLLSGRLPFlgSGVRLQQSV------ARGRLsfe 240
Cdd:cd06917  150 SLNQNSSKRSTF--VGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPY--SDVDALRAVmlipksKPPRL--- 222
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 241 apEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKLQRTHLAdtvEELKRYN 300
Cdd:cd06917  223 --EGNGYSPLLKEFVAACLDEEPKDRLSADELLKSKWIKQHSKTPTSVLK---ELISRYN 277
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
10-283 1.86e-29

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 118.69  E-value: 1.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvakFTASPGLStaDLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd06611    5 DIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQ---IESEEELE--DFMVEIDILSECKHPNIVGLYEAYFYENKLWI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLCfEVVRRAVAGFVYSE-AVACHYMrqiLEALRYCHENDILHRDVRpACALLATVDNSapVKLGGFGSAIQ 168
Cdd:cd06611   80 LIEFCDGGALD-SIMLELERGLTEPQiRYVCRQM---LEALNFLHSHKVIHRDLK-AGNILLTLDGD--VKLADFGVSAK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPGTRETIETHgrVGCPHYMAPEVV-----TRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRL-SFEA 241
Cdd:cd06611  153 NKSTLQKRDTF--IGTPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHHElNPMRVLLKILKSEPpTLDQ 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442620344 242 PE-WksiSANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDK 283
Cdd:cd06611  231 PSkW---SSSFNDFLKSCLVKDPDDRPTAAELLKHPFVSDQSD 270
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-278 2.59e-29

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 117.60  E-value: 2.59e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd08218    2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPK---EREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVvrRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLaTVDNSapVKLGGFGSAIQLPG 171
Cdd:cd08218   79 DYCDGGDLYKRI--NAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFL-TKDGI--IKLGDFGIARVLNS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF-LGSGVRLQQSVARGRLSFEAPEWksiSAN 250
Cdd:cd08218  154 TVELARTC--IGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFeAGNMKNLVLKIIRGSYPPVPSRY---SYD 228
                        250       260
                 ....*....|....*....|....*...
gi 442620344 251 AKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd08218  229 LRSLVSQLFKRNPRDRPSINSILEKPFI 256
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
12-282 3.21e-29

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 120.08  E-value: 3.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIvdvakftaspgLSTAD-LKREATICHML--------KHPHIVELLETYS 82
Cdd:cd05573    3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKI-----------LRKSDmLKREQIAHVRAerdiladaDSPWIVRLHYAFQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  83 SEGMLYMVFEFMEGSDLCFEVVRRAvagfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGG 162
Cdd:cd05573   72 DEDHLYLVMEYMPGGDLMNLLIKYD----VFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILL---DADGHIKLAD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 163 FGSAIQLP--GTRETIETHGR-------------------------VGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLL 215
Cdd:cd05573  145 FGLCTKMNksGDRESYLNDSVntlfqdnvlarrrphkqrrvraysaVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEML 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 216 SGRLPFLGSG-VRLQQSVARGRLSFEAPEWKSISANAKDLVMKMLAAnPHHRL-SITEVLDHPWIRDRD 282
Cdd:cd05573  225 YGFPPFYSDSlVETYSKIMNWKESLVFPDDPDVSPEAIDLIRRLLCD-PEDRLgSAEEIKAHPFFKGID 292
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
17-278 3.44e-29

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 117.46  E-value: 3.44e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEG 96
Cdd:cd06625    7 LLGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEASKEVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  97 sdlcfevvrravaGFVY---------SEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAI 167
Cdd:cd06625   87 -------------GSVKdeikaygalTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILR---DSNGNVKLGDFGASK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLPGTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLP----------FlgsgvrlqqSVARGRL 237
Cdd:cd06625  151 RLQTICSSTGMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPwaefepmaaiF---------KIATQPT 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 442620344 238 SFEAPEwkSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06625  222 NPQLPP--HVSEDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
12-276 3.71e-29

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 117.13  E-value: 3.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTAspgLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd08529    2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSR---KMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEVVRRAVaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSAIQLPG 171
Cdd:cd08529   79 EYAENGDL-HSLIKSQR-GRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDN---VKIGDLGVAKILSD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TreTIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF-LGSGVRLQQSVARGRLSfeaPEWKSISAN 250
Cdd:cd08529  154 T--TNFAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFeAQNQGALILKIVRGKYP---PISASYSQD 228
                        250       260
                 ....*....|....*....|....*.
gi 442620344 251 AKDLVMKMLAANPHHRLSITEVLDHP 276
Cdd:cd08529  229 LSQLIDSCLTKDYRQRPDTTELLRNP 254
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
12-277 4.75e-29

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 118.05  E-value: 4.75e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVakFTASPGLS-TAdlKREATICHMLKHPHIVELLETYSSE------ 84
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRM--ENEKEGFPiTA--IREIKLLQKLDHPNVVRLKEIVTSKgsakyk 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  85 GMLYMVFEFMEgSDLcfevvrravAGFVYSEAVAC------HYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPV 158
Cdd:cd07840   77 GSIYMVFEYMD-HDL---------TGLLDNPEVKFtesqikCYMKQLLEGLQYLHSNGILHRDIKGSNILI---NNDGVL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 159 KLGGFGSAIQLPGTRETIETHgRVGCPHYMAPEVV---TRrlYGKGCDVWGAGVMLHVLLSGRLPFLGS----------- 224
Cdd:cd07840  144 KLADFGLARPYTKENNADYTN-RVITLWYRPPELLlgaTR--YGPEVDMWSVGCILAELFTGKPIFQGKteleqlekife 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 225 -----------GVR-------LQQSVARGRLSFEapEWKS-ISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07840  221 lcgspteenwpGVSdlpwfenLKPKKPYKRRLRE--VFKNvIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
12-278 4.94e-29

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 116.88  E-value: 4.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvaKFTASPGLSTADLKREATICHMLKHPHIVELLETYS-SEGMLYMV 90
Cdd:cd14164    2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVD--RRRASPDFVQKFLPRELSILRRVNHPNIVQMFECIEvANGRLYIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEgSDLCFEVVRRAVAGFVYSEAVachyMRQILEALRYCHENDILHRDVRPACALLATVDNSapVKLGGFGSAIQLP 170
Cdd:cd14164   80 MEAAA-TDLLQKIQEVHHIPKDLARDM----FAQMVGAVNYLHDMNIVHRDLKCENILLSADDRK--IKIADFGFARFVE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRETieTHGRVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSfeaPEWKSISA 249
Cdd:cd14164  153 DYPEL--STTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPFDETNVRRLRLQQRGVLY---PSGVALEE 227
                        250       260
                 ....*....|....*....|....*....
gi 442620344 250 NAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14164  228 PCRALIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
10-282 5.57e-29

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 117.92  E-value: 5.57e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPglSTADLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd05612    1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLK--QEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQL 169
Cdd:cd05612   79 LMEYVPGGEL-FSYLRNSGR---FSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILL---DKEGHIKLTDFGFAKKL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PGTRETIethgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRLSFEapewKSIS 248
Cdd:cd05612  152 RDRTWTL-----CGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPfGIYEKILAGKLEFP----RHLD 222
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 442620344 249 ANAKDLVMKMLAANPHHRL-----SITEVLDHPWIRDRD 282
Cdd:cd05612  223 LYAKDLIKKLLVVDRTRRLgnmknGADDVKNHRWFKSVD 261
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
18-280 7.14e-29

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 116.81  E-value: 7.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLStaDLKREATICHMLKH-PHIVELLETYSSEGMLYMVFEFMEG 96
Cdd:cd05611    4 ISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVT--NVKAERAIMMIQGEsPYVAKLYYSFQSKDYLYLVMEYLNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  97 SDlCFEVVRraVAGfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFG-SAIQLpgtret 175
Cdd:cd05611   82 GD-CASLIK--TLG-GLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLL---IDQTGHLKLTDFGlSRNGL------ 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 176 IETHGR--VGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRLSFEAPEWKSISANAK 252
Cdd:cd05611  149 EKRHNKkfVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPdAVFDNILSRRINWPEEVKEFCSPEAV 228
                        250       260       270
                 ....*....|....*....|....*....|.
gi 442620344 253 DLVMKMLAANPHHRLS---ITEVLDHPWIRD 280
Cdd:cd05611  229 DLINRLLCMDPAKRLGangYQEIKSHPFFKS 259
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
10-278 8.18e-29

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 116.21  E-value: 8.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftaspglSTADLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd06612    3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEE-------DLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLC--FEVVRRavagfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAI 167
Cdd:cd06612   76 VMEYCGAGSVSdiMKITNK-----TLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILL---NEEGQAKLADFGVSG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLPGT---RETIethgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFlgSGVRLQQSVA----RGRLSFE 240
Cdd:cd06612  148 QLTDTmakRNTV-----IGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPY--SDIHPMRAIFmipnKPPPTLS 220
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 442620344 241 APE-WksiSANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06612  221 DPEkW---SPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
SH3_MPP1 cd12080
Src Homology 3 domain of Membrane Protein, Palmitoylated 1 (or MAGUK p55 subfamily member 1); ...
586-646 1.80e-28

Src Homology 3 domain of Membrane Protein, Palmitoylated 1 (or MAGUK p55 subfamily member 1); MPP1, also called 55 kDa erythrocyte membrane protein (p55), is a ubiquitously-expressed scaffolding protein that plays roles in regulating neutrophil polarity, cell shape, hair cell development, and neural development and patterning of the retina. It was originally identified as an erythrocyte protein that stabilizes the actin cytoskeleton to the plasma membrane by forming a complex with 4.1R protein and glycophorin C. MPP1 is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains the three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 213013  Cd Length: 62  Bit Score: 108.50  E-value: 1.80e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 586 FVRAQFDYNPLDDELIPCAQAGISFQVGDILQIISKDDHHWWQARLDTVG-GSAGLIPSPEL 646
Cdd:cd12080    1 YMRAQFDYDPKKDNLIPCKEAGLKFQTGDIIQIINKDDSNWWQGRVEGSGeESAGLIPSPEL 62
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
16-275 2.52e-28

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 114.72  E-value: 2.52e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADlkREATICHMLKHPHIVELLETYSSEGMLYMVFEFME 95
Cdd:cd14188    7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKID--KEIELHRILHHKHVVQFYHYFEDKENIYILLEYCS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 GSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLpgtrET 175
Cdd:cd14188   85 RRSMAHILKARKV----LTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFF---INENMELKVGDFGLAARL----EP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 176 IETHGRVGC--PHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGRLSFEApewkSISANAK 252
Cdd:cd14188  154 LEHRRRTICgtPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKeTYRCIREARYSLPS----SLLAPAK 229
                        250       260
                 ....*....|....*....|...
gi 442620344 253 DLVMKMLAANPHHRLSITEVLDH 275
Cdd:cd14188  230 HLIASMLSKNPEDRPSLDEIIRH 252
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-278 4.79e-28

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 114.07  E-value: 4.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftASPGLSTAdLKREATICHMLKHPHIVELLETYSSE-GMLYMV 90
Cdd:cd08223    2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKN--ASKRERKA-AEQEAKLLSKLKHPNIVSYKESFEGEdGFLYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLCFEVvrRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVKLGGFGSAIQLP 170
Cdd:cd08223   79 MGFCEGGDLYTRL--KEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLT---KSNIIKVGDLGIARVLE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRETIEThgRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGRLsfeAPEWKSISA 249
Cdd:cd08223  154 SSSDMATT--LIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNsLVYKILEGKL---PPMPKQYSP 228
                        250       260
                 ....*....|....*....|....*....
gi 442620344 250 NAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd08223  229 ELGELIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
16-278 6.21e-28

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 113.86  E-value: 6.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIVDvakfTASPGLSTADLKrEATICHMLKHPHIVELLETYSSEGMLYMVFEFME 95
Cdd:cd14190   10 EVLGGGKFGKVHTCTEKRTGLKLAAKVIN----KQNSKDKEMVLL-EIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 GSDLcFEvvRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVdNSAPVKLGGFGSAIQLpGTRET 175
Cdd:cd14190   85 GGEL-FE--RIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNR-TGHQVKIIDFGLARRY-NPREK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 176 IETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEWKSISANAKDL 254
Cdd:cd14190  160 LKVN--FGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGdDDTETLNNVLMGNWYFDEETFEHVSDEAKDF 237
                        250       260
                 ....*....|....*....|....
gi 442620344 255 VMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14190  238 VSNLIIKERSARMSATQCLKHPWL 261
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
12-279 9.68e-28

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 113.48  E-value: 9.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftaSPglstadlKREATICHML-----KHPHIVELLETYSSEGM 86
Cdd:cd06647    9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQ---QP-------KKELIINEILvmrenKNPNIVNYLDSYLVGDE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEGSDLCfEVVRRAVAgfvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtVDNSapVKLGGFGSA 166
Cdd:cd06647   79 LWVVMEYLAGGSLT-DVVTETCM----DEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLG-MDGS--VKLTDFGFC 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLpgTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVA-RGRLSFEAPEw 244
Cdd:cd06647  151 AQI--TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIAtNGTPELQNPE- 227
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442620344 245 kSISANAKDLVMKMLAANPHHRLSITEVLDHPWIR 279
Cdd:cd06647  228 -KLSAIFRDFLNRCLEMDVEKRGSAKELLQHPFLK 261
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
17-286 1.06e-27

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 114.62  E-value: 1.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIVdvakftaSPGLSTADLKREATIC--HML----KHPHIVELLETYSSEGMLYMV 90
Cdd:cd05570    2 VLGKGSFGKVMLAERKKTDELYAIKVL-------KKEVIIEDDDVECTMTekRVLalanRHPFLTGLHACFQTEDRLYFV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLCFEVVRravaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQlp 170
Cdd:cd05570   75 MEYVNGGDLMFHIQR----ARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLL---DAEGHIKIADFGMCKE-- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVrlqQSVARGRLSFEAPEWKSISAN 250
Cdd:cd05570  146 GIWGGNTTSTFCGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDE---DELFEAILNDEVLYPRWLSRE 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442620344 251 AKDLVMKMLAANPHHRLSIT-----EVLDHPWIR--DRDKLQR 286
Cdd:cd05570  223 AVSILKGLLTKDPARRLGCGpkgeaDIKAHPFFRniDWDKLEK 265
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
17-279 1.16e-27

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 113.96  E-value: 1.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTAdlKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEG 96
Cdd:cd05630    7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMA--LNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  97 SDLCFEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPgTRETI 176
Cdd:cd05630   85 GDLKFHIYHMGQAGF--PEARAVFYAAEICCGLEDLHRERIVYRDLKPENILL---DDHGHIRISDLGLAVHVP-EGQTI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 177 EthGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARgRLSFEAPEWKS--ISANAKDL 254
Cdd:cd05630  159 K--GRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVE-RLVKEVPEEYSekFSPQARSL 235
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 255 VMKMLAANPHHRL-----SITEVLDHPWIR 279
Cdd:cd05630  236 CSMLLCKDPAERLgcrggGAREVKEHPLFK 265
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
16-278 1.27e-27

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 112.91  E-value: 1.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRrCIHRESNQQFAVKIVDvakftaspgLSTAD----------LKREATICHMLKHPHIVELLETYSSEG 85
Cdd:cd06631    7 NVLGKGAYGTVY-CGLTSTGQLIAVKQVE---------LDTSDkekaekeyekLQEEVDLLKTLKHVNIVGYLGTCLEDN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 MLYMVFEFMEGSDLCfevvrRAVAGF-VYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvdnSAPVKLGGFG 164
Cdd:cd06631   77 VVSIFMEFVPGGSIA-----SILARFgALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMP---NGVIKLIDFG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 SAIQLpGTRETIETHGRV-----GCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPfLGSGVRLQQSVARGRLSF 239
Cdd:cd06631  149 CAKRL-CINLSSGSQSQLlksmrGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPP-WADMNPMAAIFAIGSGRK 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 442620344 240 EAPEW-KSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06631  227 PVPRLpDKFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
18-282 1.56e-27

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 113.01  E-value: 1.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREatICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKI--ILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLCFEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPGTRETie 177
Cdd:cd05577   79 DLKYHIYNVGTRGF--SEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILL---DDHGHVRISDLGLAVEFKGGKKI-- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 178 tHGRVGCPHYMAPEVVTR-RLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWK-SISANAKDLV 255
Cdd:cd05577  152 -KGRVGTHGYMAPEVLQKeVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMAVEYPdSFSPEARSLC 230
                        250       260       270
                 ....*....|....*....|....*....|..
gi 442620344 256 MKMLAANPHHRL-----SITEVLDHPWIRDRD 282
Cdd:cd05577  231 EGLLQKDPERRLgcrggSADEVKEHPFFRSLN 262
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
17-278 1.95e-27

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 112.63  E-value: 1.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIVDvakfTASPGLSTAD--------LKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd06628    7 LIGSGSFGSVYLGMNASSGELMAVKQVE----LPSVSAENKDrkksmldaLQREIALLRELQHENIVQYLGSSSDANHLN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSdlcfevvrrAVAGFV-----YSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGF 163
Cdd:cd06628   83 IFLEYVPGG---------SVATLLnnygaFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANIL---VDNKGGIKISDF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 164 GSAIQLPGTRETIETHG-RV---GCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFlgsgVRLQQSVARGRL-S 238
Cdd:cd06628  151 GISKKLEANSLSTKNNGaRPslqGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPF----PDCTQMQAIFKIgE 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 442620344 239 FEAPEWKS-ISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06628  227 NASPTIPSnISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
12-280 2.20e-27

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 115.10  E-value: 2.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVdvAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05621   54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLL--SKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVM 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCfevvrRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPG 171
Cdd:cd05621  132 EYMPGGDLV-----NLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLL---DKYGHLKLADFGTCMKMDE 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TrETIETHGRVGCPHYMAPEVVTRR----LYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEWKS 246
Cdd:cd05621  204 T-GMVHCDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLFEMLVGDTPFYAdSLVGTYSKIMDHKNSLNFPDDVE 282
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 442620344 247 ISANAKDLVMKMLAANPHH--RLSITEVLDHPWIRD 280
Cdd:cd05621  283 ISKHAKNLICAFLTDREVRlgRNGVEEIKQHPFFRN 318
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
17-286 2.46e-27

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 113.65  E-value: 2.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFS---IVRRCIHRESNQQFAVKIVDVAKFTASPGLSTadlKREATICHMLKHPHIVELLETYSSEGMLYMVFEF 93
Cdd:cd05582    2 VLGQGSFGkvfLVRKITGPDAGTLYAMKVLKKATLKVRDRVRT---KMERDILADVNHPFIVKLHYAFQTEGKLYLILDF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  94 MEGSDLcFEVVRRAVagfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSaiqlpgTR 173
Cdd:cd05582   79 LRGGDL-FTRLSKEV---MFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL---DEDGHIKLTDFGL------SK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 174 ETIETHGRV----GCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGRLSFeaPEWksIS 248
Cdd:cd05582  146 ESIDHEKKAysfcGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKeTMTMILKAKLGM--PQF--LS 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 442620344 249 ANAKDLVMKMLAANPHHRL-----SITEVLDHPWIR--DRDKLQR 286
Cdd:cd05582  222 PEAQSLLRALFKRNPANRLgagpdGVEEIKRHPFFAtiDWNKLYR 266
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
12-277 2.56e-27

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 112.39  E-value: 2.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIV---RRcihRESNQQFAVKIVDVAKftaspglsTADLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd14010    2 YVLYDEIGRGKHSVVykgRR---KGTIEFVAIKCVDKSK--------RPEVLNEVRLTHELKHPNVLKFYEWYETSNHLW 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLcfEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSA-- 166
Cdd:cd14010   71 LVVEYCTGGDL--ETLLRQDGNL--PESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILL---DGNGTLKLSDFGLArr 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 --------IQLPGTRETIETH----GRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGvrlQQSVAR 234
Cdd:cd14010  144 egeilkelFGQFSDEGNVNKVskkqAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAES---FTELVE 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 442620344 235 GRLSFEAPEWK-----SISANAKDLVMKMLAANPHHRLSITEVLDHP-W 277
Cdd:cd14010  221 KILNEDPPPPPpkvssKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
16-278 3.42e-27

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 112.03  E-value: 3.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRES-NQQFAVKIVDVAKFTASPGLstadLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFM 94
Cdd:cd14202    8 DLIGHGAFAVVFKGRHKEKhDLEVAVKCINKKNLAKSQTL----LGKEIKILKELKHENIVALYDFQEIANSVYLVMEYC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  95 EGSDLcfevvrravAGFVY-----SEAVACHYMRQILEALRYCHENDILHRDVRPACALLA------TVDNSAPVKLGGF 163
Cdd:cd14202   84 NGGDL---------ADYLHtmrtlSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrkSNPNNIRIKIADF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 164 GSAIQLPGTRETIEThgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGR-LSFEA 241
Cdd:cd14202  155 GFARYLQNNMMAATL---CGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQdLRLFYEKNKsLSPNI 231
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 442620344 242 PewKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14202  232 P--RETSSHLRQLLLGLLQRNQKDRMDFDEFFHHPFL 266
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
12-280 3.68e-27

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 113.42  E-value: 3.68e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVK-IVDV------AKFTAspglstadlkREATICHMLK-HPHIVELLETYSS 83
Cdd:cd07852    9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKkIFDAfrnatdAQRTF----------REIMFLQELNdHPNIIKLLNVIRA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGM--LYMVFEFMEgSDLcFEVVRRAVAgfvysEAVACHY-MRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKL 160
Cdd:cd07852   79 ENDkdIYLVFEYME-TDL-HAVIRANIL-----EDIHKQYiMYQLLKALKYLHSGGVIHRDLKPSNILL---NSDCRVKL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 161 GGFG---SAIQLPGTRETIETHGRVGCPHYMAPEV-VTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGS------------ 224
Cdd:cd07852  149 ADFGlarSLSQLEEDDENPVLTDYVATRWYRAPEIlLGSTRYTKGVDMWSVGCILGEMLLGKPLFPGTstlnqlekiiev 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620344 225 -GVRLQQSVArgrlSFEAPEWKSI-------------------SANAKDLVMKMLAANPHHRLSITEVLDHPWIRD 280
Cdd:cd07852  229 iGRPSAEDIE----SIQSPFAATMleslppsrpksldelfpkaSPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQ 300
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
12-278 4.25e-27

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 111.73  E-value: 4.25e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCE-----VIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglstADLKREATICHMLKHPHIVELLETYSSEGM 86
Cdd:cd06624    5 YEYDEsgervVLGKGTFGVVYAARDLSTQVRIAIKEIPERDSREV-----QPLHEEIALHSRLSHKNIVQYLGSVSEDGF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEGSDLCfEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVdnSAPVKLGGFGSA 166
Cdd:cd06624   80 FKIFMEQVPGGSLS-ALLRSKWGPLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTY--SGVVKISDFGTS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLPGTRETIETHgrVGCPHYMAPEVVTR--RLYGKGCDVWGAGVMLHVLLSGRLPF--LGSGVRLQQSVARGRLSFEAP 242
Cdd:cd06624  157 KRLAGINPCTETF--TGTLQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMATGKPPFieLGEPQAAMFKVGMFKIHPEIP 234
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 442620344 243 EwkSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06624  235 E--SLSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
10-279 5.04e-27

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 111.49  E-value: 5.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpGLStADLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd14117    6 DDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKE-GVE-HQLRREIEIQSHLRHPNILRLYNYFHDRKRIYL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvdnSAPVKLGGFGSAIQL 169
Cdd:cd14117   84 ILEYAPRGELYKELQKHGR----FDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGY---KGELKIADFGWSVHA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PGTRETIethgRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF-LGSGVRLQQSVARGRLSFEapewKSIS 248
Cdd:cd14117  157 PSLRRRT----MCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFeSASHTETYRRIVKVDLKFP----PFLS 228
                        250       260       270
                 ....*....|....*....|....*....|.
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLDHPWIR 279
Cdd:cd14117  229 DGSRDLISKLLRYHPSERLPLKGVMEHPWVK 259
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
17-280 5.07e-27

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 111.68  E-value: 5.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTAdlKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEG 96
Cdd:cd05605    7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMA--LNEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMNG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  97 SDLCFEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPgTRETI 176
Cdd:cd05605   85 GDLKFHIYNMGNPGF--EEERAVFYAAEITCGLEHLHSERIVYRDLKPENILL---DDHGHVRISDLGLAVEIP-EGETI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 177 etHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWKS-ISANAKDLV 255
Cdd:cd05605  159 --RGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRRVKEDQEEYSEkFSEEAKSIC 236
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 256 MKMLAANPHHRL-----SITEVLDHPWIRD 280
Cdd:cd05605  237 SQLLQKDPKTRLgcrgeGAEDVKSHPFFKS 266
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
18-279 6.15e-27

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 111.00  E-value: 6.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTadlkrEATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd06648   15 IGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRRELLFN-----EVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLCfEVVrraVAGFVYSEAVAChYMRQILEALRYCHENDILHRDVRPACALLATvdnSAPVKLGGFGSAIQLpgTRETIE 177
Cdd:cd06648   90 ALT-DIV---THTRMNEEQIAT-VCRAVLKALSFLHSQGVIHRDIKSDSILLTS---DGRVKLSDFGFCAQV--SKEVPR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 178 THGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLgsGVRLQQSVARGRLSfEAPEWK---SISANAKDL 254
Cdd:cd06648  160 RKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYF--NEPPLQAMKRIRDN-EPPKLKnlhKVSPRLRSF 236
                        250       260
                 ....*....|....*....|....*
gi 442620344 255 VMKMLAANPHHRLSITEVLDHPWIR 279
Cdd:cd06648  237 LDRMLVRDPAQRATAAELLNHPFLA 261
SH3_MPP cd11862
Src Homology 3 domain of Membrane Protein, Palmitoylated (or MAGUK p55 subfamily member) ...
586-645 7.57e-27

Src Homology 3 domain of Membrane Protein, Palmitoylated (or MAGUK p55 subfamily member) proteins; The MPP/p55 subfamily of MAGUK (membrane-associated guanylate kinase) proteins includes at least eight vertebrate members (MPP1-7 and CASK), four Drosophila proteins (Stardust, Varicose, CASK and Skiff), and other similar proteins; they all contain one each of the core of three domains characteristic of MAGUK proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, most members except for MPP1 contain N-terminal L27 domains and some also contain a Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. CASK has an additional calmodulin-dependent kinase (CaMK)-like domain at the N-terminus. Members of this subfamily are scaffolding proteins that play important roles in regulating and establishing cell polarity, cell adhesion, and synaptic targeting and transmission, among others. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212796  Cd Length: 61  Bit Score: 103.81  E-value: 7.57e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620344 586 FVRAQFDYNPLDDELIPCAQAGISFQVGDILQIISKDDHHWWQAR-LDTVGGSAGLIPSPE 645
Cdd:cd11862    1 FVRALFDYDPEEDPLIPCKEAGLSFKKGDILQIVNQDDPNWWQARkVGDPNGRAGLIPSQD 61
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
12-278 7.59e-27

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 110.55  E-value: 7.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKR---EATICHMLK---HPHIVELLETYSSEG 85
Cdd:cd14004    2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDTWVRDRKLGTvplEIHILDTLNkrsHPNIVKLLDFFEDDE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 MLYMVFE-FMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFG 164
Cdd:cd14004   82 FYYLVMEkHGSGMDL-FDFIERKPN---MDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVIL---DGNGTIKLIDFG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 SAIQL-PGTRETIethgrVGCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFlgsgVRLQQSVARgrlSFEAP 242
Cdd:cd14004  155 SAAYIkSGPFDTF-----VGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPF----YNIEEILEA---DLRIP 222
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 442620344 243 ewKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14004  223 --YAVSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-278 8.60e-27

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 110.21  E-value: 8.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADlkrEATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd08220    2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALN---EVKVLSMLHHPNIIEYYESFLEDKALMIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEVVRRAvAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvDNSAPVKLGGFGSAIQLpG 171
Cdd:cd08220   79 EYAPGGTL-FEYIQQR-KGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLN--KKRTVVKIGDFGISKIL-S 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIEThgRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRLSFEAPEWksiSAN 250
Cdd:cd08220  154 SKSKAYT--VVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLpALVLKIMRGTFAPISDRY---SEE 228
                        250       260
                 ....*....|....*....|....*...
gi 442620344 251 AKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd08220  229 LRHLILSMLHLDPNKRPTLSEIMAQPII 256
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
17-280 9.94e-27

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 111.24  E-value: 9.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTAdlKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEG 96
Cdd:cd05631    7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMA--LNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  97 SDLCFEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPgTRETI 176
Cdd:cd05631   85 GDLKFHIYNMGNPGF--DEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILL---DDRGHIRISDLGLAVQIP-EGETV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 177 EthGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEW-KSISANAKDLV 255
Cdd:cd05631  159 R--GRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRRVKEDQEEYsEKFSEDAKSIC 236
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 256 MKMLAANPHHRLSIT-----EVLDHPWIRD 280
Cdd:cd05631  237 RMLLTKNPKERLGCRgngaaGVKQHPIFKN 266
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
10-293 1.31e-26

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 113.56  E-value: 1.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVdvAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd05622   73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLL--SKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYM 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLCfevvrRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQL 169
Cdd:cd05622  151 VMEYMPGGDLV-----NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADFGTCMKM 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 pgTRE-TIETHGRVGCPHYMAPEVVTRR----LYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPE 243
Cdd:cd05622  223 --NKEgMVRCDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYAdSLVGTYSKIMNHKNSLTFPD 300
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442620344 244 WKSISANAKDLVMKMLAANPHH--RLSITEVLDHPWIRDrDKLQRTHLADTV 293
Cdd:cd05622  301 DNDISKEAKNLICAFLTDREVRlgRNGVEEIKRHLFFKN-DQWAWETLRDTV 351
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
10-280 1.40e-26

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 111.22  E-value: 1.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTAdlKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd05632    2 NTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMA--LNEKQILEKVNSQFVVNLAYAYETKDALCL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLCFEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQL 169
Cdd:cd05632   80 VLTIMNGGDLKFHIYNMGNPGF--EEERALFYAAEILCGLEDLHRENTVYRDLKPENILL---DDYGHIRISDLGLAVKI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PgtrETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQ-QSVARGRLSFEAPEWKSIS 248
Cdd:cd05632  155 P---EGESIRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKrEEVDRRVLETEEVYSAKFS 231
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 442620344 249 ANAKDLVMKMLAANPHHRLSIT-----EVLDHPWIRD 280
Cdd:cd05632  232 EEAKSICKMLLTKDPKQRLGCQeegagEVKRHPFFRN 268
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
12-276 1.57e-26

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 110.00  E-value: 1.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIhRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKH-PHIVELL--ETYSSEGMLY 88
Cdd:cd14131    3 YEILKQLGKGGSSKVYKVL-NPKKKIYALKRVDLEGADEQ---TLQSYKNEIELLKKLKGsDRIIQLYdyEVTDEDDYLY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGsDLCFEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatVDNSapVKLGGFG--SA 166
Cdd:cd14131   79 MVMECGEI-DLATILKKKRPKPI--DPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL--VKGR--LKLIDFGiaKA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQlPGT----RETIethgrVGCPHYMAPEVVT--------RRLY--GKGCDVWGAGVMLHVLLSGRLPFlgsgvrlqQSV 232
Cdd:cd14131  152 IQ-NDTtsivRDSQ-----VGTLNYMSPEAIKdtsasgegKPKSkiGRPSDVWSLGCILYQMVYGKTPF--------QHI 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442620344 233 ARGRLSFEA---P----EWKSISanAKDLVMKM---LAANPHHRLSITEVLDHP 276
Cdd:cd14131  218 TNPIAKLQAiidPnheiEFPDIP--NPDLIDVMkrcLQRDPKKRPSIPELLNHP 269
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
714-879 1.99e-26

Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.


Pssm-ID: 238026  Cd Length: 137  Bit Score: 105.31  E-value: 1.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 714 LVLLGAHGVGRRHIKNTLISKYPDKYAYPIPHTTRPAKPEEENGRSYYFVSHDEMMADIGANEYLEYGTHEDAMYGTKLD 793
Cdd:cd00071    2 IVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSKA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 794 TIRRIHTEGKMAILDVEPQALKILRTAEFTPYVVFIAAPslqniadydgslerlakesemlrqlyghffDLTIVNNDISE 873
Cdd:cd00071   82 AVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP------------------------------DYVIVNDDLEK 131

                 ....*.
gi 442620344 874 TIATLE 879
Cdd:cd00071  132 AYEELK 137
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
16-320 2.43e-26

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 110.77  E-value: 2.43e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIV--DVAkFTASPGLSTADLKREATICHmlKHPHIVELLETYSSEGMLYMVFEF 93
Cdd:cd05590    1 RVLGKGSFGKVMLARLKESGRLYAVKVLkkDVI-LQDDDVECTMTEKRILSLAR--NHPFLTQLYCCFQTPDRLFFVMEF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  94 MEGSDLCFEV--VRRavagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQlpG 171
Cdd:cd05590   78 VNGGDLMFHIqkSRR------FDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLL---DHEGHCKLADFGMCKE--G 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRLSFeaPEWksISAN 250
Cdd:cd05590  147 IFNGKTTSTFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEdDLFEAILNDEVVY--PTW--LSQD 222
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620344 251 AKDLVMKMLAANPHHRL-SITE-----VLDHPWIRDRDklqrthladtVEELKRYNARRKLKGAVQAIAGGTNMDP 320
Cdd:cd05590  223 AVDILKAFMTKNPTMRLgSLTLggeeaILRHPFFKELD----------WEKLNRRQIEPPFRPRIKSREDVSNFDP 288
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
18-278 3.48e-26

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 109.69  E-value: 3.48e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVrrCIHRE--SNQQFAVKIVDVAKFTASPGLSTadlkrEATICHMLKHPHIVELLETYSSEGMLYMVFEFME 95
Cdd:cd06659   29 IGEGSTGVV--CIAREkhSGRQVAVKMMDLRKQQRRELLFN-----EVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQ 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 GSDLCfevvrRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRpACALLATVDNSapVKLGGFGSAIQLpgTRET 175
Cdd:cd06659  102 GGALT-----DIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIK-SDSILLTLDGR--VKLSDFGFCAQI--SKDV 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 176 IETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLgSGVRLQqsvARGRLSFEAP----EWKSISANA 251
Cdd:cd06659  172 PKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYF-SDSPVQ---AMKRLRDSPPpklkNSHKASPVL 247
                        250       260
                 ....*....|....*....|....*..
gi 442620344 252 KDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06659  248 RDFLERMLVRDPQERATAQELLDHPFL 274
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
18-276 3.82e-26

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 108.61  E-value: 3.82e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRE-SNQQFAVKIVDVAKFTASPGLstadLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEG 96
Cdd:cd14120    1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKSQNL----LGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  97 SDLcfevVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAP------VKLGGFGSAIQLP 170
Cdd:cd14120   77 GDL----ADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRKPspndirLKIADFGFARFLQ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GT--RETIethgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGR-LSFEAPEWks 246
Cdd:cd14120  153 DGmmAATL-----CGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQeLKAFYEKNAnLRPNIPSG-- 225
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 247 ISANAKDLVMKMLAANPHHRLSITEVLDHP 276
Cdd:cd14120  226 TSPALKDLLLGLLKRNPKDRIDFEDFFSHP 255
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-278 4.39e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 108.28  E-value: 4.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKI---VDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd08222    2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVlkeISVGELQPD---ETVDANREAKLLSKLDHPAIVKFHDSFVEKESFC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLCFEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvdNSAPVKLGGFGSAIQ 168
Cdd:cd08222   79 IVTEYCEGGDLDDKISEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL----KNNVIKVGDFGISRI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPGTRETIETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVrlqQSVARGRLSFEAPEWKSI- 247
Cdd:cd08222  155 LMGTSDLATTF--TGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNL---LSVMYKIVEGETPSLPDKy 229
                        250       260       270
                 ....*....|....*....|....*....|.
gi 442620344 248 SANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd08222  230 SKELNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
12-278 4.43e-26

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 108.73  E-value: 4.43e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQ-----QFAVKIVdvAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGM 86
Cdd:cd14076    3 YILGRTLGEGEFGKVKLGWPLPKANhrsgvQVAIKLI--RRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSA 166
Cdd:cd14076   81 IGIVLEFVSGGELFDYILARRR----LKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRN---LVITDFGFA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQL-PGTRETIEThgRVGCPHYMAPE-VVTRRLY-GKGCDVWGAGVMLHVLLSGRLPF--------LGSGVRLQQSVARG 235
Cdd:cd14076  154 NTFdHFNGDLMST--SCGSPCYAAPElVVSDSMYaGRKADIWSCGVILYAMLAGYLPFdddphnpnGDNVPRLYRYICNT 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442620344 236 RLSFeaPEWksISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14076  232 PLIF--PEY--VTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
10-282 5.26e-26

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 109.03  E-value: 5.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLS-TADLKReatICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd14209    1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEhTLNEKR---ILQAINFPFLVKLEYSFKDNSNLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLcFEVVRRaVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQ 168
Cdd:cd14209   78 MVMEYVPGGEM-FSHLRR-IGRF--SEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLI---DQQGYIKVTDFGFAKR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPGTRETIethgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEApewkSI 247
Cdd:cd14209  151 VKGRTWTL-----CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFAdQPIQIYEKIVSGKVRFPS----HF 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 442620344 248 SANAKDLVMKMLAANPHHRL-----SITEVLDHPWIRDRD 282
Cdd:cd14209  222 SSDLKDLLRNLLQVDLTKRFgnlknGVNDIKNHKWFATTD 261
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
12-279 1.26e-25

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 109.39  E-value: 1.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVdvAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05596   28 FDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLL--SKFEMIKRSDSAFFWEERDIMAHANSEWIVQLHYAFQDDKYLYMVM 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCfevvrRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLpG 171
Cdd:cd05596  106 DYMPGGDLV-----NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLL---DASGHLKLADFGTCMKM-D 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHGRVGCPHYMAPEVVTRR----LYGKGCDVWGAGVMLHVLLSGRLPFLG---SGVRLQQSVARGRLSFeaPEW 244
Cdd:cd05596  177 KDGLVRSDTAVGTPDYISPEVLKSQggdgVYGRECDWWSVGVFLYEMLVGDTPFYAdslVGTYGKIMNHKNSLQF--PDD 254
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 442620344 245 KSISANAKDLVMKMLaANPHHRL---SITEVLDHPWIR 279
Cdd:cd05596  255 VEISKDAKSLICAFL-TDREVRLgrnGIEEIKAHPFFK 291
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
12-279 2.70e-25

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 107.12  E-value: 2.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftaSPGLSTadLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd06655   21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQK---QPKKEL--IINEILVMKELKNPNIVNFLDSFLVGDELFVVM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAVagfvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvdnSAPVKLGGFGSAIQLpg 171
Cdd:cd06655   96 EYLAGGSLTDVVTETCM-----DEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGM---DGSVKLTDFGFCAQI-- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVA-RGRLSFEAPEwkSISA 249
Cdd:cd06655  166 TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIAtNGTPELQNPE--KLSP 243
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 250 NAKDLVMKMLAANPHHRLSITEVLDHPWIR 279
Cdd:cd06655  244 IFRDFLNRCLEMDVEKRGSAKELLQHPFLK 273
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
12-277 3.17e-25

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 106.46  E-value: 3.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvAKFTaspglSTAD---LKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMK-KKFY-----SWEEcmnLREVKSLRKLNEHPNIVKLKEVFRENDELY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSdlCFEVVRRAvAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSAiq 168
Cdd:cd07830   75 FVFEYMEGN--LYQLMKDR-KGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEV---VKIADFGLA-- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 lpgtRETiethgRVGCPH--------YMAPEVVTR-RLYGKGCDVWGAGVMLHVLLSGRLPF---------------LGS 224
Cdd:cd07830  147 ----REI-----RSRPPYtdyvstrwYRAPEILLRsTSYSSPVDIWALGCIMAELYTLRPLFpgsseidqlykicsvLGT 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 225 --------GVRLQQsvargRLSFEAPEWKSI---------SANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07830  218 ptkqdwpeGYKLAS-----KLGFRFPQFAPTslhqlipnaSPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
12-277 3.67e-25

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 106.35  E-value: 3.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQqfavkIVDVAKFTASPGLSTAD--LKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd07846    3 YENLGLVGEGSYGMVMKCRHKETGQ-----IVAIKKFLESEDDKMVKkiAMREIKMLKQLRHENLVNLIEVFRRKKRWYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLcfEVVRRAVAGFVYSeaVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQL 169
Cdd:cd07846   78 VFEFVDHTVL--DDLEKYPNGLDES--RVRKYLFQILRGIDFCHSHNIIHRDIKPENIL---VSQSGVVKLCDFGFARTL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PGTRETIETHgrVGCPHYMAPE-VVTRRLYGKGCDVWGAGVMLHVLLSGRLPF--------------------------- 221
Cdd:cd07846  151 AAPGEVYTDY--VATRWYRAPElLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFpgdsdidqlyhiikclgnliprhqelf 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 222 ----LGSGVRLQQSVARGRLSFEAPEWKSISAnakDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07846  229 qknpLFAGVRLPEVKEVEPLERRYPKLSGVVI---DLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
16-286 3.79e-25

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 107.40  E-value: 3.79e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFME 95
Cdd:cd05595    1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKD--EVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYAN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 GSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPGTRET 175
Cdd:cd05595   79 GGELFFHLSRERV----FTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLML---DKDGHIKITDFGLCKEGITDGAT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 176 IETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGRLSFEapewKSISANAKDL 254
Cdd:cd05595  152 MKTF--CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDhERLFELILMEEIRFP----RTLSPEAKSL 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 442620344 255 VMKMLAANPHHRL-----SITEVLDHPW---IRDRDKLQR 286
Cdd:cd05595  226 LAGLLKKDPKQRLgggpsDAKEVMEHRFflsINWQDVVQK 265
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
714-882 4.20e-25

guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 213788  Cd Length: 179  Bit Score: 102.96  E-value: 4.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  714 LVLLGAHGVGrrhiKNTLIS---KYPDKYAYPIPHTTRPAKPEEENGRSYYFVSHDEMMADIGANEYLEYGTHEDAMYGT 790
Cdd:TIGR03263   3 IVISGPSGAG----KSTLVKallEEDPNLKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  791 KLDTIRRIHTEGKMAILDVEPQ-ALKILRTaeFTPYV-VFIAAPSLQNIA--------DYDGSLE-RLAK-ESEMlrqLY 858
Cdd:TIGR03263  79 PKSPVEEALAAGKDVLLEIDVQgARQVKKK--FPDAVsIFILPPSLEELErrlrkrgtDSEEVIErRLAKaKKEI---AH 153
                         170       180
                  ....*....|....*....|....
gi 442620344  859 GHFFDLTIVNNDISETIATLETAI 882
Cdd:TIGR03263 154 ADEFDYVIVNDDLEKAVEELKSII 177
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
18-278 5.00e-25

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 105.39  E-value: 5.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVakftaSPGLSTADLkREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd14110   11 INRGRFSVVRQCEEKRSGQMLAAKIIPY-----KPEDKQLVL-REYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPAcALLATVDNSapVKLGGFGSAiQLPGTRETIE 177
Cdd:cd14110   85 ELLYNLAERNS----YSEAEVTDYLWQILSAVDYLHSRRILHLDLRSE-NMIITEKNL--LKIVDLGNA-QPFNQGKVLM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 178 THGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGRLSFEAPeWKSISANAKDLVM 256
Cdd:cd14110  157 TDKKGDYVETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWeRDRNIRKGKVQLSRC-YAGLSGGAVNFLK 235
                        250       260
                 ....*....|....*....|..
gi 442620344 257 KMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14110  236 STLCAKPWGRPTASECLQNPWL 257
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
12-276 5.12e-25

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 106.14  E-value: 5.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELcEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREatICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05607    5 YEF-RVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKE--ILEKVNSPFIVSLAYAFETKTHLCLVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAVAGFVYSEAVacHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPG 171
Cdd:cd05607   82 SLMNGGDLKYHIYNVGERGIEMERVI--FYSAQITCGILHLHSLKIVYRDMKPENVLL---DDNGNCRLSDLGLAVEVKE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIEthgRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-----SGVRLQQSVARGRLSFEAPEWks 246
Cdd:cd05607  157 GKPITQ---RAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDhkekvSKEELKRRTLEDEVKFEHQNF-- 231
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 247 iSANAKDLVMKMLAANPHHRLSITEVLDHP 276
Cdd:cd05607  232 -TEEAKDICRLFLAKKPENRLGSRTNDDDP 260
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
26-277 5.31e-25

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 104.73  E-value: 5.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  26 VRRCIHRESNQQFAVKIVDVAKFTASPGlstadlkreATIChMLKHPHIVELLETYSSEGMLYMVFEFMEGSDLCFEvvr 105
Cdd:cd14022    9 VFRAVHLHSGEELVCKVFDIGCYQESLA---------PCFC-LPAHSNINQITEIILGETKAYVFFERSYGDMHSFV--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 106 RAVAGFVYSEAVACHYmrQILEALRYCHENDILHRDVRPACALLATVDNSApVKLGGFGSAIQLPGTRETIEThgRVGCP 185
Cdd:cd14022   76 RTCKKLREEEAARLFY--QIASAVAHCHDGGLVLRDLKLRKFVFKDEERTR-VKLESLEDAYILRGHDDSLSD--KHGCP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 186 HYMAPEVV-TRRLY-GKGCDVWGAGVMLHVLLSGRLPF-------LGSGVRlqqsvaRGRlsFEAPEwkSISANAKDLVM 256
Cdd:cd14022  151 AYVSPEILnTSGSYsGKAADVWSLGVMLYTMLVGRYPFhdiepssLFSKIR------RGQ--FNIPE--TLSPKAKCLIR 220
                        250       260
                 ....*....|....*....|.
gi 442620344 257 KMLAANPHHRLSITEVLDHPW 277
Cdd:cd14022  221 SILRREPSERLTSQEILDHPW 241
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
17-275 6.88e-25

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 105.01  E-value: 6.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIVDVAKfTASPG-----LSTADLKREatichmLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14189    8 LLGKGGFARCYEMTDLATNKTYAVKVIPHSR-VAKPHqrekiVNEIELHRD------LHHKHVVKFSHHFEDAENIYIFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EfmegsdLCfevVRRAVAGF-----VYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSA 166
Cdd:cd14189   81 E------LC---SRKSLAHIwkarhTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFF---INENMELKVGDFGLA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLpgtrETIETHGRVGC--PHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARgRLSFEAPew 244
Cdd:cd14189  149 ARL----EPPEQRKKTICgtPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIK-QVKYTLP-- 221
                        250       260       270
                 ....*....|....*....|....*....|.
gi 442620344 245 KSISANAKDLVMKMLAANPHHRLSITEVLDH 275
Cdd:cd14189  222 ASLSLPARHLLAGILKRNPGDRLTLDQILEH 252
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
16-276 6.89e-25

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 105.20  E-value: 6.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTAD-LKREATICHMLKHPHIVELLETYSSEGMLYMVFEFM 94
Cdd:cd06630    6 PLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQEEVVEaIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  95 EGSdlcfevvrrAVAGFV-----YSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAP-VKLGGFGSAIQ 168
Cdd:cd06630   86 AGG---------SVASLLskygaFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLL---VDSTGQrLRIADFGAAAR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LpGTRETI--ETHGR-VGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQ-QSVARGRLSFEAPEW 244
Cdd:cd06630  154 L-ASKGTGagEFQGQlLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHlALIFKIASATTPPPI 232
                        250       260       270
                 ....*....|....*....|....*....|...
gi 442620344 245 -KSISANAKDLVMKMLAANPHHRLSITEVLDHP 276
Cdd:cd06630  233 pEHLSPGLRDVTLRCLELQPEDRPPARELLKHP 265
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
12-279 7.75e-25

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 105.96  E-value: 7.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftaSPglstadlKREATICHML-----KHPHIVELLETYSSEGM 86
Cdd:cd06656   21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQ---QP-------KKELIINEILvmrenKNPNIVNYLDSYLVGDE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEGSDLCFEVVRRAVagfvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtVDNSapVKLGGFGSA 166
Cdd:cd06656   91 LWVVMEYLAGGSLTDVVTETCM-----DEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLG-MDGS--VKLTDFGFC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLpgTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVA-RGRLSFEAPEw 244
Cdd:cd06656  163 AQI--TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYLIAtNGTPELQNPE- 239
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442620344 245 kSISANAKDLVMKMLAANPHHRLSITEVLDHPWIR 279
Cdd:cd06656  240 -RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLK 273
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
17-280 1.02e-24

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 105.35  E-value: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLkrEATICHMLKHPHIVELLETYSSEGMLYMVFEFMEG 96
Cdd:cd05608    8 VLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMV--EKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  97 SDLCFEV--VRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPGTRE 174
Cdd:cd05608   86 GDLRYHIynVDEENPGF--QEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLL---DDDGNVRISDLGLAVELKDGQT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 175 tiETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEW-KSISANAKD 253
Cdd:cd05608  161 --KTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEKVENKELKQRILNDSVTYsEKFSPASKS 238
                        250       260       270
                 ....*....|....*....|....*....|..
gi 442620344 254 LVMKMLAANPHHRL-----SITEVLDHPWIRD 280
Cdd:cd05608  239 ICEALLAKDPEKRLgfrdgNCDGLRTHPFFRD 270
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
714-882 1.21e-24

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 102.07  E-value: 1.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 714 LVLLGAHGVGRRHIKNTLISKYPDkYAYPIPHTTRPAKPEEENGRSYYFVSHDEMMADIGANEYLEYGTHEDAMYGTKLD 793
Cdd:COG0194    5 IVLSGPSGAGKTTLVKALLERDPD-LRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGTPKA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 794 TIRRIHTEGKMAILDVEPQ-ALKILRTAeftPYVV--FIAAPSLQ---------------NIAdydgslERLAK-ESEML 854
Cdd:COG0194   84 EVEEALAAGKDVLLEIDVQgARQVKKKF---PDAVsiFILPPSLEelerrlrgrgtdseeVIE------RRLAKaREELA 154
                        170       180
                 ....*....|....*....|....*...
gi 442620344 855 RQlygHFFDLTIVNNDISETIATLETAI 882
Cdd:COG0194  155 HA---DEFDYVVVNDDLDRAVEELKAII 179
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
16-282 2.12e-24

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 105.13  E-value: 2.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKI----VDVAKFTASPGLStadlkrEATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05571    1 KVLGKGTFGKVILCREKATGELYAIKIlkkeVIIAKDEVAHTLT------ENRVLQNTRHPFLTSLKYSFQTNDRLCFVM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAiqlpg 171
Cdd:cd05571   75 EYVNGGELFFHLSRERV----FSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLL---DKDGHIKITDFGLC----- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 tRETIeTHGRV-----GCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGRLSFeaPewK 245
Cdd:cd05571  143 -KEEI-SYGATtktfcGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDhEVLFELILMEEVRF--P--S 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 442620344 246 SISANAKDLVMKMLAANPHHRL-----SITEVLDHPWIRDRD 282
Cdd:cd05571  217 TLSPEAKSLLAGLLKKDPKKRLgggprDAKEIMEHPFFASIN 258
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
12-277 3.96e-24

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 103.52  E-value: 3.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAkfTASPGL-STAdlKREATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd07835    1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLE--TEDEGVpSTA--IREISLLKELNHPNIVRLLDVVHSENKLYLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMegsDLCFEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFG--SAIQ 168
Cdd:cd07835   77 FEFL---DLDLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLL---IDTEGALKLADFGlaRAFG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPGTRETIEthgrVGCPHYMAPEVVT-RRLYGKGCDVWGAG------VMLHVLLSG-----------RLpfLGS------ 224
Cdd:cd07835  151 VPVRTYTHE----VVTLWYRAPEILLgSKHYSTPVDIWSVGcifaemVTRRPLFPGdseidqlfrifRT--LGTpdedvw 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620344 225 -GVrlqQSVARGRLSFeaPEWK---------SISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07835  225 pGV---TSLPDYKPTF--PKWArqdlskvvpSLDEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
12-329 3.98e-24

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 104.62  E-value: 3.98e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFS---IVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd05614    2 FELLKVLGTGAYGkvfLVRKVSGHDANKLYAMKVLRKAALVQKAKTVEHTRTERNVLEHVRQSPFLVTLHYAFQTDAKLH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQ 168
Cdd:cd05614   82 LILDYVSGGELFTHLYQRDH----FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILL---DSEGHVVLTDFGLSKE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPgTRETIETHGRVGCPHYMAPEVV-TRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQS-VARGRLSFEAPEWKS 246
Cdd:cd05614  155 FL-TEEKERTYSFCGTIEYMAPEIIrGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSeVSRRILKCDPPFPSF 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 247 ISANAKDLVMKMLAANPHHRL-----SITEVLDHPWIRDrdkLQRTHLAD-TVEELKRYNARRKLKgaVQAIAGG-TNMD 319
Cdd:cd05614  234 IGPVARDLLQKLLCKDPKKRLgagpqGAQEIKEHPFFKG---LDWEALALrKVNPPFRPSIRSELD--VGNFAEEfTNLE 308
                        330
                 ....*....|
gi 442620344 320 PLYATDADMP 329
Cdd:cd05614  309 PVYSPAGTPP 318
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
12-282 4.84e-24

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 102.87  E-value: 4.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREatICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05609    2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERD--ILTFAENPFVVSMYCSFETKRHLCMVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDlCFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFG-SAIQLP 170
Cdd:cd05609   80 EYVEGGD-CATLLKNIGP---LPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGH---IKLTDFGlSKIGLM 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 G-TRETIETH-----------GRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGRL 237
Cdd:cd05609  153 SlTTNLYEGHiekdtrefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEeLFGQVISDEI 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 442620344 238 SF-EAPEWksISANAKDLVMKMLAANPHHRL---SITEVLDHPWIRDRD 282
Cdd:cd05609  233 EWpEGDDA--LPDDAQDLITRLLQQNPLERLgtgGAEEVKQHPFFQDLD 279
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
28-278 5.49e-24

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 101.88  E-value: 5.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  28 RCIHRESNQQFAVKIVDVAKFTASPGLSTadlkreaticHMLKHPHIVELLETYSSEGMLYMVFEFMEGsDLCFEVVRRA 107
Cdd:cd14024   11 RAEHYQTEKEYTCKVLSLRSYQECLAPYD----------RLGPHEGVCSVLEVVIGQDRAYAFFSRHYG-DMHSHVRRRR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 108 VagfvYSEAVACHYMRQILEALRYCHENDILHRDVRpACALLATVDNSAPVKLGGFGSAIQLPGTRETIEThgRVGCPHY 187
Cdd:cd14024   80 R----LSEDEARGLFTQMARAVAHCHQHGVILRDLK-LRRFVFTDELRTKLVLVNLEDSCPLNGDDDSLTD--KHGCPAY 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 188 MAPEVV-TRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGrlSFEAPEWksISANAKDLVMKMLAANPH 264
Cdd:cd14024  153 VGPEILsSRRSYsGKAADVWSLGVCLYTMLLGRYPFQDTEpAALFAKIRRG--AFSLPAW--LSPGARCLVSCMLRRSPA 228
                        250
                 ....*....|....
gi 442620344 265 HRLSITEVLDHPWI 278
Cdd:cd14024  229 ERLKASEILLHPWL 242
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
12-277 5.97e-24

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 102.74  E-value: 5.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVK-----IVDVAKFTASPGLSTadLKReatichMLKHPHIVELLETY--SSE 84
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKcmkkhFKSLEQVNNLREIQA--LRR------LSPHPNILRLIEVLfdRKT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  85 GMLYMVFEFMEGSdlCFEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvdNSAPVKLGGFG 164
Cdd:cd07831   73 GRLALVFELMDMN--LYELIKGRKRPL--PEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI----KDDILKLADFG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 SA----IQLPGTrETIETHgrvgcpHYMAPE-VVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGS--------------- 224
Cdd:cd07831  145 SCrgiySKPPYT-EYISTR------WYRAPEcLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTneldqiakihdvlgt 217
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620344 225 -GVRLQQSVARGR-LSFEAPEWK---------SISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07831  218 pDAEVLKKFRKSRhMNYNFPSKKgtglrkllpNASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
17-286 6.71e-24

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 103.63  E-value: 6.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIvdvakftaspglstadLKREATI------CHML---------KHPHIVELLETY 81
Cdd:cd05587    3 VLGKGSFGKVMLAERKGTDELYAIKI----------------LKKDVIIqdddveCTMVekrvlalsgKPPFLTQLHSCF 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  82 SSEGMLYMVFEFMEGSDLCFEVvrRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLG 161
Cdd:cd05587   67 QTMDRLYFVMEYVNGGDLMYHI--QQVGKF--KEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML---DAEGHIKIA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 162 GFGSAIQlpGTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRLSFE 240
Cdd:cd05587  140 DFGMCKE--GIFGGKTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEdELFQSIMEHNVSYP 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442620344 241 apewKSISANAKDLVMKMLAANPHHRLSIT-----EVLDHPWIR--DRDKLQR 286
Cdd:cd05587  218 ----KSLSKEAVSICKGLLTKHPAKRLGCGptgerDIKEHPFFRriDWEKLER 266
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
12-277 7.07e-24

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 103.76  E-value: 7.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVK-IVDVAKftaspglSTADLK---REATICHMLKHPHIVELL-----ETYS 82
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKkISNVFD-------DLIDAKrilREIKILRHLKHENIIGLLdilrpPSPE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  83 SEGMLYMVFEFMEgSDLCfEVVRravAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPAcALLATVDNSapVKLGG 162
Cdd:cd07834   75 EFNDVYIVTELME-TDLH-KVIK---SPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPS-NILVNSNCD--LKICD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 163 FGSA-IQLPGTRETIETHGrVGCPHYMAPEVVtrrL----YGKGCDVWGAGVMLHVLLSGRLPFLGS------------- 224
Cdd:cd07834  147 FGLArGVDPDEDKGFLTEY-VVTRWYRAPELL---LsskkYTKAIDIWSVGCIFAELLTRKPLFPGRdyidqlnlivevl 222
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 225 GV-------RLQQSVARGRL----SFEAPEWKSI----SANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07834  223 GTpseedlkFISSEKARNYLkslpKKPKKPLSEVfpgaSPEAIDLLEKMLVFNPKKRITADEALAHPY 290
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
12-281 9.15e-24

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 102.38  E-value: 9.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKivdvaKFTASPglSTADLK----REATICHMLKHPHIVELLETYSSEGML 87
Cdd:cd07848    3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIK-----KFKDSE--ENEEVKettlRELKMLRTLKQENIVELKEAFRRRGKL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLcfEVVRRAVAGfVYSEAVAChYMRQILEALRYCHENDILHRDVRPACALLATVDnsaPVKLGGFGSAI 167
Cdd:cd07848   76 YLVFEYVEKNML--ELLEEMPNG-VPPEKVRS-YIYQLIKAIHWCHKNDIVHRDIKPENLLISHND---VLKLCDFGFAR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLPGTRETIETHgRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWksi 247
Cdd:cd07848  149 NLSEGSNANYTE-YVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPAEQ--- 224
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442620344 248 sanakdlvMKMLAANPH-HRLSITEVlDHPWIRDR 281
Cdd:cd07848  225 --------MKLFYSNPRfHGLRFPAV-NHPQSLER 250
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
12-279 9.89e-24

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 102.50  E-value: 9.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftaSPglstadlKREATICHML-----KHPHIVELLETYSSEGM 86
Cdd:cd06654   22 YTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQ---QP-------KKELIINEILvmrenKNPNIVNYLDSYLVGDE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEGSDLCFEVVRRAVagfvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtVDNSapVKLGGFGSA 166
Cdd:cd06654   92 LWVVMEYLAGGSLTDVVTETCM-----DEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLG-MDGS--VKLTDFGFC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLpgTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVA-RGRLSFEAPEw 244
Cdd:cd06654  164 AQI--TPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENpLRALYLIAtNGTPELQNPE- 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442620344 245 kSISANAKDLVMKMLAANPHHRLSITEVLDHPWIR 279
Cdd:cd06654  241 -KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLK 274
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
9-278 1.08e-23

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 102.03  E-value: 1.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   9 DDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvakfTASPGlSTADLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd06643    4 EDFWEIVGELGDGAFGKVYKAQNKETGILAAAKVID----TKSEE-ELEDYMVEIDILASCDHPNIVKLLDAFYYENNLW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGS--DLCFEVVRRAVagfvySEA---VAChymRQILEALRYCHENDILHRDVRpACALLATVDNSapVKLGGF 163
Cdd:cd06643   79 ILIEFCAGGavDAVMLELERPL-----TEPqirVVC---KQTLEALVYLHENKIIHRDLK-AGNILFTLDGD--IKLADF 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 164 GsaIQLPGTRETIETHGRVGCPHYMAPEVV-----TRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGR- 236
Cdd:cd06643  148 G--VSAKNTRTLQRRDSFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHElNPMRVLLKIAKSEp 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442620344 237 LSFEAP-EWksiSANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06643  226 PTLAQPsRW---SPEFKDFLRKCLEKNVDARWTTSQLLQHPFV 265
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
12-282 1.13e-23

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 103.08  E-value: 1.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIvdvakftaspgLSTADLKREATICHM---------LKHPHIVELLETYS 82
Cdd:cd05599    3 FEPLKVIGRGAFGEVRLVRKKDTGHVYAMKK-----------LRKSEMLEKEQVAHVraerdilaeADNPWVVKLYYSFQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  83 SEGMLYMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGG 162
Cdd:cd05599   72 DEENLYLIMEFLPGGDMMTLLMKKDT----LTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLL---DARGHIKLSD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 163 FGSAIQLPGTRETIEThgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEA 241
Cdd:cd05599  145 FGLCTGLKKSHLAYST---VGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSdDPQETCRKIMNWRETLVF 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 442620344 242 PEWKSISANAKDLVMKmLAANPHHRL---SITEVLDHPWIRDRD 282
Cdd:cd05599  222 PPEVPISPEAKDLIER-LLCDAEHRLganGVEEIKSHPFFKGVD 264
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
17-286 1.19e-23

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 102.85  E-value: 1.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIV--DVAkftaspglstadLKREATICHML---------KHPHIVELLETYSSEG 85
Cdd:cd05592    2 VLGKGSFGKVMLAELKGTNQYFAIKALkkDVV------------LEDDDVECTMIerrvlalasQHPFLTHLFCTFQTES 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 MLYMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGS 165
Cdd:cd05592   70 HLFFVMEYLNGGDLMFHIQQSGR----FDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLL---DREGHIKIADFGM 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 166 AiQLPGTRETiETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRLSFeaPEW 244
Cdd:cd05592  143 C-KENIYGEN-KASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEdELFWSICNDTPHY--PRW 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 442620344 245 ksISANAKDLVMKMLAANPHHRLSITE-----VLDHPWIR--DRDKLQR 286
Cdd:cd05592  219 --LTKEAASCLSLLLERNPEKRLGVPEcpagdIRDHPFFKtiDWDKLER 265
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
11-278 1.36e-23

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 101.23  E-value: 1.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  11 VYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVakftaSPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd06613    1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKL-----EPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEG---SDLcFEVVRravagfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvdnSAPVKLGGFGSAI 167
Cdd:cd06613   76 MEYCGGgslQDI-YQVTG------PLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTE---DGDVKLADFGVSA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLPGT---RETIethgrVGCPHYMAPEV--VTRRL-YGKGCDVWGAGVMLHVLLSGRLPFlgSGVRLQQSVAR-GRLSFE 240
Cdd:cd06613  146 QLTATiakRKSF-----IGTPYWMAPEVaaVERKGgYDGKCDIWALGITAIELAELQPPM--FDLHPMRALFLiPKSNFD 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 442620344 241 APEWKS---ISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06613  219 PPKLKDkekWSPDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
12-277 1.99e-23

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 101.40  E-value: 1.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPglSTAdlKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd07836    2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEEGTP--STA--IREISLMKELKHENIVRLHDVIHTENKLMLVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGsDLCFEVVRRAVAGFVySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFG--SAIQL 169
Cdd:cd07836   78 EYMDK-DLKKYMDTHGVRGAL-DPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLI---NKRGELKLADFGlaRAFGI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PGTRETIEthgrVGCPHYMAPEVVT-RRLYGKGCDVWGAGVMLHVLLSGRLPFLGS-------------GVRLQQSVARG 235
Cdd:cd07836  153 PVNTFSNE----VVTLWYRAPDVLLgSRTYSTSIDIWSVGCIMAEMITGRPLFPGTnnedqllkifrimGTPTESTWPGI 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 236 RLSfeaPEWK----------------SISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07836  229 SQL---PEYKptfpryppqdlqqlfpHADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
26-278 2.26e-23

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 100.20  E-value: 2.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  26 VRRCIHRESNQQFAVKIVDVAKFTAspglstadlKREATIChMLKHPHIVELLETYSSEGMLYMVFEFMEGSDLCFEVVR 105
Cdd:cd13976    9 LYRCVDIHTGEELVCKVVPVPECHA---------VLRAYFR-LPSHPNISGVHEVIAGETKAYVFFERDHGDLHSYVRSR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 106 RAVagfvySEAVACHYMRQILEALRYCHENDILHRDVRpACALLATVDNSAPVKLGGFGSAIQLPGTRETIetHGRVGCP 185
Cdd:cd13976   79 KRL-----REPEAARLFRQIASAVAHCHRNGIVLRDLK-LRKFVFADEERTKLRLESLEDAVILEGEDDSL--SDKHGCP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 186 HYMAPEVV-TRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGrlSFEAPEwkSISANAKDLVMKMLAAN 262
Cdd:cd13976  151 AYVSPEILnSGATYsGKAADVWSLGVILYTMLVGRYPFHDSEpASLFAKIRRG--QFAIPE--TLSPRARCLIRSLLRRE 226
                        250
                 ....*....|....*.
gi 442620344 263 PHHRLSITEVLDHPWI 278
Cdd:cd13976  227 PSERLTAEDILLHPWL 242
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
13-274 2.69e-23

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 100.32  E-value: 2.69e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344    13 ELCEVIGKGPFSIVRRCIHRESN----QQFAVKIVDVAKFTASpglsTADLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTLKGKGdgkeVEVAVKTLKEDASEQQ----IEEFLREARIMRKLDHPNIVKLLGVCTEEEPLM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344    89 MVFEFMEGSDLcFEVVRRAVAGFVySEAVACHYMRQILEALRYCHENDILHRDvrpacalLAT----VDNSAPVKLGGFG 164
Cdd:smart00221  78 IVMEYMPGGDL-LDYLRKNRPKEL-SLSDLLSFALQIARGMEYLESKNFIHRD-------LAArnclVGENLVVKISDFG 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   165 SAIQLPGTRETIETHGRVgcP-HYMAPEVVTRRLYGKGCDVWGAGVMLHVLLS-GRLPFLG-SGVRLQQSVARG-RLSFE 240
Cdd:smart00221 149 LSRDLYDDDYYKVKGGKL--PiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGmSNAEVLEYLKKGyRLPKP 226
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 442620344   241 A---PEWKSIsanakdlvMKM-LAANPHHRLSITEVLD 274
Cdd:smart00221 227 PncpPELYKL--------MLQcWAEDPEDRPTFSELVE 256
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
13-274 2.88e-23

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 100.30  E-value: 2.88e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344    13 ELCEVIGKGPFSIVRRCIHRESN----QQFAVKivdVAKFTASPGLsTADLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKLKGKGgkkkVEVAVK---TLKEDASEQQ-IEEFLREARIMRKLDHPNVVKLLGVCTEEEPLY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344    89 MVFEFMEGSDLcFEVVRRAVAGFVYSEAVacHYMRQILEALRYCHENDILHRDvrpacalLAT----VDNSAPVKLGGFG 164
Cdd:smart00219  78 IVMEYMEGGDL-LSYLRKNRPKLSLSDLL--SFALQIARGMEYLESKNFIHRD-------LAArnclVGENLVVKISDFG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   165 SAIQLPGTRETIETHGRVgcP-HYMAPEVVTRRLYGKGCDVWGAGVMLHVLLS-GRLPFLG-SGVRLQQSVARG-RLsfE 240
Cdd:smart00219 148 LSRDLYDDDYYRKRGGKL--PiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGmSNEEVLEYLKNGyRL--P 223
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 442620344   241 APEWKSisanaKDLVMKML---AANPHHRLSITEVLD 274
Cdd:smart00219 224 QPPNCP-----PELYDLMLqcwAEDPEDRPTFSELVE 255
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
18-274 4.21e-23

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 100.01  E-value: 4.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDvAKFTASPGlSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd14187   15 LGKGGFAKCYEITDADTKEVFAGKIVP-KSLLLKPH-QKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPGTRETIE 177
Cdd:cd14187   93 SL-LELHKRRKA---LTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFL---NDDMEVKIGDFGLATKVEYDGERKK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 178 ThgRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGvrLQQSVAR-GRLSFEAPewKSISANAKDLVM 256
Cdd:cd14187  166 T--LCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSC--LKETYLRiKKNEYSIP--KHINPVAASLIQ 239
                        250
                 ....*....|....*...
gi 442620344 257 KMLAANPHHRLSITEVLD 274
Cdd:cd14187  240 KMLQTDPTARPTINELLN 257
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
8-273 4.49e-23

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 100.06  E-value: 4.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVdvaKFTASPGLSTADLkREATICHMLKHPHIVELLETYSSEGML 87
Cdd:cd13996    4 YLNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKI---RLTEKSSASEKVL-REVKALAKLNHPNIVRYYTAWVEEPPL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLCFEVVRRAVAGFVySEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSapVKLGGFGSA- 166
Cdd:cd13996   80 YIQMELCEGGTLRDWIDRRNSSSKN-DRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQ--VKIGDFGLAt 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 ---IQLPGTRETIETHGR--------VGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSgrlPFLGSGVRLQ--QSVA 233
Cdd:cd13996  157 sigNQKRELNNLNNNNNGntsnnsvgIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLH---PFKTAMERSTilTDLR 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 442620344 234 RGRLsfeaPEWKSISANA-KDLVMKMLAANPHHRLSITEVL 273
Cdd:cd13996  234 NGIL----PESFKAKHPKeADLIQSLLSKNPEERPSAEQLL 270
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
13-275 5.09e-23

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze 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 catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 99.49  E-value: 5.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   13 ELCEVIGKGPFSIVRRCI----HRESNQQFAVKIVdvaKFTASPgLSTADLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGTlkgeGENTKIKVAVKTL---KEGADE-EEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   89 MVFEFMEGSDLcFEVVRRAVAGFVYSEAVacHYMRQILEALRYCHENDILHRDvrpacalLAT----VDNSAPVKLGGFG 164
Cdd:pfam07714  78 IVTEYMPGGDL-LDFLRKHKRKLTLKDLL--SMALQIAKGMEYLESKNFVHRD-------LAArnclVSENLVVKISDFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  165 SAIQLPGTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLS-GRLPFLG-SGVRLQQSVARG-RLsfEA 241
Cdd:pfam07714 148 LSRDIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGmSNEEVLEFLEDGyRL--PQ 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 442620344  242 PE--WKSIsanaKDLVMKMLAANPHHRLSITEVLDH 275
Cdd:pfam07714 226 PEncPDEL----YDLMKQCWAYDPEDRPTFSELVED 257
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
10-282 6.15e-23

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 100.85  E-value: 6.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPF---SIVRRcihRESNQQFAVKIV---DVAKFTaspglSTADLKREATICHMLKHPHIVELLETYSS 83
Cdd:cd05598    1 SMFEKIKTIGVGAFgevSLVRK---KDTNALYAMKTLrkkDVLKRN-----QVAHVKAERDILAEADNEWVVKLYYSFQD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGMLYMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGF 163
Cdd:cd05598   73 KENLYFVMDYIPGGDLMSLLIKKGI----FEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNIL---IDRDGHIKLTDF 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 164 GSAIqlpGTRETIET-----HGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRL 237
Cdd:cd05598  146 GLCT---GFRWTHDSkyylaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAqTPAETQLKVINWRT 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 442620344 238 SFEAPEWKSISANAKDLVMKmLAANPHHRLS---ITEVLDHPWIRDRD 282
Cdd:cd05598  223 TLKIPHEANLSPEAKDLILR-LCCDAEDRLGrngADEIKAHPFFAGID 269
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
12-277 6.54e-23

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 100.47  E-value: 6.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVK--IVDVAK----FTAspglstadlKREATICHMLKHPHIVELLE------ 79
Cdd:cd07866   10 YEILGKLGEGTFGEVYKARQIKTGRVVALKkiLMHNEKdgfpITA---------LREIKILKKLKHPNVVPLIDmaverp 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  80 --TYSSEGMLYMVFEFMEgSDLCfevvrravaGFVYSEAV---ACH---YMRQILEALRYCHENDILHRDVRPACALlat 151
Cdd:cd07866   81 dkSKRKRGSVYMVTPYMD-HDLS---------GLLENPSVkltESQikcYMLQLLEGINYLHENHILHRDIKAANIL--- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 152 VDNSAPVKLGGFGSA------IQLPGTRETIETHGRVGC---PHYMAPEVVT-RRLYGKGCDVWGAGVMLHVLLSGRLPF 221
Cdd:cd07866  148 IDNQGILKIADFGLArpydgpPPNPKGGGGGGTRKYTNLvvtRWYRPPELLLgERRYTTAVDIWGIGCVFAEMFTRRPIL 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 222 LGSGVRLQQSV---ARGRLSFEA-PEWKS--------ISANAK---------------DLVMKMLAANPHHRLSITEVLD 274
Cdd:cd07866  228 QGKSDIDQLHLifkLCGTPTEETwPGWRSlpgcegvhSFTNYPrtleerfgklgpeglDLLSKLLSLDPYKRLTASDALE 307

                 ...
gi 442620344 275 HPW 277
Cdd:cd07866  308 HPY 310
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
10-278 7.68e-23

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 99.30  E-value: 7.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVakftaspglsTADLKREatICH---MLK----HPHIVELLETY- 81
Cdd:cd06608    6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDI----------IEDEEEE--IKLeinILRkfsnHPNIATFYGAFi 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  82 -----SSEGMLYMVFEFMEGSDLCfEVVRRAVA-GFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvdnS 155
Cdd:cd06608   74 kkdppGGDDQLWLVMEYCGGGSVT-DLVKGLRKkGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTE---E 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 156 APVKLGGFGSAIQLPGTRETIETHgrVGCPHYMAPEVVT-----RRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQ 229
Cdd:cd06608  150 AEVKLVDFGVSAQLDSTLGRRNTF--IGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPLCDmHPMRAL 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442620344 230 QSVARG---RLSfEAPEWksiSANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06608  228 FKIPRNpppTLK-SPEKW---SKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
12-276 1.02e-22

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 103.03  E-value: 1.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAkftaspGLSTADLKR-EATICHMLKHPH--IVELLE--TYSSEG- 85
Cdd:PTZ00283  34 YWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDME------GMSEADKNRaQAEVCCLLNCDFfsIVKCHEdfAKKDPRn 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 -----MLYMVFEFMEGSDLCFEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvdnSAPVKL 160
Cdd:PTZ00283 108 penvlMIALVLDYANAGDLRQEIKSRAKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCS---NGLVKL 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 161 GGFGSAIQLPGTreTIETHGRVGC--PHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR--LQQSVArGR 236
Cdd:PTZ00283 185 GDFGFSKMYAAT--VSDDVGRTFCgtPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEevMHKTLA-GR 261
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 442620344 237 LSfeaPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHP 276
Cdd:PTZ00283 262 YD---PLPPSISPEMQEIVTALLSSDPKRRPSSSKLLNMP 298
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
12-282 1.08e-22

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 100.08  E-value: 1.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvaKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05601    3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLK--KSETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENLYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRavaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPG 171
Cdd:cd05601   81 EYHPGGDLLSLLSRY---DDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILI---DRTGHIKLADFGSAAKLSS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TReTIETHGRVGCPHYMAPEVVT------RRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVrlqqSVARGRL-----SFE 240
Cdd:cd05601  155 DK-TVTSKMPVGTPDYIAPEVLTsmnggsKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTV----IKTYSNImnfkkFLK 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 442620344 241 APEWKSISANAKDLVMKMLaANPHHRLSITEVLDHPWIRDRD 282
Cdd:cd05601  230 FPEDPKVSESAVDLIKGLL-TDAKERLGYEGLCCHPFFSGID 270
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
5-275 1.42e-22

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 98.58  E-value: 1.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   5 EILFDDVyELCEVIGKGPFSIVRRCIHreSNQQFAVKivdVAKFTASPGLSTA--DLKREATICHMLKHPHIVELLETYS 82
Cdd:cd14145    2 EIDFSEL-VLEEIIGIGGFGKVYRAIW--IGDEVAVK---AARHDPDEDISQTieNVRQEAKLFAMLKHPNIIALRGVCL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  83 SEGMLYMVFEFMEGSDLcfevvRRAVAGFVYSEAVACHYMRQILEALRYCHENDI---LHRDVRPACAL-LATVDN---- 154
Cdd:cd14145   76 KEPNLCLVMEFARGGPL-----NRVLSGKRIPPDILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILiLEKVENgdls 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 155 SAPVKLGGFGSAIQLPGTRETiethGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVA 233
Cdd:cd14145  151 NKILKITDFGLAREWHRTTKM----SAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGiDGLAVAYGVA 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 442620344 234 RGRLSFEAPEwkSISANAKDLVMKMLAANPHHRLSITEVLDH 275
Cdd:cd14145  227 MNKLSLPIPS--TCPEPFARLMEDCWNPDPHSRPPFTNILDQ 266
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
12-267 1.83e-22

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 100.16  E-value: 1.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05593   17 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKD--EVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVM 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPG 171
Cdd:cd05593   95 EYVNGGELFFHLSRERV----FSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGLCKEGIT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGRLSFEapewKSISAN 250
Cdd:cd05593  168 DAATMKTF--CGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDhEKLFELILMEDIKFP----RTLSAD 241
                        250
                 ....*....|....*..
gi 442620344 251 AKDLVMKMLAANPHHRL 267
Cdd:cd05593  242 AKSLLSGLLIKDPNKRL 258
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
12-278 3.77e-22

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 98.92  E-value: 3.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVdvakftaSP------GLSTAdlkREATICHMLKHPHIVELLE-----T 80
Cdd:cd07849    7 YQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKI-------SPfehqtyCLRTL---REIKILLRFKHENIIGILDiqrppT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  81 YSSEGMLYMVFEFMEgSDLCfevvrRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALL-ATVDnsapVK 159
Cdd:cd07849   77 FESFKDVYIVQELME-TDLY-----KLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLnTNCD----LK 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 160 LGGFGSA-IQLPGTRETIETHGRVGCPHYMAPEV-VTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQ-------- 229
Cdd:cd07849  147 ICDFGLArIADPEHDHTGFLTEYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQlnlilgil 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 230 --------QSV--ARGR-----LSFEAP-EWKSISANAK----DLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd07849  227 gtpsqedlNCIisLKARnyiksLPFKPKvPWNKLFPNADpkalDLLDKMLTFNPHKRITVEEALAHPYL 295
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-278 4.09e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 96.73  E-value: 4.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPF---SIVRRCihrESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd08221    2 YIPVRVLGRGAFgeaVLYRKT---EDNSLVVWKEVNLSRLSEK---ERRDALNEIDILSLLNHDNIITYYNHFLDGESLF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLCFEVVRRAvaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDnsaPVKLGGFGSAIQ 168
Cdd:cd08221   76 IEMEYCNGGNLHDKIAQQK--NQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKAD---LVKLGDFGISKV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPGTRETIETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGRLSFEAPEWksi 247
Cdd:cd08221  151 LDSESSMAESI--VGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNpLRLAVKIVQGEYEDIDEQY--- 225
                        250       260       270
                 ....*....|....*....|....*....|.
gi 442620344 248 SANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd08221  226 SEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
18-272 4.36e-22

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 96.74  E-value: 4.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHResNQQFAVKIVDVAKftaspglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd14058    1 VGRGSFGVVCKARWR--NQIVAVKIIESES-------EKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLcFEVVRRAVAGFVYSEAVACHYMRQILEALRYCH---ENDILHRDVRPACALLatVDNSAPVKLGGFGSAIqlpgtre 174
Cdd:cd14058   72 SL-YNVLHGKEPKPIYTAAHAMSWALQCAKGVAYLHsmkPKALIHRDLKPPNLLL--TNGGTVLKICDFGTAC------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 175 TIETHGRV--GCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF---LGSGVRLQQSVARGRlsfEAPEWKSISA 249
Cdd:cd14058  142 DISTHMTNnkGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFdhiGGPAFRIMWAVHNGE---RPPLIKNCPK 218
                        250       260
                 ....*....|....*....|...
gi 442620344 250 NAKDLVMKMLAANPHHRLSITEV 272
Cdd:cd14058  219 PIESLMTRCWSKDPEKRPSMKEI 241
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
7-266 4.62e-22

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 101.41  E-value: 4.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   7 LFDDVYELCEVIGKGPFSIVRR--CI--HREsnqqFAVKIVD---------VAKFtaspglstadlKREATICHMLKHPH 73
Cdd:NF033483   4 LLGGRYEIGERIGRGGMAEVYLakDTrlDRD----VAVKVLRpdlardpefVARF-----------RREAQSAASLSHPN 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  74 IVELLETYSSEGMLYMVFEFMEGSDLcFEVVRRavaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvD 153
Cdd:NF033483  69 IVSVYDVGEDGGIPYIVMEYVDGRTL-KDYIRE---HGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILI---T 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 154 NSAPVKLGGFGSAIQLPGTRETiETHGRVGCPHYMAPE-----VVTRRlygkgCDVWGAGVMLHVLLSGRLPFLG-SGVr 227
Cdd:NF033483 142 KDGRVKVTDFGIARALSSTTMT-QTNSVLGTVHYLSPEqarggTVDAR-----SDIYSLGIVLYEMLTGRPPFDGdSPV- 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442620344 228 lqqSVARGRLSFEAP---EW-KSISANAKDLVMKMLAANPHHR 266
Cdd:NF033483 215 ---SVAYKHVQEDPPppsELnPGIPQSLDAVVLKATAKDPDDR 254
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
12-222 5.74e-22

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 96.65  E-value: 5.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVdvAKFTASPGLSTADLK----REATICHML-KHPHIVELLETYSSEGM 86
Cdd:cd13993    2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCL--YKSGPNSKDGNDFQKlpqlREIDLHRRVsRHPNIITLHDVFETEVA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEGSDLcFEVVRrAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSapVKLGGFGSA 166
Cdd:cd13993   80 IYIVLEYCPNGDL-FEAIT-ENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGT--VKLCDFGLA 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 167 iqlpgTRETIETHGRVGCPHYMAPEVVTRRL-YGKGC-----DVWGAGVMLHVLLSGRLPFL 222
Cdd:cd13993  156 -----TTEKISMDFGVGSEFYMAPECFDEVGrSLKGYpcaagDIWSLGIILLNLTFGRNPWK 212
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
18-276 5.78e-22

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 96.30  E-value: 5.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVaKFTASPglSTADLKREATICHMLK-HPHIVELLETYSSEGMLYMVFEFMEG 96
Cdd:cd13997    8 IGSGSFSEVFKVRSKVDGCLYAVKKSKK-PFRGPK--ERARALREVEAHAALGqHPNIVRYYSSWEEGGHLYIQMELCEN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  97 SDLCfEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPGTRETI 176
Cdd:cd13997   85 GSLQ-DALEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFI---SNKGTCKIGDFGLATRLETSGDVE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 177 EthgrvGCPHYMAPEVVTRRL-YGKGCDVWGAGVMLHVLLSGrLPFLGSGVRLQQsVARGRLSFeaPEWKSISANAKDLV 255
Cdd:cd13997  161 E-----GDSRYLAPELLNENYtHLPKADIFSLGVTVYEAATG-EPLPRNGQQWQQ-LRQGKLPL--PPGLVLSQELTRLL 231
                        250       260
                 ....*....|....*....|.
gi 442620344 256 MKMLAANPHHRLSITEVLDHP 276
Cdd:cd13997  232 KVMLDPDPTRRPTADQLLAHD 252
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
12-277 5.82e-22

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 97.11  E-value: 5.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAkfTASPGL-STAdlKREATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd07861    2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLE--SEEEGVpSTA--IREISLLKELQHPNIVCLEDVLMQENRLYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEgSDLCFEVVRRAVAGFVYSEAVAcHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLp 170
Cdd:cd07861   78 FEFLS-MDLKKYLDSLPKGKYMDAELVK-SYLYQILQGILFCHSRRVLHRDLKPQNLL---IDNKGVIKLADFGLARAF- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRETIETHgRVGCPHYMAPEVVT-RRLYGKGCDVWGAGVMLHVLLSGRLPFLGS----------------------GVr 227
Cdd:cd07861  152 GIPVRVYTH-EVVTLWYRAPEVLLgSPRYSTPVDIWSIGTIFAEMATKKPLFHGDseidqlfrifrilgtptediwpGV- 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 228 lqQSVARGRLSFeaPEW---------KSISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07861  230 --TSLPDYKNTF--PKWkkgslrtavKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPY 284
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
18-277 7.25e-22

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 96.24  E-value: 7.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKivdvakFTASPGLSTADLKREATI-CHMLKHPHIVELLETYSsEGMLYMVF--EFM 94
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALK------FVPKPSTKLKDFLREYNIsLELSVHPHIIKTYDVAF-ETEDYYVFaqEYA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  95 EGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSApVKLGGFGSaiqlpgTRe 174
Cdd:cd13987   74 PYGDL-FSIIPPQVG---LPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRR-VKLCDFGL------TR- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 175 tiethgRVGCP--------HYMAPEVVTRRLYGKGC-----DVWGAGVMLHVLLSGRLPF---LGSGVRLQQSVA-RGRL 237
Cdd:cd13987  142 ------RVGSTvkrvsgtiPYTAPEVCEAKKNEGFVvdpsiDVWAFGVLLFCCLTGNFPWekaDSDDQFYEEFVRwQKRK 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 442620344 238 SFEAP-EWKSISANAKDLVMKMLAANPHHRLSITEV---LDHPW 277
Cdd:cd13987  216 NTAVPsQWRRFTPKALRMFKKLLAPEPERRCSIKEVfkyLGDRW 259
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
10-277 7.55e-22

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 96.67  E-value: 7.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQqfavkIVDVAKFTAS---PGLSTADLkREATICHMLKHPHIVELLETYSSEGM 86
Cdd:cd07847    1 EKYEKLSKIGEGSYGVVFKCRNRETGQ-----IVAIKKFVESeddPVIKKIAL-REIRMLKQLKHPNLVNLIEVFRRKRK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEGSDLcfEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVKLGGFGSA 166
Cdd:cd07847   75 LHLVFEYCDHTVL--NELEKNPRGV--PEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILIT---KQGQIKLCDFGFA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLPGTRETIETHgrVGCPHYMAPE-VVTRRLYGKGCDVWGAGVMLHVLLSGrLPF----------------LG------ 223
Cdd:cd07847  148 RILTGPGDDYTDY--VATRWYRAPElLVGDTQYGPPVDVWAIGCVFAELLTG-QPLwpgksdvdqlylirktLGdliprh 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620344 224 ----------SGVRLQQSVARGRLSFEAPewkSISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07847  225 qqifstnqffKGLSIPEPETREPLESKFP---NISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
17-279 9.76e-22

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 95.92  E-value: 9.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFS---IVRRCIHRESNQQFAVK------IVDVAKftaspglSTADLKREATICHMLKH-PHIVELLETYSSEGM 86
Cdd:cd05583    1 VLGTGAYGkvfLVRKVGGHDAGKLYAMKvlkkatIVQKAK-------TAEHTMTERQVLEAVRQsPFLVTLHYAFQTDAK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFG-S 165
Cdd:cd05583   74 LHLILDYVNGGELFTHLYQREH----FTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILL---DSEGHVVLTDFGlS 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 166 AIQLPGTREtiETHGRVGCPHYMAPEVVTR--RLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQS-VARGRLSFEAP 242
Cdd:cd05583  147 KEFLPGEND--RAYSFCGTIEYMAPEVVRGgsDGHDKAVDWWSLGVLTYELLTGASPFTVDGERNSQSeISKRILKSHPP 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 442620344 243 EWKSISANAKDLVMKMLAANPHHRL-----SITEVLDHPWIR 279
Cdd:cd05583  225 IPKTFSAEAKDFILKLLEKDPKKRLgagprGAHEIKEHPFFK 266
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
16-275 1.27e-21

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 95.30  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRC-IHRESNQ--QFAVKivdvakfTASPGLSTADLK---REATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd00192    1 KKLGEGAFGEVYKGkLKGGDGKtvDVAVK-------TLKEDASESERKdflKEARVMKKLGHPNVVRLLGVCTEEEPLYL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDL------CFEVVRRAVAGFVySEAVACHYMRQILEALRYCHENDILHRDvrpacalLAT----VDNSAPVK 159
Cdd:cd00192   74 VMEYMEGGDLldflrkSRPVFPSPEPSTL-SLKDLLSFAIQIAKGMEYLASKKFVHRD-------LAArnclVGEDLVVK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 160 LGGFGSAIQLPGTRETIETHGRVgCP-HYMAPEVVTRRLYGKGCDVWGAGVMLHVLLS-GRLPFLG-SGVRLQQSVARG- 235
Cdd:cd00192  146 ISDFGLSRDIYDDDYYRKKTGGK-LPiRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGlSNEEVLEYLRKGy 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 442620344 236 RLsfEAPEwkSISANAKDLVMKMLAANPHHRLSITEVLDH 275
Cdd:cd00192  225 RL--PKPE--NCPDELYELMLSCWQLDPEDRPTFSELVER 260
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
5-278 1.36e-21

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 95.85  E-value: 1.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   5 EILFDDVYELCEVIGKGPFSIVRRCIHRE-SNQQFAVKIVDVAKFTASPGLstadLKREATICHMLKHPHIVELLETYSS 83
Cdd:cd14201    1 EVVGDFEYSRKDLVGHGAFAVVFKGRHRKkTDWEVAIKSINKKNLSKSQIL----LGKEIKILKELQHENIVALYDVQEM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGMLYMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAP------ 157
Cdd:cd14201   77 PNSVFLVMEYCNGGDLADYLQAKGT----LSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKKSsvsgir 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 158 VKLGGFGSAIQLpgtRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRL 237
Cdd:cd14201  153 IKIADFGFARYL---QSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNK 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 442620344 238 SFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14201  230 NLQPSIPRETSPYLADLLLGLLQRNQKDRMDFEAFFSHPFL 270
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
18-279 1.36e-21

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 96.26  E-value: 1.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTadlkrEATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd06658   30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLFN-----EVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLCFEVVRRAVagfvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvdnSAPVKLGGFGSAIQLpgTRETIE 177
Cdd:cd06658  105 ALTDIVTHTRM-----NEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTS---DGRIKLSDFGFCAQV--SKEVPK 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 178 THGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWKSISANAKDLVMK 257
Cdd:cd06658  175 RKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKDSHKVSSVLRGFLDL 254
                        250       260
                 ....*....|....*....|..
gi 442620344 258 MLAANPHHRLSITEVLDHPWIR 279
Cdd:cd06658  255 MLVREPSQRATAQELLQHPFLK 276
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
12-279 1.41e-21

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 96.22  E-value: 1.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFS---IVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd05613    2 FELLKVLGTGAYGkvfLVRKVSGHDAGKLYAMKVLKKATIVQKAKTAEHTRTERQVLEHIRQSPFLVTLHYAFQTDTKLH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQ 168
Cdd:cd05613   82 LILDYINGGELFTHLSQRER----FTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILL---DSSGHVVLTDFGLSKE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPgTRETIETHGRVGCPHYMAPEVVTRRLYG--KGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQS-VARGRLSFEAPEWK 245
Cdd:cd05613  155 FL-LDENERAYSFCGTIEYMAPEIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAeISRRILKSEPPYPQ 233
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 442620344 246 SISANAKDLVMKMLAANPHHRL-----SITEVLDHPWIR 279
Cdd:cd05613  234 EMSALAKDIIQRLLMKDPKKRLgcgpnGADEIKKHPFFQ 272
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
12-277 1.44e-21

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 96.03  E-value: 1.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAkfTASPGL-STAdlKREATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd07860    2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLD--TETEGVpSTA--IREISLLKELNHPNIVKLLDVIHTENKLYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEgSDLCFEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLp 170
Cdd:cd07860   78 FEFLH-QDLKKFMDASALTGI--PLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLL---INTEGAIKLADFGLARAF- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRETIETHgRVGCPHYMAPEVVT-RRLYGKGCDVWGAGVMLHVLLSGRLPFLGS----------------------GVr 227
Cdd:cd07860  151 GVPVRTYTH-EVVTLWYRAPEILLgCKYYSTAVDIWSLGCIFAEMVTRRALFPGDseidqlfrifrtlgtpdevvwpGV- 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 228 lqQSVARGRLSFeaPEWK---------SISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07860  229 --TSMPDYKPSF--PKWArqdfskvvpPLDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
9-299 1.60e-21

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 95.50  E-value: 1.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   9 DDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglsTADLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd06640    3 EELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDE----IEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDlCFEVVRravAGfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVKLGGFGSAIQ 168
Cdd:cd06640   79 IIMEYLGGGS-ALDLLR---AG-PFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLS---EQGDVKLADFGVAGQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPGTRETIETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPflgsgvrlQQSVARGRLSFEAPEWKS-- 246
Cdd:cd06640  151 LTDTQIKRNTF--VGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP--------NSDMHPMRVLFLIPKNNPpt 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344 247 ----ISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKlQRTHLADTVEELKRY 299
Cdd:cd06640  221 lvgdFSKPFKEFIDACLNKDPSFRPTAKELLKHKFIVKNAK-KTSYLTELIDRFKRW 276
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
9-299 1.71e-21

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 95.52  E-value: 1.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   9 DDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglsTADLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd06641    3 EELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDE----IEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDlCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVKLGGFGSAIQ 168
Cdd:cd06641   79 IIMEYLGGGS-ALDLLEPGP----LDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLS---EHGEVKLADFGVAGQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPGTRetIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPflgsgvrlQQSVARGRLSFEAPEWK--- 245
Cdd:cd06641  151 LTDTQ--IKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPP--------HSELHPMKVLFLIPKNNppt 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344 246 ---SISANAKDLVMKMLAANPHHRLSITEVLDHPWIRdRDKLQRTHLADTVEELKRY 299
Cdd:cd06641  221 legNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFIL-RNAKKTSYLTELIDRYKRW 276
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
16-274 1.75e-21

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 95.14  E-value: 1.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHResNQQFAVKIVD-VAKFTASpglsTADLKREATICHmLKHPHIVELL-----ETYSSEGMLYM 89
Cdd:cd13979    9 EPLGSGGFGSVYKATYK--GETVAVKIVRrRRKNRAS----RQSFWAELNAAR-LRHENIVRVLaaetgTDFASLGLIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 vfEFMEGSDLcFEVVRRAvAGFVYSEAVAChYMRQILEALRYCHENDILHRDVRPACALLAtvDNSAPvKLGGFGSAIQL 169
Cdd:cd13979   82 --EYCGNGTL-QQLIYEG-SEPLPLAHRIL-ISLDIARALRFCHSHGIVHLDVKPANILIS--EQGVC-KLCDFGCSVKL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PGTREtIETHGRV--GCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARG-RLSFEAPEWK 245
Cdd:cd13979  154 GEGNE-VGTPRSHigGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGlRQHVLYAVVAKDlRPDLSGLEDS 232
                        250       260
                 ....*....|....*....|....*....
gi 442620344 246 SISANAKDLVMKMLAANPHHRLSITEVLD 274
Cdd:cd13979  233 EFGQRLRSLISRCWSAQPAERPNADESLL 261
PDZ_MPP3-MPP4-MPP7-like cd06799
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ...
493-574 1.92e-21

PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP3, MPP4, and MPP7, and related domains. MPP3 (also known as MAGUK p55 subfamily member 3, erythrocyte membrane protein p55, or EMP55), MPP4 (also known as MAGUK p55 subfamily member 4 or Discs large homolog 6), and MPP7 (also known as MAGUK p55 subfamily member 7) are membrane-associated guanylate kinase (MAGUK)-like proteins. MPP3 is part of a cell adhesion protein complex including tumor suppressor CADM1 and actin-binding protein 4.1B. Participation in the Crumbs cell polarity complex has also been demonstrated for MPP7 in epithelial cells, and for MPP3 and MPP4 in the retina. MPP4 is needed for proper localization of plasma membrane calcium ATPases and maintenance of calcium homeostasis at the rod photoreceptor synaptic terminals. Binding partners of the MPP3 PDZ domain include nectin-3, serotonin 5-hydroxytryptamine, 5-HT(2C) receptor, and a cell adhesion protein, TSLC1 (tumor suppressor in lung cancer 1); fragments of MPP4 having the PDZ domain bind CRB (PDZ-SH3-GUK) and GABA transporter GAT1 (PDZ-SH3). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467260 [Multi-domain]  Cd Length: 81  Bit Score: 89.22  E-value: 1.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 493 VRLVqfqKNtDEPMGITLKMTED-GRCIVARIMHGGMIHRQATLHVGDEIREINGQPVQHQSVGQLQRMLREARGSVTFK 571
Cdd:cd06799    3 VRLV---KN-NEPLGATIKRDEKtGAIVVARIMRGGAADRSGLIHVGDELREVNGISVEGKDPEEVIQILANSQGPITFK 78

                 ...
gi 442620344 572 IVP 574
Cdd:cd06799   79 LIP 81
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
18-273 1.93e-21

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 95.09  E-value: 1.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVakFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd08228   10 IGRGQFSEVYRATCLLDRKPVALKKVQI--FEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELADAG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLC-----FEVVRRAVAgfvysEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvdnSAPVKLGGFGSAIQLpgT 172
Cdd:cd08228   88 DLSqmikyFKKQKRLIP-----ERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITA---TGVVKLGDLGLGRFF--S 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 173 RETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLqQSVARGRLSFEAPEW--KSISAN 250
Cdd:cd08228  158 SKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNL-FSLCQKIEQCDYPPLptEHYSEK 236
                        250       260
                 ....*....|....*....|...
gi 442620344 251 AKDLVMKMLAANPHHRLSITEVL 273
Cdd:cd08228  237 LRELVSMCIYPDPDQRPDIGYVH 259
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
17-278 1.99e-21

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 95.10  E-value: 1.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIV----DVAKFTAspglstadLKREATICHMLKHPHIVELLETYSSEGMLYMVFE 92
Cdd:cd06605    8 ELGEGNGGVVSKVRHRPSGQIMAVKVIrleiDEALQKQ--------ILRELDVLHKCNSPYIVGFYGAFYSEGDISICME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  93 FMEGSdlCFEVVRRAVAGFvySEAVACHYMRQILEALRYCHEN-DILHRDVRPACALlatVDNSAPVKLGGFGSAIQLpg 171
Cdd:cd06605   80 YMDGG--SLDKILKEVGRI--PERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNIL---VNSRGQVKLCDFGVSGQL-- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 tretIETHGR--VGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR--------LQQSVARgrlsfEA 241
Cdd:cd06605  151 ----VDSLAKtfVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKpsmmifelLSYIVDE-----PP 221
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 442620344 242 PEWKS--ISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06605  222 PLLPSgkFSPDFQDFVSQCLQKDPTERPSYKELMEHPFI 260
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
12-289 2.62e-21

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 95.84  E-value: 2.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIvdvakftaspglstadLKREATI------CHML---------KHPHIVE 76
Cdd:cd05616    2 FNFLMVLGKGSFGKVMLAERKGTDELYAVKI----------------LKKDVVIqdddveCTMVekrvlalsgKPPFLTQ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  77 LLETYSSEGMLYMVFEFMEGSDLCFEVvrRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSA 156
Cdd:cd05616   66 LHSCFQTMDRLYFVMEYVNGGDLMYHI--QQVGRF--KEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVML---DSEG 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 157 PVKLGGFGSAIQlpGTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARG 235
Cdd:cd05616  139 HIKIADFGMCKE--NIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEdELFQSIMEH 216
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620344 236 RLSFEapewKSISANAKDLVMKMLAANPHHRLSI-----TEVLDHPWIR--DRDKLQRTHL 289
Cdd:cd05616  217 NVAYP----KSMSKEAVAICKGLMTKHPGKRLGCgpegeRDIKEHAFFRyiDWEKLERKEI 273
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
9-299 3.26e-21

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 94.74  E-value: 3.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   9 DDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglsTADLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd06642    3 EELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDE----IEDIQQEITVLSQCDSPYITRYYGSYLKGTKLW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDlCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVKLGGFGSAIQ 168
Cdd:cd06642   79 IIMEYLGGGS-ALDLLKPGP----LEETYIATILREILKGLDYLHSERKIHRDIKAANVLLS---EQGDVKLADFGVAGQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPGTRetIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFlgsgvrlqQSVARGRLSFEAPEWKSIS 248
Cdd:cd06642  151 LTDTQ--IKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPN--------SDLHPMRVLFLIPKNSPPT 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344 249 ANA------KDLVMKMLAANPHHRLSITEVLDHPWIRDRDKlQRTHLADTVEELKRY 299
Cdd:cd06642  221 LEGqhskpfKEFVEACLNKDPRFRPTAKELLKHKFITRYTK-KTSFLTELIDRYKRW 276
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
18-283 3.29e-21

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 94.80  E-value: 3.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVdvakfTASPglsTADLK----REATICHMLKHPHIVELLETY--SSEGMLYMVF 91
Cdd:cd06621    9 LGEGAGGSVTKCRLRNTKTIFALKTI-----TTDP---NPDVQkqilRELEINKSCASPYIVKYYGAFldEQDSSIGIAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDL--CFEVVRRAvaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSAIQL 169
Cdd:cd06621   81 EYCEGGSLdsIYKKVKKK--GGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQ---VKLCDFGVSGEL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PGTRETIEThgrvGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGvrlQQSVARGRL-----SFEAPEW 244
Cdd:cd06621  156 VNSLAGTFT----GTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEG---EPPLGPIELlsyivNMPNPEL 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 442620344 245 K-------SISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDK 283
Cdd:cd06621  229 KdepengiKWSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEK 274
gmk PRK00300
guanylate kinase; Provisional
714-882 4.57e-21

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 92.07  E-value: 4.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 714 LVLLGAHGVGrrhiKNTLIS---KYPDKYAYPIPHTTRPAKPEEENGRSYYFVSHDEMMADIGANEYLEYGTHEDAMYGT 790
Cdd:PRK00300   8 IVLSGPSGAG----KSTLVKallERDPNLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYYGT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 791 KLDTIRRIHTEGKMAILDVEPQ-ALKILRTAeftPYVV--FIAAPSLQN---------------IAdydgslERLAK-ES 851
Cdd:PRK00300  84 PRSPVEEALAAGKDVLLEIDWQgARQVKKKM---PDAVsiFILPPSLEElerrlrgrgtdseevIA------RRLAKaRE 154
                        170       180       190
                 ....*....|....*....|....*....|.
gi 442620344 852 EMLRQlygHFFDLTIVNNDISETIATLETAI 882
Cdd:PRK00300 155 EIAHA---SEYDYVIVNDDLDTALEELKAII 182
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
6-278 5.82e-21

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 94.31  E-value: 5.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   6 ILFD------DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglstaDLKREATICHMLK-HPHIVELL 78
Cdd:cd06638    8 IIFDsfpdpsDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDE------EIEAEYNILKALSdHPNVVKFY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  79 ETYSSEGM-----LYMVFEFMEG---SDLCFEVVRRavaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLA 150
Cdd:cd06638   82 GMYYKKDVkngdqLWLVLELCNGgsvTDLVKGFLKR---GERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 151 TvdnSAPVKLGGFGSAIQLPGTRETIEThgRVGCPHYMAPEVVT--RRL---YGKGCDVWGAGVMLHVLLSGRLPFLG-S 224
Cdd:cd06638  159 T---EGGVKLVDFGVSAQLTSTRLRRNT--SVGTPFWMAPEVIAceQQLdstYDARCDVWSLGITAIELGDGDPPLADlH 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442620344 225 GVRLQQSVARG-RLSFEAPE-WksiSANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06638  234 PMRALFKIPRNpPPTLHQPElW---SNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
SH3_MPP7 cd12033
Src Homology 3 domain of Membrane Protein, Palmitoylated 7 (or MAGUK p55 subfamily member 7); ...
586-643 6.69e-21

Src Homology 3 domain of Membrane Protein, Palmitoylated 7 (or MAGUK p55 subfamily member 7); MPP7 is a scaffolding protein that binds to DLG1 and promotes tight junction formation and epithelial cell polarity. Mutations in the MPP7 gene may be associated with the pathogenesis of diabetes and extreme bone mineral density. It is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212966  Cd Length: 61  Bit Score: 87.00  E-value: 6.69e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 586 FVRAQFDYNPLDDELIPCAQAGISFQVGDILQIISKDDHHWWQARLDTVGG-SAGLIPS 643
Cdd:cd12033    1 FIKALFDYNPNEDKAIPCKEAGLSFKKGDILQIMSQDDATWWQAKHEGDANpRAGLIPS 59
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
17-282 1.05e-20

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 94.17  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKReaTICHMLKHPHIVELLETYSSEGMLYMVFEFMEG 96
Cdd:cd05585    1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAER--TVLAQVDCPFIVPLKFSFQSPEKLYLVLAFING 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  97 SDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGsaIQLPGTRETI 176
Cdd:cd05585   79 GELFHHLQREGR----FDLSRARFYTAELLCALECLHKFNVIYRDLKPENILL---DYTGHIALCDFG--LCKLNMKDDD 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 177 ETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRLSFEAPewksISANAKDLV 255
Cdd:cd05585  150 KTNTFCGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTnEMYRKILQEPLRFPDG----FDRDAKDLL 225
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 256 MKMLAANPHHRLSI---TEVLDHPWIRDRD 282
Cdd:cd05585  226 IGLLNRDPTKRLGYngaQEIKNHPFFDQID 255
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
12-278 1.36e-20

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 92.33  E-value: 1.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLStadlkrEATICHMLK------HPHIVELLETYSSEG 85
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLD------EIRLLELLNkkdkadKYHIVRLKDVFYFKN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 MLYMVFEfMEGSDLcFEVVRRAVagFVY-SEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSApVKLGGFG 164
Cdd:cd14133   75 HLCIVFE-LLSQNL-YEFLKQNK--FQYlSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQ-IKIIDFG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 SAIQlpgtrETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVrlQQSVARGRLSFEAPEW 244
Cdd:cd14133  150 SSCF-----LTQRLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASE--VDQLARIIGTIGIPPA 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 442620344 245 KSISANA------KDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14133  223 HMLDQGKaddelfVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
9-277 1.89e-20

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 93.20  E-value: 1.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   9 DDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftASPGLSTADLkREATICHMLKHPHIVELLETYSSE---- 84
Cdd:cd07865   11 VSKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMEN--EKEGFPITAL-REIKILQLLKHENVVNLIEICRTKatpy 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  85 ----GMLYMVFEFMEgSDLcfevvrravAGFV------YSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDN 154
Cdd:cd07865   88 nrykGSIYLVFEFCE-HDL---------AGLLsnknvkFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANIL---ITK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 155 SAPVKLGGFG--SAIQLPGTRETIETHGRVGCPHYMAPEVVT-RRLYGKGCDVWGAGVMLHVLLSgRLPFLGSGVRLQQ- 230
Cdd:cd07865  155 DGVLKLADFGlaRAFSLAKNSQPNRYTNRVVTLWYRPPELLLgERDYGPPIDMWGAGCIMAEMWT-RSPIMQGNTEQHQl 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620344 231 ---SVARGRLSFEA-------PEWKSI-------------------SANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07865  234 tliSQLCGSITPEVwpgvdklELFKKMelpqgqkrkvkerlkpyvkDPYALDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
17-275 1.89e-20

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 92.41  E-value: 1.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHResNQQFAVKIV------DVAkftaspglSTAD-LKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd14146    1 IIGVGGFGKVYRATWK--GQEVAVKAArqdpdeDIK--------ATAEsVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLcfevvRRAVAGFVYSEA----------VACHYMRQILEALRYCHEN---DILHRDVRPA-CALLATVDN- 154
Cdd:cd14146   71 VMEFARGGTL-----NRALAAANAAPGprrarripphILVNWAVQIARGMLYLHEEavvPILHRDLKSSnILLLEKIEHd 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 155 ---SAPVKLGGFGSAIQLPGTRETiethGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQ 230
Cdd:cd14146  146 dicNKTLKITDFGLAREWHRTTKM----SAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGiDGLAVAY 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 442620344 231 SVARGRLSFEAPEwkSISANAKDLVMKMLAANPHHRLSITEVLDH 275
Cdd:cd14146  222 GVAVNKLTLPIPS--TCPEPFAKLMKECWEQDPHIRPSFALILEQ 264
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
12-277 2.12e-20

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 92.34  E-value: 2.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAkfTASPGLSTADLkREATICHMLK---HPHIVELLE-----TYSS 83
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVP--LSEEGIPLSTI-REIALLKQLEsfeHPNVVRLLDvchgpRTDR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGMLYMVFEFMEgSDLCFEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGF 163
Cdd:cd07838   78 ELKLTLVFEHVD-QDLATYLDKCPKPGL--PPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNIL---VTSDGQVKLADF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 164 GSAiqlpgtretiethgRVGCPH-----------YMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGvRLQQ-- 230
Cdd:cd07838  152 GLA--------------RIYSFEmaltsvvvtlwYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSS-EADQlg 216
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 231 ------------------SVARGRLSFEAPEWK-----SISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07838  217 kifdviglpseeewprnsALPRSSFPSYTPRPFksfvpEIDEEGLDLLKKMLTFNPHKRISAFEALQHPY 286
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
12-280 2.26e-20

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 93.07  E-value: 2.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvaKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05574    3 FKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLD--KEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEVVRRAvAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALL----------------ATVDNS 155
Cdd:cd05574   81 DYCPGGEL-FRLLQKQ-PGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLhesghimltdfdlskqSSVTPP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 156 APVKLGGFGSA--IQLPGTRETIE------THGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSgvR 227
Cdd:cd05574  159 PVRKSLRKGSRrsSVKSIEKETFVaepsarSNSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGS--N 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 228 LQQ---SVARGRLSFeaPEWKSISANAKDLVMKMLAANPHHRL----SITEVLDHPWIRD 280
Cdd:cd05574  237 RDEtfsNILKKELTF--PESPPVSSEAKDLIRKLLVKDPSKRLgskrGASEIKRHPFFRG 294
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
18-275 2.32e-20

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 91.95  E-value: 2.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCiHRESNQQFAVKIVDVAKFTASPGlstaDLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd14066    1 IGSGGFGTVYKG-VLENGTVVAVKRLNEMNCAASKK----EFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLcFEVVRRAVAGFVYSEAVACHYMRQILEALRYCHE---NDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPGTRE 174
Cdd:cd14066   76 SL-EDRLHCHKGSPPLPWPQRLKIAKGIARGLEYLHEecpPPIIHGDIKSSNILL---DEDFEPKLTDFGLARLIPPSES 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 175 TIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF-----LGSGVRLQQSVAR-GRLSFEA---PEWK 245
Cdd:cd14066  152 VSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVdenreNASRKDLVEWVESkGKEELEDildKRLV 231
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 442620344 246 SISANAKDLVMKML-------AANPHHRLSITEVLDH 275
Cdd:cd14066  232 DDDGVEEEEVEALLrlallctRSDPSLRPSMKEVVQM 268
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
10-298 3.02e-20

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 92.22  E-value: 3.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIV----DVAKFTAspglstadLKREATICHMLKHPHIVELLETYSSEG 85
Cdd:cd06622    1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIrlelDESKFNQ--------IIMELDILHKAVSPYIVDFYGAFFIEG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 MLYMVFEFMEGSDLcfevvRRAVAGFVYSEAVACHYMRQILEA----LRYCHEN-DILHRDVRPACALlatVDNSAPVKL 160
Cdd:cd06622   73 AVYMCMEYMDAGSL-----DKLYAGGVATEGIPEDVLRRITYAvvkgLKFLKEEhNIIHRDVKPTNVL---VNGNGQVKL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 161 GGFGSAIQLpgtrETIETHGRVGCPHYMAPEVVT------RRLYGKGCDVWGAGVMLHVLLSGRLPF---LGSGVRLQ-Q 230
Cdd:cd06622  145 CDFGVSGNL----VASLAKTNIGCQSYMAPERIKsggpnqNPTYTVQSDVWSLGLSILEMALGRYPYppeTYANIFAQlS 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 231 SVARGRLSFEAPEWksiSANAKDLVMKMLAANPHHRLSITEVLDHPWIRdRDKLQRTHLADTVEE-LKR 298
Cdd:cd06622  221 AIVDGDPPTLPSGY---SDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLV-KYKNADVDMAEWVTGaLKR 285
SH3_MPP5 cd12036
Src Homology 3 domain of Membrane Protein, Palmitoylated 5 (or MAGUK p55 subfamily member 5); ...
587-645 3.44e-20

Src Homology 3 domain of Membrane Protein, Palmitoylated 5 (or MAGUK p55 subfamily member 5); MPP5, also called PALS1 (Protein associated with Lin7) or Nagie oko protein in zebrafish or Stardust in Drosophila, is a scaffolding protein which associates with Crumbs homolog 1 (CRB1), CRB2, or CRB3 through its PDZ domain and with PALS1-associated tight junction protein (PATJ) or multi-PDZ domain protein 1 (MUPP1) through its L27 domain. The resulting tri-protein complexes are core proteins of the Crumb complex, which localizes at tight junctions or subapical regions, and is involved in the maintenance of apical-basal polarity in epithelial cells and the morphogenesis and function of photoreceptor cells. MPP5 is critical for the proper stratification of the retina and is also expressed in T lymphocytes where it is important for TCR-mediated activation of NFkB. Drosophila Stardust exists in several isoforms, some of which show opposing functions in photoreceptor cells, which suggests that the relative ratio of different Crumbs complexes regulates photoreceptor homeostasis. MPP5 contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212969  Cd Length: 63  Bit Score: 84.77  E-value: 3.44e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 587 VRAQFDYNPLDDELIPCAQAGISFQVGDILQIISKDDHHWWQARLD---TVGGSAGLIPSPE 645
Cdd:cd12036    2 VRAHFDYDPEDDPYIPCRELGLSFQKGDILHVISQEDPNWWQAYREgeeDNQSLAGLIPSKS 63
SH3_MPP2 cd12037
Src Homology 3 domain of Membrane Protein, Palmitoylated 2 (or MAGUK p55 subfamily member 2); ...
586-643 3.59e-20

Src Homology 3 domain of Membrane Protein, Palmitoylated 2 (or MAGUK p55 subfamily member 2); MPP2 is a scaffolding protein that interacts with the non-receptor tyrosine kinase c-Src in epithelial cells to negatively regulate its activity and morphological function. It is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212970  Cd Length: 59  Bit Score: 84.62  E-value: 3.59e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 586 FVRAQFDYNPLDDELIPCAQAGISFQVGDILQIISKDDHHWWQARLdTVGGSAGLIPS 643
Cdd:cd12037    1 FVKCHFDYDPSSDSLIPCKEAGLKFRAGDLLQIVNQEDPNWWQACH-VEGGSAGLIPS 57
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
12-267 5.27e-20

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 92.78  E-value: 5.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKI----VDVAKFTASPGLStadlkrEATICHMLKHPHIVELLETYSSEGML 87
Cdd:cd05594   27 FEYLKLLGKGTFGKVILVKEKATGRYYAMKIlkkeVIVAKDEVAHTLT------ENRVLQNSRHPFLTALKYSFQTHDRL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCH-ENDILHRDVRPACALLatvDNSAPVKLGGFGSA 166
Cdd:cd05594  101 CFVMEYANGGELFFHLSRERV----FSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLML---DKDGHIKITDFGLC 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQlpGTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVARGRLSFEapewK 245
Cdd:cd05594  174 KE--GIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDhEKLFELILMEEIRFP----R 247
                        250       260
                 ....*....|....*....|..
gi 442620344 246 SISANAKDLVMKMLAANPHHRL 267
Cdd:cd05594  248 TLSPEAKSLLSGLLKKDPKQRL 269
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
61-275 6.88e-20

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 90.82  E-value: 6.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  61 REATICHMLKHPHIVELL-------ETYSSEgmLYMVFEFMEGSDLCFEVVRRAVAGFVYSEAVACHYMRQILEALRYCH 133
Cdd:cd13986   46 REIENYRLFNHPNILRLLdsqivkeAGGKKE--VYLLLPYYKRGSLQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMH 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 134 ENDIL---HRDVRPACALLAtvDNSAPVkLGGFGSA----IQLPGTRETI---ETHGRVGCPHYMAPE---VVTRRLYGK 200
Cdd:cd13986  124 EPELVpyaHRDIKPGNVLLS--EDDEPI-LMDLGSMnparIEIEGRREALalqDWAAEHCTMPYRAPElfdVKSHCTIDE 200
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 201 GCDVWGAGVMLHVLLSGRLPF---LGSGVRLQQSVARGRLSFeaPEWKSISANAKDLVMKMLAANPHHRLSITEVLDH 275
Cdd:cd13986  201 KTDIWSLGCTLYALMYGESPFeriFQKGDSLALAVLSGNYSF--PDNSRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
18-278 6.93e-20

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 91.24  E-value: 6.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTadlkrEATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd06657   28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLFN-----EVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLCFEVVRRAVagfvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVKLGGFGSAIQLpgTRETIE 177
Cdd:cd06657  103 ALTDIVTHTRM-----NEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLT---HDGRVKLSDFGFCAQV--SKEVPR 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 178 THGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWKSISANAKDLVMK 257
Cdd:cd06657  173 RKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNLHKVSPSLKGFLDR 252
                        250       260
                 ....*....|....*....|.
gi 442620344 258 MLAANPHHRLSITEVLDHPWI 278
Cdd:cd06657  253 LLVRDPAQRATAAELLKHPFL 273
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
10-282 7.02e-20

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 91.91  E-value: 7.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIV--DVAkftaspglstadLKREATICHMLK---------HPHIVELL 78
Cdd:cd05619    5 EDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALkkDVV------------LMDDDVECTMVEkrvlslaweHPFLTHLF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  79 ETYSSEGMLYMVFEFMEGSDLCFEVvrRAVAGFVYSEAVacHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPV 158
Cdd:cd05619   73 CTFQTKENLFFVMEYLNGGDLMFHI--QSCHKFDLPRAT--FYAAEIICGLQFLHSKGIVYRDLKLDNILL---DKDGHI 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 159 KLGGFGSAiqlpgtRETI----ETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG-VRLQQSVA 233
Cdd:cd05619  146 KIADFGMC------KENMlgdaKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDeEELFQSIR 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 442620344 234 RGRLSFeaPEWksISANAKDLVMKMLAANPHHRLSIT-EVLDHPWIRDRD 282
Cdd:cd05619  220 MDNPFY--PRW--LEKEAKDILVKLFVREPERRLGVRgDIRQHPFFREIN 265
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
18-282 8.60e-20

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 91.48  E-value: 8.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREATICHMLKH-PHIVELLETYSSEGMLYMVFEFMEG 96
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILVRTALDEsPFIVGLKFSFQTPTDLYLVTDYMSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  97 SDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGsaIQLPGTRETI 176
Cdd:cd05586   81 GELFWHLQKEGR----FSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILL---DANGHIALCDFG--LSKADLTDNK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 177 ETHGRVGCPHYMAPEV-VTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRLSFeaPEwKSISANAKDL 254
Cdd:cd05586  152 TTNTFCGTTEYLAPEVlLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTqQMYRNIAFGKVRF--PK-DVLSDEGRSF 228
                        250       260       270
                 ....*....|....*....|....*....|..
gi 442620344 255 VMKMLAANPHHRL----SITEVLDHPWIRDRD 282
Cdd:cd05586  229 VKGLLNRNPKHRLgahdDAVELKEHPFFADID 260
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
10-278 8.88e-20

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 91.02  E-value: 8.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftASPGLSTADLkREATICHMLKHPHIVELLETYSSE----- 84
Cdd:cd07864    7 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDN--EKEGFPITAI-REIKILRQLNHRSVVNLKEIVTDKqdald 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  85 -----GMLYMVFEFMEgsdlcFEVVRRAVAGFV-YSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPV 158
Cdd:cd07864   84 fkkdkGAFYLVFEYMD-----HDLMGLLESGLVhFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILL---NNKGQI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 159 KLGGFGSAiQLPGTRETIETHGRVGCPHYMAPEVVT-RRLYGKGCDVWGAGVMLHVLLSGRlPFLGSGVRLQQSVARGRL 237
Cdd:cd07864  156 KLADFGLA-RLYNSEESRPYTNKVITLWYRPPELLLgEERYGPAIDVWSCGCILGELFTKK-PIFQANQELAQLELISRL 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 238 S-----------FEAPEWKS-----------------ISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd07864  234 CgspcpavwpdvIKLPYFNTmkpkkqyrrrlreefsfIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
17-286 1.03e-19

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 91.22  E-value: 1.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFtaspglstadLKREATICHM---------LKHPHIVELLETYSSEGML 87
Cdd:cd05575    2 VIGKGSFGKVLLARHKAEGKLYAVKVLQKKAI----------LKRNEVKHIMaernvllknVKHPFLVGLHYSFQTKDKL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFG--- 164
Cdd:cd05575   72 YFVLDYVNGGELFFHLQRERH----FPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILL---DSQGHVVLTDFGlck 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 SAIQLPGTRETIethgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRLSFEApe 243
Cdd:cd05575  145 EGIEPSDTTSTF-----CGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTaEMYDNILHKPLRLRT-- 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 442620344 244 wkSISANAKDLVMKMLAANPHHRL----SITEVLDHPWIR--DRDKLQR 286
Cdd:cd05575  218 --NVSPSARDLLEGLLQKDRTKRLgsgnDFLEIKNHSFFRpiNWDDLEA 264
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
10-276 1.11e-19

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 90.68  E-value: 1.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKI---VDVAKFtaspglstadlKREATICHMLK-HPHIVELL------- 78
Cdd:cd14132   18 DDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVlkpVKKKKI-----------KREIKILQNLRgGPNIVKLLdvvkdpq 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  79 -ETYSsegmlyMVFEFMEGSDLcfevvRRAVAGFVYSEAvaCHYMRQILEALRYCHENDILHRDVRPACALlatVDNS-A 156
Cdd:cd14132   87 sKTPS------LIFEYVNNTDF-----KTLYPTLTDYDI--RYYMYELLKALDYCHSKGIMHRDVKPHNIM---IDHEkR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 157 PVKLGGFGSA-IQLPGTRETIethgRVGCPHYMAPEV-VTRRLYGKGCDVWGAGVMLHVLLSGRLPF------------- 221
Cdd:cd14132  151 KLRLIDWGLAeFYHPGQEYNV----RVASRYYKGPELlVDYQYYDYSLDMWSLGCMLASMIFRKEPFfhghdnydqlvki 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344 222 ---LGS----------GVRLQQSVARGRLSFEAPEWKS---------ISANAKDLVMKMLAANPHHRLSITEVLDHP 276
Cdd:cd14132  227 akvLGTddlyayldkyGIELPPRLNDILGRHSKKPWERfvnsenqhlVTPEALDLLDKLLRYDHQERITAKEAMQHP 303
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
11-278 1.29e-19

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 89.24  E-value: 1.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  11 VYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREATICHMLKHPH--IVELLETYSSEGMLY 88
Cdd:cd14102    1 VYQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVPLEIVLLKKVGSGFrgVIKLLDWYERPDGFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLCFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvdNSAPVKLGGFGSAIQ 168
Cdd:cd14102   81 IVMERPEPVKDLFDFITEKGA---LDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDL--RTGELKLIDFGSGAL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPGTRETIETHGRVgcphYMAPEVVT-RRLYGKGCDVWGAGVMLHVLLSGRLPFlgsgvRLQQSVARGRLSFEapewKSI 247
Cdd:cd14102  156 LKDTVYTDFDGTRV----YSPPEWIRyHRYHGRSATVWSLGVLLYDMVCGDIPF-----EQDEEILRGRLYFR----RRV 222
                        250       260       270
                 ....*....|....*....|....*....|.
gi 442620344 248 SANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14102  223 SPECQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
9-279 1.57e-19

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 90.09  E-value: 1.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   9 DDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvakfTASPGlSTADLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd06644   11 NEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIE----TKSEE-ELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLW 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEG---SDLCFEVVRravaGFVYSE-AVAChymRQILEALRYCHENDILHRDVRPACALLaTVDNSapVKLGGFG 164
Cdd:cd06644   86 IMIEFCPGgavDAIMLELDR----GLTEPQiQVIC---RQMLEALQYLHSMKIIHRDLKAGNVLL-TLDGD--IKLADFG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 SAIQLPGTRETIETHgrVGCPHYMAPEVVTRRL-----YGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGR-L 237
Cdd:cd06644  156 VSAKNVKTLQRRDSF--IGTPYWMAPEVVMCETmkdtpYDYKADIWSLGITLIEMAQIEPPHHElNPMRVLLKIAKSEpP 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442620344 238 SFEAP-EWksiSANAKDLVMKMLAANPHHRLSITEVLDHPWIR 279
Cdd:cd06644  234 TLSQPsKW---SMEFRDFLKTALDKHPETRPSAAQLLEHPFVS 273
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
17-285 2.17e-19

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 90.83  E-value: 2.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREaTICHMLKHPHIVELLETYSSEGMLYMVFEFMEG 96
Cdd:cd05615   17 VLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKR-VLALQDKPPFLTQLHSCFQTVDRLYFVMEYVNG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  97 SDLCFEVvrRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQlpGTRETI 176
Cdd:cd05615   96 GDLMYHI--QQVGKF--KEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVML---DSEGHIKIADFGMCKE--HMVEGV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 177 ETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRLSFEapewKSISANAKDLV 255
Cdd:cd05615  167 TTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEdELFQSIMEHNVSYP----KSLSKEAVSIC 242
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 442620344 256 MKMLAANPHHRLSI-----TEVLDHPWIR--DRDKLQ 285
Cdd:cd05615  243 KGLMTKHPAKRLGCgpegeRDIREHAFFRriDWDKLE 279
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
10-277 2.67e-19

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 89.51  E-value: 2.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAkfTASPGLSTADLkREATICHMLKH-PHIVELLETYSSE---- 84
Cdd:cd07837    1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLE--MEEEGVPSTAL-REVSLLQMLSQsIYIVRLLDVEHVEengk 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  85 GMLYMVFEFMEgSDL--CFEVVRRAVAGFVYSEAVAcHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGG 162
Cdd:cd07837   78 PLLYLVFEYLD-TDLkkFIDSYGRGPHNPLPAKTIQ-SFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLLKIADLG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 163 FGSAIQLPGTRETIEthgrVGCPHYMAPEVVT-RRLYGKGCDVWGAGVMLhVLLSGRLPFLGSGVRLQQ----------- 230
Cdd:cd07837  156 LGRAFTIPIKSYTHE----IVTLWYRAPEVLLgSTHYSTPVDMWSVGCIF-AEMSRKQPLFPGDSELQQllhifrllgtp 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 231 ------SVARGRLSFEAPEWK---------SISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07837  231 neevwpGVSKLRDWHEYPQWKpqdlsravpDLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
12-276 2.72e-19

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 89.02  E-value: 2.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHR-ESNQQFAVKivdVAKFTASPGLSTADLKREATICHMLK---HPHIVELLETYSSEGML 87
Cdd:cd14052    2 FANVELIGSGEFSQVYKVSERvPTGKVYAVK---KLKPNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLCF---EVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFG 164
Cdd:cd14052   79 YIQTELCENGSLDVflsELGLLGR----LDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGT---LKIGDFG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 SAIQLPGTReTIETHG-RVgcphYMAPEVVTRRLYGKGCDVWGAGVML----------------HVLLSGRLPFLG--SG 225
Cdd:cd14052  152 MATVWPLIR-GIEREGdRE----YIAPEILSEHMYDKPADIFSLGLILleaaanvvlpdngdawQKLRSGDLSDAPrlSS 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442620344 226 VRLQQSVARGRLSFEAPEWKSISANAKD-LVMKMLAANPHHRLSITEVLDHP 276
Cdd:cd14052  227 TDLHSASSPSSNPPPDPPNMPILSGSLDrVVRWMLSPEPDRRPTADDVLATP 278
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
12-277 2.74e-19

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 91.23  E-value: 2.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvaKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05623   74 FEILKVIGRGAFGEVAVVKLKNADKVFAMKILN--KWEMLKRAETACFREERDVLVNGDSQWITTLHYAFQDDNNLYLVM 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCfevvrRAVAGFV--YSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQL 169
Cdd:cd05623  152 DYYVGGDLL-----TLLSKFEdrLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILM---DMNGHIRLADFGSCLKL 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PgTRETIETHGRVGCPHYMAPEVVTRRLYGKG-----CDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAP- 242
Cdd:cd05623  224 M-EDGTVQSSVAVGTPDYISPEILQAMEDGKGkygpeCDWWSLGVCMYEMLYGETPFYAeSLVETYGKIMNHKERFQFPt 302
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 442620344 243 EWKSISANAKDLVMKMLAANpHHRL---SITEVLDHPW 277
Cdd:cd05623  303 QVTDVSENAKDLIRRLICSR-EHRLgqnGIEDFKNHPF 339
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
12-278 4.52e-19

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 88.16  E-value: 4.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREATICHMLKHPHIVELLETYS--SEGMLYM 89
Cdd:cd06653    4 WRLGKLLGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRdpEEKKLSI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSdlcfEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQL 169
Cdd:cd06653   84 FVEYMPGG----SVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILR---DSAGNVKLGDFGASKRI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 pgtrETIETHGR-----VGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF-----LGSGVRLQQSVARGRLsf 239
Cdd:cd06653  157 ----QTICMSGTgiksvTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWaeyeaMAAIFKIATQPTKPQL-- 230
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 442620344 240 eaPEwkSISANAKDLvMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06653  231 --PD--GVSDACRDF-LRQIFVEEKRRPTAEFLLRHPFV 264
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
10-279 4.72e-19

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 88.51  E-value: 4.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvakftaspGLSTADLKREA--TICHML-KHPHIVELLET-YSSE- 84
Cdd:cd06639   22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILD--------PISDVDEEIEAeyNILRSLpNHPNVVKFYGMfYKADq 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  85 ---GMLYMVFEFMEGSDLCFEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvdnSAPVKLG 161
Cdd:cd06639   94 yvgGQLWLVLELCNGGSVTELVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTT---EGGVKLV 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 162 GFGSAIQLPGTRetIETHGRVGCPHYMAPEVVT-----RRLYGKGCDVWGAGVMLHVLLSGRLP-FLGSGVRLQQSVARG 235
Cdd:cd06639  171 DFGVSAQLTSAR--LRRNTSVGTPFWMAPEVIAceqqyDYSYDARCDVWSLGITAIELADGDPPlFDMHPVKALFKIPRN 248
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 442620344 236 -RLSFEAPE-W-KSISANAKDLVMKMLAANPhhrlSITEVLDHPWIR 279
Cdd:cd06639  249 pPPTLLNPEkWcRGFSHFISQCLIKDFEKRP----SVTHLLEHPFIK 291
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
12-279 4.77e-19

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 87.98  E-value: 4.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCiHRESN-QQFAVKIVD---VAKFTASPGLSTADLKRE--ATICHMLKHPHIVELLETYSSEG 85
Cdd:cd14101    2 YTMGNLLGKGGFGTVYAG-HRISDgLQVAIKQISrnrVQQWSKLPGVNPVPNEVAllQSVGGGPGHRGVIRLLDWFEIPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 MLYMVFEFMEGSDLCFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvdNSAPVKLGGFGS 165
Cdd:cd14101   81 GFLLVLERPQHCQDLFDYITERGA---LDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDL--RTGDIKLIDFGS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 166 AIQLPGTRETIETHGRVgcphYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFlgsgvRLQQSVARGRLSFEAPew 244
Cdd:cd14101  156 GATLKDSMYTDFDGTRV----YSPPEWILYHQYhALPATVWSLGILLYDMVCGDIPF-----ERDTDILKAKPSFNKR-- 224
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442620344 245 ksISANAKDLVMKMLAANPHHRLSITEVLDHPWIR 279
Cdd:cd14101  225 --VSNDCRSLIRSCLAYNPSDRPSLEQILLHPWMM 257
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
12-221 5.60e-19

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 87.79  E-value: 5.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREATICHMLKHPHIVELLETY--SSEGMLYM 89
Cdd:cd06652    4 WRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESPETSKEVNALECEIQLLKNLLHERIVQYYGCLrdPQERTLSI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLCFEVvrRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQL 169
Cdd:cd06652   84 FMEYMPGGSIKDQL--KSYGAL--TENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILR---DSVGNVKLGDFGASKRL 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344 170 pgtrETIETHGR-----VGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF 221
Cdd:cd06652  157 ----QTICLSGTgmksvTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPW 209
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
17-274 6.28e-19

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 87.45  E-value: 6.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHResNQQFAVKI--VDVAKftaSPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFM 94
Cdd:cd14061    1 VIGVGGFGKVYRGIWR--GEEVAVKAarQDPDE---DISVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  95 EGSDLcfevvRRAVAGFVYSEAVACHYMRQILEALRYCHEND---ILHRDVRPACALLATVDNSAPV-----KLGGFGSA 166
Cdd:cd14061   76 RGGAL-----NRVLAGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAIENEDLenktlKITDFGLA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 iqlpgtRETIETHgRV---GCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAP 242
Cdd:cd14061  151 ------REWHKTT-RMsaaGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGiDGLAVAYGVAVNKLTLPIP 223
                        250       260       270
                 ....*....|....*....|....*....|..
gi 442620344 243 ewKSISANAKDLVMKMLAANPHHRLSITEVLD 274
Cdd:cd14061  224 --STCPEPFAQLMKDCWQPDPHDRPSFADILK 253
SH3_MPP6 cd12038
Src Homology 3 domain of Membrane Protein, Palmitoylated 6 (or MAGUK p55 subfamily member 6); ...
586-643 6.33e-19

Src Homology 3 domain of Membrane Protein, Palmitoylated 6 (or MAGUK p55 subfamily member 6); MPP6, also called Veli-associated MAGUK 1 (VAM-1) or PALS2, is a scaffolding protein that binds to Veli-1, a homolog of Caenorhabditis Lin-7. It is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212971  Cd Length: 61  Bit Score: 81.26  E-value: 6.33e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 586 FVRAQFDYNPLDDELIPCAQAGISFQVGDILQIISKDDHHWWQARLDTVGGSAGLIPS 643
Cdd:cd12038    1 FVKCHFDYNPYNDNLIPCKEAGLKFSKGEILQIVNREDPNWWQASHVKEGGSAGLIPS 58
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
10-280 6.69e-19

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 88.34  E-value: 6.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftASPGL-STAdlKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:PLN00009   2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQ--EDEGVpSTA--IREISLLKEMQHGNIVRLQDVVHSEKRLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMegsDLCFEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSapVKLGGFGSAIQ 168
Cdd:PLN00009  78 LVFEYL---DLDLKKHMDSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNA--LKLADFGLARA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LpGTRETIETHgRVGCPHYMAPEVVT-RRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG--------VRL----QQSVARG 235
Cdd:PLN00009 153 F-GIPVRTFTH-EVVTLWYRAPEILLgSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSeidelfkiFRIlgtpNEETWPG 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 236 RLSFEA-----PEWKS---------ISANAKDLVMKMLAANPHHRLSITEVLDHPWIRD 280
Cdd:PLN00009 231 VTSLPDyksafPKWPPkdlatvvptLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKD 289
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
16-277 8.15e-19

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 87.44  E-value: 8.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEG--MLYMVFEF 93
Cdd:cd06651   13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAekTLTIFMEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  94 MEGSdlcfEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLpgtr 173
Cdd:cd06651   93 MPGG----SVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILR---DSAGNVKLGDFGASKRL---- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 174 ETIETHGR-----VGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFlgSGVRLQQSVARGRLSFEAPEWKS-I 247
Cdd:cd06651  162 QTICMSGTgirsvTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW--AEYEAMAAIFKIATQPTNPQLPShI 239
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 248 SANAKDLVMKMLaANPHHRLSITEVLDHPW 277
Cdd:cd06651  240 SEHARDFLGCIF-VEARHRPSAEELLRHPF 268
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
18-276 9.66e-19

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 87.12  E-value: 9.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVdvaKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCL---HSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLcFEVVRRAVAGFVYSeaVACHYMRQILEALRYCHEND--ILHRDVRPACALLatvDNSAPVKLGGFGSA------IQL 169
Cdd:cd13978   78 SL-KSLLEREIQDVPWS--LRFRIIHEIALGMNFLHNMDppLLHHDLKPENILL---DNHFHVKISDFGLSklgmksISA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PGTRETIETHgrvGCPHYMAPEVV--TRRLYGKGCDVWGAGVMLHVLLSGRLPFLgsGVRLQQSVARGRLSFEAPEWKSI 247
Cdd:cd13978  152 NRRRGTENLG---GTPIYMAPEAFddFNKKPTSKSDVYSFAIVIWAVLTRKEPFE--NAINPLLIMQIVSKGDRPSLDDI 226
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 442620344 248 S--------ANAKDLVMKMLAANPHHRLSITEVLDHP 276
Cdd:cd13978  227 GrlkqienvQELISLMIRCWDGNPDARPTFLECLDRL 263
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
10-276 1.01e-18

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 86.89  E-value: 1.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIH-------RESNQQFAVKIVDVakfTASPglstadlKREATICHMLK----HPHIVELL 78
Cdd:cd14019    1 NKYRIIEKIGEGTFSSVYKAEDklhdlydRNKGRLVALKHIYP---TSSP-------SRILNELECLErlggSNNVSGLI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  79 ETYSSEGMLYMVFEFMEGSD-------LCFEVVRravagfvyseavacHYMRQILEALRYCHENDILHRDVRPACALL-- 149
Cdd:cd14019   71 TAFRNEDQVVAVLPYIEHDDfrdfyrkMSLTDIR--------------IYLRNLFKALKHVHSFGIIHRDVKPGNFLYnr 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 150 -----ATVDnsapvklggFGSAiQLPGTRETIETHgRVGCPHYMAPEVVTRrlygkgC-------DVWGAGVMLHVLLSG 217
Cdd:cd14019  137 etgkgVLVD---------FGLA-QREEDRPEQRAP-RAGTRGFRAPEVLFK------CphqttaiDIWSAGVILLSILSG 199
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620344 218 RLPFLGSGVRLQQSVargrlsfeapEWKSI--SANAKDLVMKMLAANPHHRLSITEVLDHP 276
Cdd:cd14019  200 RFPFFFSSDDIDALA----------EIATIfgSDEAYDLLDKLLELDPSKRITAEEALKHP 250
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
45-273 1.09e-18

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 90.46  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  45 VAKFTASPGLSTADLKREATIC-HMLKHPHIVELLETYSSEGMLYMVFEFMEGSDLCFEVVRRAVAGFVYSEAVACHYMR 123
Cdd:PTZ00267  97 VAKFVMLNDERQAAYARSELHClAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRLKEHLPFQEYEVGLLFY 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 124 QILEALRYCHENDILHRDVRPACALLATvdnSAPVKLGGFGSAIQLPGTRETIETHGRVGCPHYMAPEVVTRRLYGKGCD 203
Cdd:PTZ00267 177 QIVLALDEVHSRKMMHRDLKSANIFLMP---TGIIKLGDFGFSKQYSDSVSLDVASSFCGTPYYLAPELWERKRYSKKAD 253
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 204 VWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGRLS-FEAPewksISANAKDLVMKMLAANPHHRLSITEVL 273
Cdd:PTZ00267 254 MWSLGVILYELLTLHRPFKGPSQReIMQQVLYGKYDpFPCP----VSSGMKALLDPLLSKNPALRPTTQQLL 321
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
16-278 1.12e-18

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 87.05  E-value: 1.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTA----SPGLSTAD-LKREATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd06629    7 ELIGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSdradSRQKTVVDaLKSEIDTLKDLDHPNIVQYLGFEETEDYFSIF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLCfEVVRRaVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRpACALLatVDNSAPVKLGGFG---SAI 167
Cdd:cd06629   87 LEYVPGGSIG-SCLRK-YGKF--EEDLVRFFTRQILDGLAYLHSKGILHRDLK-ADNIL--VDLEGICKISDFGiskKSD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLPGTRETIETHGRVgcpHYMAPEVV--TRRLYGKGCDVWGAGVMLHVLLSGRLPFlgSGVRLQQS---VARGRLSFEAP 242
Cdd:cd06629  160 DIYGNNGATSMQGSV---FWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPW--SDDEAIAAmfkLGNKRSAPPVP 234
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 442620344 243 EWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06629  235 EDVNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
3-282 1.35e-18

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 88.11  E-value: 1.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   3 EDEILFDDvYELCEVIGKGPFSivRRCIHRESNQQFAVkiVDVAKFTASPGLSTADLKR---EATICHMLKHPHIVELLE 79
Cdd:PTZ00426  24 KNKMKYED-FNFIRTLGTGSFG--RVILATYKNEDFPP--VAIKRFEKSKIIKQKQVDHvfsERKILNYINHPFCVNLYG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  80 TYSSEGMLYMVFEFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVK 159
Cdd:PTZ00426  99 SFKDESYLYLVLEFVIGGEF-FTFLRRNKR---FPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLL---DKDGFIK 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 160 LGGFGSAiQLPGTRetieTHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGS-GVRLQQSVARGRLS 238
Cdd:PTZ00426 172 MTDFGFA-KVVDTR----TYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANePLLIYQKILEGIIY 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 442620344 239 FEapewKSISANAKDLVMKMLAANPHHRL-----SITEVLDHPWIRDRD 282
Cdd:PTZ00426 247 FP----KFLDNNCKHLMKKLLSHDLTKRYgnlkkGAQNVKEHPWFGNID 291
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
18-287 1.73e-18

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 87.96  E-value: 1.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIV------DVAKftaspglstaDLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:PLN00034  82 IGSGAGGTVYKVIHRPTGRLYALKVIygnhedTVRR----------QICREIEILRDVNHPNVVKCHDMFDHNGEIQVLL 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcfEVVRravagfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLPG 171
Cdd:PLN00034 152 EFMDGGSL--EGTH------IADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLL---INSAKNVKIADFGVSRILAQ 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIEThgRVGCPHYMAPEVVTRRL----Y-GKGCDVWGAGVMLHVLLSGRLPFlgsGVRLQQSVARGRLSF------E 240
Cdd:PLN00034 221 TMDPCNS--SVGTIAYMSPERINTDLnhgaYdGYAGDIWSLGVSILEFYLGRFPF---GVGRQGDWASLMCAIcmsqppE 295
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 442620344 241 APewKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDKLQRT 287
Cdd:PLN00034 296 AP--ATASREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQ 340
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
8-278 1.82e-18

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 87.81  E-value: 1.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKivDVAKFTASPGLSTADLkREATICHMLKHPHIVELLETYSSEGML 87
Cdd:cd07855    3 VGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIK--KIPNAFDVVTTAKRTL-RELKILRHFKHDNIIAIRDILRPKVPY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 ------YMVFEFMEgSDLcFEVVRravAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLG 161
Cdd:cd07855   80 adfkdvYVVLDLME-SDL-HHIIH---SDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLL---VNENCELKIG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 162 GFGSAIQL---PGTRETIETHgRVGCPHYMAPEVV-TRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-------------- 223
Cdd:cd07855  152 DFGMARGLctsPEEHKYFMTE-YVATRWYRAPELMlSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGknyvhqlqliltvl 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 224 ----SGVRLQQSVARGRLSFE------APEWKSI----SANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd07855  231 gtpsQAVINAIGADRVRRYIQnlpnkqPVPWETLypkaDQQALDLLSQMLRFDPSERITVAEALQHPFL 299
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
12-287 2.21e-18

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 88.37  E-value: 2.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLstADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05629    3 FHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQL--AHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAvagfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFG------- 164
Cdd:cd05629   81 EFLPGGDLMTMLIKYD----TFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILI---DRGGHIKLSDFGlstgfhk 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 ----------------------------SAIQLP-GTRETIET---------HGRVGCPHYMAPEVVTRRLYGKGCDVWG 206
Cdd:cd05629  154 qhdsayyqkllqgksnknridnrnsvavDSINLTmSSKDQIATwkknrrlmaYSTVGTPDYIAPEIFLQQGYGQECDWWS 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 207 AGVMLHVLLSGRLPFLGSGVR-LQQSVARGRLSFEAPEWKSISANAKDLVMKMLaANPHHRL---SITEVLDHPWIR--D 280
Cdd:cd05629  234 LGAIMFECLIGWPPFCSENSHeTYRKIINWRETLYFPDDIHLSVEAEDLIRRLI-TNAENRLgrgGAHEIKSHPFFRgvD 312

                 ....*..
gi 442620344 281 RDKLQRT 287
Cdd:cd05629  313 WDTIRQI 319
SH3_MPP4 cd12034
Src Homology 3 domain of Membrane Protein, Palmitoylated 4 (or MAGUK p55 subfamily member 4); ...
586-643 2.38e-18

Src Homology 3 domain of Membrane Protein, Palmitoylated 4 (or MAGUK p55 subfamily member 4); MPP4, also called Disks Large homolog 6 (DLG6) or Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 5 protein (ALS2CR5), is a retina-specific scaffolding protein that plays a role in organizing presynaptic protein complexes in the photoreceptor synapse, where it localizes to the plasma membrane. It is required in the proper localization of calcium ATPases and for maintenance of calcium homeostasis. MPP4 is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212967  Cd Length: 61  Bit Score: 79.55  E-value: 2.38e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 586 FVRAQFDYNPLDDELIPCAQAGISFQVGDILQIISKDDHHWWQAR-LDTVGGSAGLIPS 643
Cdd:cd12034    1 YVRAMVDYWPQQDPSIPCADAGLPFRKGDILQIVDQNDSLWWQARkLSDLAACAGLIPS 59
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
12-221 2.49e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 87.38  E-value: 2.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05602    9 FHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQ-KKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAiqlpg 171
Cdd:cd05602   88 DYINGGELFYHLQRERC----FLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILL---DSQGHIVLTDFGLC----- 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442620344 172 tRETIETHGRV----GCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF 221
Cdd:cd05602  156 -KENIEPNGTTstfcGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPF 208
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
12-276 2.71e-18

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 86.40  E-value: 2.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVK-IVDVAKFtaspglstadlK-REATICHMLKHPHIVELLETYSSEG---- 85
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKkVLQDKRY-----------KnRELQIMRRLKHPNIVKLKYFFYSSGekkd 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 --MLYMVFEFMEGSdlCFEVVRRavagfvYSEAV----ACH---YMRQILEALRYCHENDILHRDVRPAcALLatVD-NS 155
Cdd:cd14137   75 evYLNLVMEYMPET--LYRVIRH------YSKNKqtipIIYvklYSYQLFRGLAYLHSLGICHRDIKPQ-NLL--VDpET 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 156 APVKLGGFGSAIQL-PG--------TRetiethgrvgcpHYMAPEVV---TRrlYGKGCDVWGAG------VMLHVLLSG 217
Cdd:cd14137  144 GVLKLCDFGSAKRLvPGepnvsyicSR------------YYRAPELIfgaTD--YTTAIDIWSAGcvlaelLLGQPLFPG 209
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 218 R---------LPFLGSGVRLQ-QSVARGRLSFEAPEWKSIS----------ANAKDLVMKMLAANPHHRLSITEVLDHP 276
Cdd:cd14137  210 EssvdqlveiIKVLGTPTREQiKAMNPNYTEFKFPQIKPHPwekvfpkrtpPDAIDLLSKILVYNPSKRLTALEALAHP 288
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
67-277 3.16e-18

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 85.10  E-value: 3.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  67 HMLKHPHIVELLETYSSEGMLYMVFEfMEGSDLCFEVVRRAVAGfvysEAVACHYMRQILEALRYCHENDILHRDVRPAC 146
Cdd:cd14023   40 QLPSHRNITGIVEVILGDTKAYVFFE-KDFGDMHSYVRSCKRLR----EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRK 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 147 ALLATVDNSApVKLGGFGSAIQLPGTRETIEThgRVGCPHYMAPEVV--TRRLYGKGCDVWGAGVMLHVLLSGRLPFLGS 224
Cdd:cd14023  115 FVFSDEERTQ-LRLESLEDTHIMKGEDDALSD--KHGCPAYVSPEILntTGTYSGKSADVWSLGVMLYTLLVGRYPFHDS 191
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442620344 225 G-VRLQQSVARGRlsFEAPEwkSISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14023  192 DpSALFSKIRRGQ--FCIPD--HVSPKARCLIRSLLRREPSERLTAPEILLHPW 241
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
16-274 3.80e-18

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 86.56  E-value: 3.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIVDvAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFME 95
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQ-KKTILKKKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 GSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPGTRET 175
Cdd:cd05603   80 GGELFFHLQRERC----FLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILL---DCQGHVVLTDFGLCKEGMEPEET 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 176 IETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRLSFeaPEWKSISANakDL 254
Cdd:cd05603  153 TSTF--CGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVsQMYDNILHKPLHL--PGGKTVAAC--DL 226
                        250       260
                 ....*....|....*....|.
gi 442620344 255 VMKMLAANPHHRL-SITEVLD 274
Cdd:cd05603  227 LQGLLHKDQRRRLgAKADFLE 247
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
16-277 4.58e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 86.55  E-value: 4.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIVDvAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFME 95
Cdd:cd05604    2 KVIGKGSFGKVLLAKRKRDGKYYAVKVLQ-KKVILNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 GSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPGTRET 175
Cdd:cd05604   81 GGELFFHLQRERS----FPEPRARFYAAEIASALGYLHSINIVYRDLKPENILL---DSQGHIVLTDFGLCKEGISNSDT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 176 IETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRLSFEApewkSISANAKDL 254
Cdd:cd05604  154 TTTF--CGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTaEMYENILHKPLVLRP----GISLTAWSI 227
                        250       260
                 ....*....|....*....|....*..
gi 442620344 255 VMKMLAANPHHRLSIT----EVLDHPW 277
Cdd:cd05604  228 LEELLEKDRQLRLGAKedflEIKNHPF 254
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
61-278 5.47e-18

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 85.35  E-value: 5.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  61 REATICHMLKHPHIVELLETYSSEGM--LYMVFEFMEgSDL--CFEVVRRAvagFVYSEaVAChYMRQILEALRYCHEND 136
Cdd:cd07843   53 REINILLKLQHPNIVTVKEVVVGSNLdkIYMVMEYVE-HDLksLMETMKQP---FLQSE-VKC-LMLQLLSGVAHLHDNW 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 137 ILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPGTRETIeTHGRVGCpHYMAPEVV-TRRLYGKGCDVWGAG------V 209
Cdd:cd07843  127 ILHRDLKTSNLLL---NNRGILKICDFGLAREYGSPLKPY-TQLVVTL-WYRAPELLlGAKEYSTAIDMWSVGcifaelL 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 210 MLHVLLSGR--------------------------LPFLGSGVRLQQSVARGRLSFEAPewkSISANAKDLVMKMLAANP 263
Cdd:cd07843  202 TKKPLFPGKseidqlnkifkllgtptekiwpgfseLPGAKKKTFTKYPYNQLRKKFPAL---SLSDNGFDLLNRLLTYDP 278
                        250
                 ....*....|....*
gi 442620344 264 HHRLSITEVLDHPWI 278
Cdd:cd07843  279 AKRISAEDALKHPYF 293
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
10-277 5.48e-18

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 86.25  E-value: 5.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIvdvakftaspgLSTAD-LKREATICH-----MLKH---PHIVELLET 80
Cdd:cd05597    1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKI-----------LNKWEmLKRAETACFreerdVLVNgdrRWITKLHYA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  81 YSSEGMLYMVFEFMEGSDLC-----FEVVrravagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNS 155
Cdd:cd05597   70 FQDENYLYLVMDYYCGGDLLtllskFEDR--------LPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLL---DRN 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 156 APVKLGGFGSAIQLpGTRETIETHGRVGCPHYMAPEVVT-----RRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGvrLQQ 230
Cdd:cd05597  139 GHIRLADFGSCLKL-REDGTVQSSVAVGTPDYISPEILQamedgKGRYGPECDWWSLGVCMYEMLYGETPFYAES--LVE 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442620344 231 SVAR-----GRLSFEAPEwKSISANAKDLvMKMLAANPHHRL---SITEVLDHPW 277
Cdd:cd05597  216 TYGKimnhkEHFSFPDDE-DDVSEEAKDL-IRRLICSRERRLgqnGIDDFKKHPF 268
PLN02772 PLN02772
guanylate kinase
697-879 5.93e-18

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 87.20  E-value: 5.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 697 EEVVKVPVGDPNFQRKTLVLLGAHGVGrrhiKNTLISK----YPDKYAYPIPHTTRPAKPEEENGRSYYFVSHDEMMADI 772
Cdd:PLN02772 121 TEVVAWSKGVRGNAEKPIVISGPSGVG----KGTLISMlmkeFPSMFGFSVSHTTRAPREMEKDGVHYHFTERSVMEKEI 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 773 GANEYLEYGTHEDAMYGTKLDTIRRIHTEGKMAILDVEPQALKILRTAEFTPYVVFIAAPSLQNIADY---------DGS 843
Cdd:PLN02772 197 KDGKFLEFASVHGNLYGTSIEAVEVVTDSGKRCILDIDVQGARSVRASSLEAIFIFICPPSMEELEKRlrargteteEQI 276
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 442620344 844 LERLAK-ESEMLRQLYGHFFDLTIVNNDISETIATLE 879
Cdd:PLN02772 277 QKRLRNaEAELEQGKSSGIFDHILYNDNLEECYKNLK 313
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
11-278 6.49e-18

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 84.64  E-value: 6.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  11 VYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTAdlKREATICHMLKH-----PHIVELLETYSSEG 85
Cdd:cd14100    1 QYQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEWGELPNG--TRVPMEIVLLKKvgsgfRGVIRLLDWFERPD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 MLYMVFEFMEGSDLCFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvdNSAPVKLGGFGS 165
Cdd:cd14100   79 SFVLVLERPEPVQDLFDFITERGA---LPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDL--NTGELKLIDFGS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 166 AIQLPGTRETIETHGRVgcphYMAPEVVT-RRLYGKGCDVWGAGVMLHVLLSGRLPFlgsgvRLQQSVARGRLSFEapew 244
Cdd:cd14100  154 GALLKDTVYTDFDGTRV----YSPPEWIRfHRYHGRSAAVWSLGILLYDMVCGDIPF-----EHDEEIIRGQVFFR---- 220
                        250       260       270
                 ....*....|....*....|....*....|....
gi 442620344 245 KSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14100  221 QRVSSECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
12-282 7.38e-18

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 85.82  E-value: 7.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGL-STADLKREATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd05589    1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVeSLMCEKRIFETVNSARHPFLVNLFACFQTPEHVCFV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLCFEVVRRavagfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGsaiqL- 169
Cdd:cd05589   81 MEYAAGGDLMMHIHED-----VFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLL---DTEGYVKIADFG----Lc 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 -----PGTRetieTHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGvrlQQSVARGRLSFEAPEW 244
Cdd:cd05589  149 kegmgFGDR----TSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDD---EEEVFDSIVNDEVRYP 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442620344 245 KSISANAKDLVMKMLAANPHHRLSITE-----VLDHPWIRDRD 282
Cdd:cd05589  222 RFLSTEAISIMRRLLRKNPERRLGASErdaedVKKQPFFRNID 264
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
17-274 7.90e-18

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 84.69  E-value: 7.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKivdVAKFTASPGLSTAdlKREATICHML-KHPHIVELL--ETYSSEGML--YMVF 91
Cdd:cd13985    7 QLGEGGFSYVYLAHDVNTGRRYALK---RMYFNDEEQLRVA--IKEIEIMKRLcGHPNIVQYYdsAILSSEGRKevLLLM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSdlCFEVVRRAVAGFvYSEAVACHYMRQILEALRYCHEND--ILHRDVRPACALLAtvdNSAPVKLGGFGSA--I 167
Cdd:cd13985   82 EYCPGS--LVDILEKSPPSP-LSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFS---NTGRFKLCDFGSAttE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLPGTRET-----IETHGRVGCPHYMAPEVVTrrLYGK---GC--DVWGAGVMLHVLLSGRLPFLGSGVrlqqsVARGRL 237
Cdd:cd13985  156 HYPLERAEevniiEEEIQKNTTPMYRAPEMID--LYSKkpiGEkaDIWALGCLLYKLCFFKLPFDESSK-----LAIVAG 228
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 442620344 238 SFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLD 274
Cdd:cd13985  229 KYSIPEQPRYSPELHDLIRHMLTPDPAERPDIFQVIN 265
SH3_MPP3 cd12039
Src Homology 3 domain of Membrane Protein, Palmitoylated 3 (or MAGUK p55 subfamily member 3); ...
586-643 9.26e-18

Src Homology 3 domain of Membrane Protein, Palmitoylated 3 (or MAGUK p55 subfamily member 3); MPP3 is a scaffolding protein that colocalizes with MPP5 and CRB1 at the subdpical region adjacent to adherens junctions and may function in photoreceptor polarity. It interacts with some nectins and regulates their trafficking and processing. Nectins are cell-cell adhesion proteins involved in the establishment apical-basal polarity at cell adhesion sites. It is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212972  Cd Length: 62  Bit Score: 78.08  E-value: 9.26e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 586 FVRAQFDYNPLDDELIPCAQAGISFQVGDILQIISKDDHHWWQA-RLDTVGGSAGLIPS 643
Cdd:cd12039    1 FMRALFDYNPYEDRAIPCQEAGLPFKRRDILEVVSQDDPTWWQAkRVGDTNLRAGLIPS 59
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-221 1.32e-17

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 84.09  E-value: 1.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRcIHRESNQQ--FAVKIVdvakFTASPGLSTADLKREATICHM----------LKHPHIVELLE 79
Cdd:cd08528    2 YAVLELLGSGAFGCVYK-VRKKSNGQtlLALKEI----NMTNPAFGRTEQERDKSVGDIisevniikeqLRHPNIVRYYK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  80 TYSSEGMLYMVFEFMEGSDLCFEVVRRAVAGFVYSEAVACHYMRQILEALRYCH-ENDILHRDVRPACALLATVDNsapV 158
Cdd:cd08528   77 TFLENDRLYIVMELIEGAPLGEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDK---V 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620344 159 KLGGFGSAIQlpGTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF 221
Cdd:cd08528  154 TITDFGLAKQ--KGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPF 214
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
10-278 1.45e-17

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 83.35  E-value: 1.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHR--ESNQQFAVKIVDvakftasPGLSTADLKREATICHMLKHPHIVELLETYSSEGML 87
Cdd:cd14112    3 GRFSFGSEIFRGRFSVIVKAVDSttETDAHCAVKIFE-------VSDEASEAVREFESLRTLQHENVQRLIAAFKPSNFA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGsdlcfEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVdNSAPVKLGGFGSAi 167
Cdd:cd14112   76 YLVMEKLQE-----DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSV-RSWQVKLVDFGRA- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 qlpgtrETIETHGRVGCP---HYMAPEVV-TRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR---LQQSVARGRLSFE 240
Cdd:cd14112  149 ------QKVSKLGKVPVDgdtDWASPEFHnPETPITVQSDIWGLGVLTFCLLSGFHPFTSEYDDeeeTKENVIFVKCRPN 222
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 442620344 241 APeWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14112  223 LI-FVEATQEALRFATWALKKSPTRRMRTDEALEHRWL 259
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
16-282 1.54e-17

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 84.85  E-value: 1.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIvdvakftaspglstadLKREATI------CHML---------KHPHIVELLET 80
Cdd:cd05591    1 KVLGKGSFGKVMLAERKGTDEVYAIKV----------------LKKDVILqdddvdCTMTekrilalaaKHPFLTALHSC 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  81 YSSEGMLYMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKL 160
Cdd:cd05591   65 FQTKDRLFFVMEYVNGGDLMFQIQRARK----FDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILL---DAEGHCKL 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 161 GGFGSAIQlpGTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR-LQQSVARGRLSF 239
Cdd:cd05591  138 ADFGMCKE--GILNGKTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDdLFESILHDDVLY 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 442620344 240 eaPEWksISANAKDLVMKMLAANPHHRLSITE-------VLDHPWIRDRD 282
Cdd:cd05591  216 --PVW--LSKEAVSILKAFMTKNPAKRLGCVAsqggedaIRQHPFFREID 261
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
7-261 1.78e-17

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 85.83  E-value: 1.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   7 LFDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvaKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGM 86
Cdd:cd05624   69 LHRDDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILN--KWEMLKRAETACFREERNVLVNGDCQWITTLHYAFQDENY 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEGSDLCfevvrRAVAGF--VYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFG 164
Cdd:cd05624  147 LYLVMDYYVGGDLL-----TLLSKFedKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLL---DMNGHIRLADFG 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 SAIQLpGTRETIETHGRVGCPHYMAPEVVTRR-----LYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLS 238
Cdd:cd05624  219 SCLKM-NDDGTVQSSVAVGTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFYAeSLVETYGKIMNHEER 297
                        250       260
                 ....*....|....*....|....
gi 442620344 239 FEAPEW-KSISANAKDLVMKMLAA 261
Cdd:cd05624  298 FQFPSHvTDVSEEAKDLIQRLICS 321
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
12-277 1.86e-17

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 83.64  E-value: 1.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftASPGLSTADLkREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd07839    2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDD--DDEGVPSSAL-REICLLKELKHKNIVRLYDVLHSDKKLTLVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEgSDL--CFEVVRRAVagfvySEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFG--SAI 167
Cdd:cd07839   79 EYCD-QDLkkYFDSCNGDI-----DPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLL---INKNGELKLADFGlaRAF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLPGTRETIEthgrVGCPHYMAPEVVT-RRLYGKGCDVWGAGVMLHVLLSGRLP-FLGSGVRLQ---------------- 229
Cdd:cd07839  150 GIPVRCYSAE----VVTLWYRPPDVLFgAKLYSTSIDMWSAGCIFAELANAGRPlFPGNDVDDQlkrifrllgtpteesw 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 230 QSVAR----------GRLSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07839  226 PGVSKlpdykpypmyPATTSLVNVVPKLNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
16-279 1.91e-17

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 84.23  E-value: 1.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIV--DVAKFTASPGLSTADlKREATIChmLKHPHIVELLETYSSEGMLYMVFEF 93
Cdd:cd05620    1 KVLGKGSFGKVLLAELKGKGEYFAVKALkkDVVLIDDDVECTMVE-KRVLALA--WENPFLTHLYCTFQTKEHLFFVMEF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  94 MEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAiqlpgtR 173
Cdd:cd05620   78 LNGGDLMFHIQDKGR----FDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVML---DRDGHIKIADFGMC------K 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 174 ETIETHGRV----GCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGV-RLQQSVARGRLSFeaPEWksIS 248
Cdd:cd05620  145 ENVFGDNRAstfcGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEdELFESIRVDTPHY--PRW--IT 220
                        250       260       270
                 ....*....|....*....|....*....|..
gi 442620344 249 ANAKDLVMKMLAANPHHRLSIT-EVLDHPWIR 279
Cdd:cd05620  221 KESKDILEKLFERDPTRRLGVVgNIRGHPFFK 252
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
11-276 1.94e-17

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 82.74  E-value: 1.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  11 VYELCEVIGKGPFSIVRRCIHRESNQQFAVKIvdvakfTASPGLSTADLKR--EATICHML--KHPHIVELLETYSSEGM 86
Cdd:cd14050    2 CFTILSKLGEGSFGEVFKVRSREDGKLYAVKR------SRSRFRGEKDRKRklEEVERHEKlgEHPNCVRFIKAWEEKGI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEfmegsdLCFEVVRRAVAGFVY-SEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVKLGGFGS 165
Cdd:cd14050   76 LYIQTE------LCDTSLQQYCEETHSlPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLS---KDGVCKLGDFGL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 166 AIQLPgtRETIeTHGRVGCPHYMAPEVVtRRLYGKGCDVWGAGV-MLHVLLSGRLPflgSGVRLQQSVARGRLsfeaPE- 243
Cdd:cd14050  147 VVELD--KEDI-HDAQEGDPRYMAPELL-QGSFTKAADIFSLGItILELACNLELP---SGGDGWHQLRQGYL----PEe 215
                        250       260       270
                 ....*....|....*....|....*....|....
gi 442620344 244 -WKSISANAKDLVMKMLAANPHHRLSITEVLDHP 276
Cdd:cd14050  216 fTAGLSPELRSIIKLMMDPDPERRPTAEDLLALP 249
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
12-277 2.13e-17

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 83.52  E-value: 2.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftaspglSTADLK---------REATICHMLKHPHIVELLETYS 82
Cdd:cd13990    2 YLLLNLLGKGGFSEVYKAFDLVEQRYVACKIHQLNK-------DWSEEKkqnyikhalREYEIHKSLDHPRIVKLYDVFE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  83 -SEGMLYMVFEFMEGSDLCFEVVRRAvagfVYSEAVACHYMRQILEALRYC--HENDILHRDVRPACALLATVDNSAPVK 159
Cdd:cd13990   75 iDTDSFCTVLEYCDGNDLDFYLKQHK----SIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNVSGEIK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 160 LGGFGSAIQLP---GTRETIE-THGRVGCPHYMAPEVVTRrlyGKG-------CDVWGAGVMLHVLLSGRLPFlgsGVRL 228
Cdd:cd13990  151 ITDFGLSKIMDdesYNSDGMElTSQGAGTYWYLPPECFVV---GKTppkisskVDVWSVGVIFYQMLYGRKPF---GHNQ 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442620344 229 -QQSVARGRLSFEA-----PEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd13990  225 sQEAILEENTILKAtevefPSKPVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
12-282 2.20e-17

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 85.08  E-value: 2.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREaTICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05618   22 FDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKH-VFEQASNHPFLVGLHSCFQTESRLFFVI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQlpG 171
Cdd:cd05618  101 EYVNGGDLMFHMQRQRK----LPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLL---DSEGHIKLTDYGMCKE--G 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF--LGSGVRLQQSVA----RGRLSFEAPEWK 245
Cdd:cd05618  172 LRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdiVGSSDNPDQNTEdylfQVILEKQIRIPR 251
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442620344 246 SISANAKDLVMKMLAANPHHRL------SITEVLDHPWIRDRD 282
Cdd:cd05618  252 SLSVKAASVLKSFLNKDPKERLgchpqtGFADIQGHPFFRNVD 294
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
11-298 2.34e-17

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 83.61  E-value: 2.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  11 VYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAkftaspGLSTADLKREatICHMLKHPHIVELLETYSS------- 83
Cdd:cd06637    7 IFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVT------GDEEEEIKQE--INMLKKYSHHRNIATYYGAfikknpp 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 --EGMLYMVFEFMeGSDLCFEVVRRAVAGFVYSEAVAcHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVKLG 161
Cdd:cd06637   79 gmDDQLWLVMEFC-GAGSVTDLIKNTKGNTLKEEWIA-YICREILRGLSHLHQHKVIHRDIKGQNVLLT---ENAEVKLV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 162 GFGSAIQLP---GTRETIethgrVGCPHYMAPEVVT-----RRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSV 232
Cdd:cd06637  154 DFGVSAQLDrtvGRRNTF-----IGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPLCDmHPMRALFLI 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 233 ARGrlsfEAPEWKS--ISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDR--DKLQRTHLADTVEELKR 298
Cdd:cd06637  229 PRN----PAPRLKSkkWSKKFQSFIESCLVKNHSQRPSTEQLMKHPFIRDQpnERQVRIQLKDHIDRTKK 294
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
10-282 2.38e-17

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 84.72  E-value: 2.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPglSTADLKREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd05627    2 DDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKE--QVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLCFEVVRRAvagfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFG----- 164
Cdd:cd05627   80 IMEFLPGGDMMTLLMKKD----TLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLL---DAKGHVKLSDFGlctgl 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 -------------------SAIQLPGTRETIET---------HGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLS 216
Cdd:cd05627  153 kkahrtefyrnlthnppsdFSFQNMNSKRKAETwkknrrqlaYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLI 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 217 GRLPFLG-SGVRLQQSVARGRLSFEAPEWKSISANAKDLVMKML--AANPHHRLSITEVLDHPWIRDRD 282
Cdd:cd05627  233 GYPPFCSeTPQETYRKVMNWKETLVFPPEVPISEKAKDLILRFCtdAENRIGSNGVEEIKSHPFFEGVD 301
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
57-282 3.27e-17

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 84.71  E-value: 3.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  57 ADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHEND 136
Cdd:cd05625   46 AHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGV----FPEDLARFYIAELTCAVESVHKMG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 137 ILHRDVRPACALlatVDNSAPVKLGGFGSAIQL---------------------------------------PGTRETIE 177
Cdd:cd05625  122 FIHRDIKPDNIL---IDRDGHIKLTDFGLCTGFrwthdskyyqsgdhlrqdsmdfsnewgdpencrcgdrlkPLERRAAR 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 178 THGR------VGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEWKSISAN 250
Cdd:cd05625  199 QHQRclahslVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAqTPLETQMKVINWQTSLHIPPQAKLSPE 278
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442620344 251 AKDLVMKmLAANPHHRL---SITEVLDHPWIRDRD 282
Cdd:cd05625  279 ASDLIIK-LCRGPEDRLgknGADEIKAHPFFKTID 312
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
5-306 4.15e-17

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 83.16  E-value: 4.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   5 EILFDDVYElcevIGKGPFSIVRRCIHRESNQQFAVKivdvaKFTASPGLST---ADLKREATICHMLKHPHIVELLETY 81
Cdd:cd06633   20 EEIFVDLHE----IGHGSFGAVYFATNSHTNEVVAIK-----KMSYSGKQTNekwQDIIKEVKFLQQLKHPNTIEYKGCY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  82 SSEGMLYMVFEFMEGS--DLcFEVVRRAVagfvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVK 159
Cdd:cd06633   91 LKDHTAWLVMEYCLGSasDL-LEVHKKPL-----QEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLT---EPGQVK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 160 LGGFGSA-IQLPGtretietHGRVGCPHYMAPEVV---TRRLYGKGCDVWGAGVMLhVLLSGRLPFL---GSGVRLQQSV 232
Cdd:cd06633  162 LADFGSAsIASPA-------NSFVGTPYWMAPEVIlamDEGQYDGKVDIWSLGITC-IELAERKPPLfnmNAMSALYHIA 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 233 ARGRLSFEAPEWksiSANAKDLVMKMLAANPHHRLSITEVLDHPWI-RDR------DKLQRTHlaDTVEELKRYNARRKL 305
Cdd:cd06633  234 QNDSPTLQSNEW---TDSFRGFVDYCLQKIPQERPSSAELLRHDFVrRERpprvliDLIQRTK--DAVRELDNLQYRKMK 308

                 .
gi 442620344 306 K 306
Cdd:cd06633  309 K 309
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
12-277 4.26e-17

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 83.49  E-value: 4.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRES--NQQFAVKivdvaKFTASP----GLSTADLkREATICHMLKHPHIVELLETY--SS 83
Cdd:cd07842    2 YEIEGCIGRGTYGRVYKAKRKNGkdGKEYAIK-----KFKGDKeqytGISQSAC-REIALLRELKHENVVSLVEVFleHA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGMLYMVFEFMEgSDLcFEVV---RRAVAGFVYSEAVAcHYMRQILEALRYCHENDILHRDVRPACALL-ATVDNSAPVK 159
Cdd:cd07842   76 DKSVYLLFDYAE-HDL-WQIIkfhRQAKRVSIPPSMVK-SLLWQILNGIHYLHSNWVLHRDLKPANILVmGEGPERGVVK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 160 LGGFG------SAIQLPGTRE----TIethgrvgcpHYMAPEVVT-RRLYGKGCDVWGAGVMLHVLLSGRLPFLG----- 223
Cdd:cd07842  153 IGDLGlarlfnAPLKPLADLDpvvvTI---------WYRAPELLLgARHYTKAIDIWAIGCIFAELLTLEPIFKGreaki 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 224 --------------------------SGV-------RLQQSVARGRL--SFEAP---EWKSISANAKDLVMKMLAANPHH 265
Cdd:cd07842  224 kksnpfqrdqlerifevlgtptekdwPDIkkmpeydTLKSDTKASTYpnSLLAKwmhKHKKPDSQGFDLLRKLLEYDPTK 303
                        330
                 ....*....|..
gi 442620344 266 RLSITEVLDHPW 277
Cdd:cd07842  304 RITAEEALEHPY 315
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
18-220 4.36e-17

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 82.15  E-value: 4.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglstadLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRS-------FLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLcFEVVRRAVAGFVYSEAVacHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSAIQLPGTRETIE 177
Cdd:cd14065   74 TL-EELLKSMDEQLPWSQRV--SLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVVADFGLAREMPDEKTKKP 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 442620344 178 THGR----VGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLsGRLP 220
Cdd:cd14065  151 DRKKrltvVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEII-GRVP 196
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
18-274 5.06e-17

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 82.77  E-value: 5.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVakFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd08229   32 IGRGQFSEVYRATCLLDGVPVALKKVQI--FDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLC-----FEVVRRAVAgfvysEAVACHYMRQILEALRYCHENDILHRDVRPACALLATvdnSAPVKLGGFGSAIQLpgT 172
Cdd:cd08229  110 DLSrmikhFKKQKRLIP-----EKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITA---TGVVKLGDLGLGRFF--S 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 173 RETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLqQSVARGRLSFEAPEWKS--ISAN 250
Cdd:cd08229  180 SKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNL-YSLCKKIEQCDYPPLPSdhYSEE 258
                        250       260
                 ....*....|....*....|....
gi 442620344 251 AKDLVMKMLAANPHHRLSITEVLD 274
Cdd:cd08229  259 LRQLVNMCINPDPEKRPDITYVYD 282
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
12-278 6.24e-17

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 82.32  E-value: 6.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTAdlkREATICHMLK---HPHIVELLETYSS----- 83
Cdd:cd07863    2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGLPLSTV---REVALLKRLEafdHPNIVRLMDVCATsrtdr 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGMLYMVFEFMEgSDLcFEVVRRAVAGFVYSEAVAcHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGF 163
Cdd:cd07863   79 ETKVTLVFEHVD-QDL-RTYLDKVPPPGLPAETIK-DLMRQFLRGLDFLHANCIVHRDLKPENIL---VTSGGQVKLADF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 164 GSA----IQLPGTRETIEThgrvgcpHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQ--------- 230
Cdd:cd07863  153 GLAriysCQMALTPVVVTL-------WYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLgkifdligl 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620344 231 ----------SVARGRLSFEAPE-----WKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd07863  226 ppeddwprdvTLPRGAFSPRGPRpvqsvVPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
12-289 6.75e-17

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 83.53  E-value: 6.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTaspglSTADLKREATICHMLK----HPHIVELLETYSSEGML 87
Cdd:cd05617   17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVH-----DDEDIDWVQTEKHVFEqassNPFLVGLHSCFQTTSRL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAI 167
Cdd:cd05617   92 FLVIEYVNGGDLMFHMQRQRK----LPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLL---DADGHIKLTDYGMCK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLPGTRETIETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF--LGSGVRLQQSVARGRLSFEAPEW- 244
Cdd:cd05617  165 EGLGPGDTTSTF--CGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiITDNPDMNTEDYLFQVILEKPIRi 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442620344 245 -KSISANAKDLVMKMLAANPHHRL------SITEVLDHPWIR--DRDKLQRTHL 289
Cdd:cd05617  243 pRFLSVKASHVLKGFLNKDPKERLgcqpqtGFSDIKSHTFFRsiDWDLLEKKQV 296
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
16-277 7.93e-17

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 81.93  E-value: 7.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTadlkREATICHMLKHPHIVELLETYSSEGMLYMVFEFME 95
Cdd:cd07870    6 EKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTAI----REASLLKGLKHANIVLLHDIIHTKETLTFVFEYMH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 gSDLCFEVVRRAvaGFVYSEAVAChYMRQILEALRYCHENDILHRDVRPACALLATVdnsAPVKLGGFG--SAIQLPGTR 173
Cdd:cd07870   82 -TDLAQYMIQHP--GGLHPYNVRL-FMFQLLRGLAYIHGQHILHRDLKPQNLLISYL---GELKLADFGlaRAKSIPSQT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 174 ETIEthgrVGCPHYMAPEVVTRRL-YGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSV---------------ARGRL 237
Cdd:cd07870  155 YSSE----VVTLWYRPPDVLLGATdYSSALDIWGAGCIFIEMLQGQPAFPGVSDVFEQLEkiwtvlgvptedtwpGVSKL 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442620344 238 SFEAPEWKSISA---------------NAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07870  231 PNYKPEWFLPCKpqqlrvvwkrlsrppKAEDLASQMLMMFPKDRISAQDALLHPY 285
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
14-273 8.69e-17

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 81.61  E-value: 8.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  14 LCEVIGKGPFSIVRRCIHResNQQFAVKivdVAKFTASPGLSTA--DLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14147    7 LEEVIGIGGFGKVYRGSWR--GELVAVK---AARQDPDEDISVTaeSVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcfevvRRAVAGFVYSEAVACHYMRQILEALRYCHENDI---LHRDVRPACALLA-TVDNSA----PVKLGGF 163
Cdd:cd14147   82 EYAAGGPL-----SRALAGRRVPPHVLVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLLqPIENDDmehkTLKITDF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 164 GSAIQLPGTRETiethGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAP 242
Cdd:cd14147  157 GLAREWHKTTQM----SAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGiDCLAVAYGVAVNKLTLPIP 232
                        250       260       270
                 ....*....|....*....|....*....|.
gi 442620344 243 EwkSISANAKDLVMKMLAANPHHRLSITEVL 273
Cdd:cd14147  233 S--TCPEPFAQLMADCWAQDPHRRPDFASIL 261
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
12-305 9.32e-17

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 82.52  E-value: 9.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAV-KIVDVAKFTAspglSTADLKREATICHMLKHPHIVELLETyssegML--- 87
Cdd:cd07859    2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIkKINDVFEHVS----DATRILREIKLLRLLRHPDIVEIKHI-----MLpps 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 -------YMVFEFMEgSDLcFEVVRravagfVYSEAVACHY---MRQILEALRYCHENDILHRDVRPAcALLATVDnsAP 157
Cdd:cd07859   73 rrefkdiYVVFELME-SDL-HQVIK------ANDDLTPEHHqffLYQLLRALKYIHTANVFHRDLKPK-NILANAD--CK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 158 VKLGGFGSA-IQLPGTRETIETHGRVGCPHYMAPEVVTRRL--YGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVAR 234
Cdd:cd07859  142 LKICDFGLArVAFNDTPTAIFWTDYVATRWYRAPELCGSFFskYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLIT 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 235 GRLSFEAPEWKSISANAK----------------------------DLVMKMLAANPHHRLSITEVLDHPWIRDRDKLQR 286
Cdd:cd07859  222 DLLGTPSPETISRVRNEKarrylssmrkkqpvpfsqkfpnadplalRLLERLLAFDPKDRPTAEEALADPYFKGLAKVER 301
                        330
                 ....*....|....*....
gi 442620344 287 THLADTVEELKRYNARRKL 305
Cdd:cd07859  302 EPSAQPITKLEFEFERRRL 320
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
12-278 1.43e-16

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 80.86  E-value: 1.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVakftaSPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd06645   13 FELIQRIGSGTYGDVYKARNVNTGELAAIKVIKL-----EPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcfEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVKLGGFGSAIQLPG 171
Cdd:cd06645   88 EFCGGGSL--QDIYHVTGPL--SESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLT---DNGHVKLADFGVSAQITA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHgrVGCPHYMAPEV--VTRR-LYGKGCDVWGAGVMLhVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWK--- 245
Cdd:cd06645  161 TIAKRKSF--IGTPYWMAPEVaaVERKgGYNQLCDIWAVGITA-IELAELQPPMFDLHPMRALFLMTKSNFQPPKLKdkm 237
                        250       260       270
                 ....*....|....*....|....*....|...
gi 442620344 246 SISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06645  238 KWSNSFHHFVKMALTKNPKKRPTAEKLLQHPFV 270
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
48-276 1.67e-16

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 80.10  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  48 FTASPGLSTADLKREA--------TICHmLKHPHIVELLE------TYSSEGMLYMVFEFMEGSDLcFEVVRRAvaGFVY 113
Cdd:cd14012   27 LTSQEYFKTSNGKKQIqllekeleSLKK-LRHPNLVSYLAfsierrGRSDGWKVYLLTEYAPGGSL-SELLDSV--GSVP 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 114 SEAVaCHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGF--GSAIQLPGTRETIETHGRvgcPHYMAPE 191
Cdd:cd14012  103 LDTA-RRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTGIVKLTDYslGKTLLDMCSRGSLDEFKQ---TYWLPPE 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 192 VVTRRL-YGKGCDVWGAGVMLHVLLSGRLPFLgsgvrlqqsvaRGRLSFEAPEWKSISANAKDLVMKMLAANPHHRLSIT 270
Cdd:cd14012  179 LAQGSKsPTRKTDVWDLGLLFLQMLFGLDVLE-----------KYTSPNPVLVSLDLSASLQDFLSKCLSLDPKKRPTAL 247

                 ....*.
gi 442620344 271 EVLDHP 276
Cdd:cd14012  248 ELLPHE 253
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
9-280 1.72e-16

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 80.87  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   9 DDVYELCEvIGKGPFSIVRRCIHRESNQQFAVK----IVDvakftaspGLSTADLKREA-TICHMLKHPHIVELLETYSS 83
Cdd:cd06616    6 EDLKDLGE-IGRGAFGTVNKMLHKPSGTIMAVKrirsTVD--------EKEQKRLLMDLdVVMRSSDCPYIVKFYGALFR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGMLYMVFEFMEGS-DLCFEVVRRAVAGfVYSEAVACHYMRQILEALRYCHEN-DILHRDVRPACALLatvDNSAPVKLG 161
Cdd:cd06616   77 EGDCWICMELMDISlDKFYKYVYEVLDS-VIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILL---DRNGNIKLC 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 162 GFGSAIQLpgtRETIETHGRVGCPHYMAPEVVT----RRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG---VRLQQSVar 234
Cdd:cd06616  153 DFGISGQL---VDSIAKTRDAGCRPYMAPERIDpsasRDGYDVRSDVWSLGITLYEVATGKFPYPKWNsvfDQLTQVV-- 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 442620344 235 grlSFEAP-----EWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRD 280
Cdd:cd06616  228 ---KGDPPilsnsEEREFSPSFVNFVNLCLIKDESKRPKYKELLKHPFIKM 275
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
17-221 1.75e-16

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 80.42  E-value: 1.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHResNQQFAVKIV--DVAKftaSPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFM 94
Cdd:cd14148    1 IIGVGGFGKVYKGLWR--GEEVAVKAArqDPDE---DIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  95 EGSDLcfevvRRAVAGFVYSEAVACHYMRQILEALRYCHeND----ILHRDVRPACAL-LATVDN----SAPVKLGGFGS 165
Cdd:cd14148   76 RGGAL-----NRALAGKKVPPHVLVNWAVQIARGMNYLH-NEaivpIIHRDLKSSNILiLEPIENddlsGKTLKITDFGL 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442620344 166 AIQLPGTRETiethGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF 221
Cdd:cd14148  150 AREWHKTTKM----SAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
16-282 1.90e-16

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 80.69  E-value: 1.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIVdvakftasPGLSTADLKR----EATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd06619    7 EILGHGNGGTVYKAYHLLTRRILAVKVI--------PLDITVELQKqimsELEILYKCDSPYIIGFYGAFFVENRISICT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcfEVVRRAVAGFVYSEAVAchymrqILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLPG 171
Cdd:cd06619   79 EFMDGGSL--DVYRKIPEHVLGRIAVA------VVKGLTYLWSLKILHRDVKPSNML---VNTRGQVKLCDFGVSTQLVN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIethgRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFL------GSGVRLQ--QSVARgrlsfEAPE 243
Cdd:cd06619  148 SIAKT----YVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPqiqknqGSLMPLQllQCIVD-----EDPP 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 442620344 244 WKSI---SANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRD 282
Cdd:cd06619  219 VLPVgqfSEKFVHFITQCMRKQPKERPAPENLMDHPFIVQYN 260
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
17-282 2.75e-16

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 80.17  E-value: 2.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKRE--ATICHMLKHPHIVELLETYSSEGMLYMVFEFM 94
Cdd:cd05606    1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERImlSLVSTGGDCPFIVCMTYAFQTPDKLCFILDLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  95 EGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPGTRe 174
Cdd:cd05606   81 NGGDLHYHLSQHGV----FSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILL---DEHGHVRISDLGLACDFSKKK- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 175 tieTHGRVGCPHYMAPEVVTRRL-YGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWKSISANAKD 253
Cdd:cd05606  153 ---PHASVGTHGYMAPEVLQKGVaYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKHEIDRMTLTMNVELPDSFSPELKS 229
                        250       260       270
                 ....*....|....*....|....*....|....
gi 442620344 254 LVMKMLAANPHHRL-----SITEVLDHPWIRDRD 282
Cdd:cd05606  230 LLEGLLQRDVSKRLgclgrGATEVKEHPFFKGVD 263
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
16-278 3.77e-16

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 79.19  E-value: 3.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF--EF 93
Cdd:cd13983    7 EVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKA---ERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIFitEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  94 MEGSDLcFEVVRRAVagfVYSEAVACHYMRQILEALRYCHEND--ILHRDVRpaCallatvDN------SAPVKLGGFGS 165
Cdd:cd13983   84 MTSGTL-KQYLKRFK---RLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLK--C------DNifingnTGEVKIGDLGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 166 AIQLpgtrETIETHGRVGCPHYMAPEVVTRRlYGKGCDVWGAGVMLHVLLSGRLPFL--GSGVRLQQSVARGRL--SFEa 241
Cdd:cd13983  152 ATLL----RQSFAKSVIGTPEFMAPEMYEEH-YDEKVDIYAFGMCLLEMATGEYPYSecTNAAQIYKKVTSGIKpeSLS- 225
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 442620344 242 pewKSISANAKDLVMKMLaANPHHRLSITEVLDHPWI 278
Cdd:cd13983  226 ---KVKDPELKDFIEKCL-KPPDERPSARELLEHPFF 258
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
9-278 4.59e-16

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 79.78  E-value: 4.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   9 DDVYELCEvIGKGPFSIVRRCIHRESNQQFAVKivdvaKFTASpgLSTADLKR---EATICHMLKH-PHIVELLETYSSE 84
Cdd:cd06617    1 DDLEVIEE-LGRGAYGVVDKMRHVPTGTIMAVK-----RIRAT--VNSQEQKRllmDLDISMRSVDcPYTVTFYGALFRE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  85 GMLYMVFEFMegsDLCFEVVRRAV--AGFVYSEAVACHYMRQILEALRYCHEN-DILHRDVRPACALLatvDNSAPVKLG 161
Cdd:cd06617   73 GDVWICMEVM---DTSLDKFYKKVydKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLI---NRNGQVKLC 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 162 GFGSAIQLPGT-RETIEthgrVGCPHYMAPEVVTRRLYGKG----CDVWGAGVMLHVLLSGRLPFLGSGVRLQQ--SVAR 234
Cdd:cd06617  147 DFGISGYLVDSvAKTID----AGCKPYMAPERINPELNQKGydvkSDVWSLGITMIELATGRFPYDSWKTPFQQlkQVVE 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 442620344 235 GRlSFEAPEwKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06617  223 EP-SPQLPA-EKFSPEFQDFVNKCLKKNYKERPNYPELLQHPFF 264
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
12-282 5.17e-16

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 80.09  E-value: 5.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKR-EATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd14223    2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERiMLSLVSTGDCPFIVCMSYAFHTPDKLSFI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLP 170
Cdd:cd14223   82 LDLMNGGDLHYHLSQHGV----FSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILL---DEFGHVRISDLGLACDFS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRetieTHGRVGCPHYMAPEVVTRRL-YGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWKSISA 249
Cdd:cd14223  155 KKK----PHASVGTHGYMAPEVLQKGVaYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSP 230
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 442620344 250 NAKDLVMKMLAANPHHRLSI-----TEVLDHPWIRDRD 282
Cdd:cd14223  231 ELRSLLEGLLQRDVNRRLGCmgrgaQEVKEEPFFRGLD 268
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
18-282 5.74e-16

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 80.31  E-value: 5.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKREATIchMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd05610   12 ISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALA--LSKSPFIVHLYYSLQSANNVYLVMEYLIGG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DlcfevVRRAVAGFVY-SEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVKLGGFG-SAIQL------ 169
Cdd:cd05610   90 D-----VKSLLHIYGYfDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLIS---NEGHIKLTDFGlSKVTLnrelnm 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 -------------------PG------------------TRETIE------THGRV-GCPHYMAPEVVTRRLYGKGCDVW 205
Cdd:cd05610  162 mdilttpsmakpkndysrtPGqvlslisslgfntptpyrTPKSVRrgaarvEGERIlGTPDYLAPELLLGKPHGPAVDWW 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 206 GAGVMLHVLLSGRLPFlgsGVRLQQSVARGRLSFEAPeW----KSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDR 281
Cdd:cd05610  242 ALGVCLFEFLTGIPPF---NDETPQQVFQNILNRDIP-WpegeEELSVNAQNAIEILLTMDPTKRAGLKELKQHPLFHGV 317

                 .
gi 442620344 282 D 282
Cdd:cd05610  318 D 318
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
12-280 5.78e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 79.72  E-value: 5.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftASPGLSTADLkREATICHMLKHPHIVELLETYSSEGM--LYM 89
Cdd:cd07845    9 FEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDN--ERDGIPISSL-REITLLLNLRHPNIVELKEVVVGKHLdsIFL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEgSDLCfEVVRRAVAGFVYSEaVAChYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVKLGGFGSAiql 169
Cdd:cd07845   86 VMEYCE-QDLA-SLLDNMPTPFSESQ-VKC-LMLQLLRGLQYLHENFIIHRDLKVSNLLLT---DKGCLKIADFGLA--- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 pgtrETIETHgrvgcPHYMAPEVVT-----------RRLYGKGCDVWGAGVMLHVLLSGR--LP-------------FLG 223
Cdd:cd07845  156 ----RTYGLP-----AKPMTPKVVTlwyrapelllgCTTYTTAIDMWAVGCILAELLAHKplLPgkseieqldliiqLLG 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 224 S-------GVRLQQSVARGRL-----SFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRD 280
Cdd:cd07845  227 TpnesiwpGFSDLPLVGKFTLpkqpyNNLKHKFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYFKE 295
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
18-278 5.94e-16

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 79.92  E-value: 5.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKivDVAKFTASPGLSTADLkREATICHMLKHPHIVELLETYSSEGM-LYMVFEFMeG 96
Cdd:cd07856   18 VGMGAFGLVCSARDQLTGQNVAVK--KIMKPFSTPVLAKRTY-RELKLLKHLRHENIISLSDIFISPLEdIYFVTELL-G 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  97 SDLCFEVVRRAVagfvySEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSA-IQLPgtret 175
Cdd:cd07856   94 TDLHRLLTSRPL-----EKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNIL---VNENCDLKICDFGLArIQDP----- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 176 iETHGRVGCPHYMAPEV-VTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG----------------------------SGV 226
Cdd:cd07856  161 -QMTGYVSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGkdhvnqfsiitellgtppddvinticseNTL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 442620344 227 RLQQSVA-RGRLSFeAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd07856  240 RFVQSLPkRERVPF-SEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYL 291
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
8-298 6.45e-16

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 80.03  E-value: 6.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKivdvaKFtASPGLSTADLK---REATICHMLKHPHIVELLETY--- 81
Cdd:cd07851   13 VPDRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIK-----KL-SRPFQSAIHAKrtyRELRLLKHMKHENVIGLLDVFtpa 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  82 -SSEGM--LYMVFEFMeGSDLcFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACalLAtVDNSAPV 158
Cdd:cd07851   87 sSLEDFqdVYLVTHLM-GADL-NNIVKCQK----LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSN--LA-VNEDCEL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 159 KLGGFGSAIQLpgtreTIETHGRVGCPHYMAPEVVTRRL-YGKGCDVWGAGVMLHVLLSGRLPFLGS------------- 224
Cdd:cd07851  158 KILDFGLARHT-----DDEMTGYVATRWYRAPEIMLNWMhYNQTVDIWSVGCIMAELLTGKTLFPGSdhidqlkrimnlv 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 225 GV-------RLQQSVARGRLS----FEAPEWKSI----SANAKDLVMKMLAANPHHRLSITEVLDHPWIR---DRDKLQR 286
Cdd:cd07851  233 GTpdeellkKISSESARNYIQslpqMPKKDFKEVfsgaNPLAIDLLEKMLVLDPDKRITAAEALAHPYLAeyhDPEDEPV 312
                        330       340
                 ....*....|....*....|
gi 442620344 287 THLAD--------TVEELKR 298
Cdd:cd07851  313 APPYDqsfesrdlTVDEWKE 332
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
8-275 6.54e-16

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 78.69  E-value: 6.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDvakftaspgLSTADLKREATICHMLKHPHIVE----------L 77
Cdd:cd14047    4 FRQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVK---------LNNEKAEREVKALAKLDHPNIVRyngcwdgfdyD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  78 LETYSS------EGMLYMVFEFMEGSDLCFEVVRRAvaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLAt 151
Cdd:cd14047   75 PETSSSnssrskTKCLFIQMEFCEKGTLESWIEKRN--GEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLV- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 152 vdNSAPVKLGGFGSAIQLPGTREtiETHGRvGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSgrlpFLGSGV---RL 228
Cdd:cd14047  152 --DTGKVKIGDFGLVTSLKNDGK--RTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFELLH----VCDSAFeksKF 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 442620344 229 QQSVARGRLSFEAPEWKSISanaKDLVMKMLAANPHHRLSITEVLDH 275
Cdd:cd14047  223 WTDLRNGILPDIFDKRYKIE---KTIIKKMLSKKPEDRPNASEILRT 266
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
12-272 7.70e-16

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 80.47  E-value: 7.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05628    3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKE--QVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCFEVVRRAvagfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPG 171
Cdd:cd05628   81 EFLPGGDMMTLLMKKD----TLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLL---DSKGHVKLSDFGLCTGLKK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRET------------------------IETHGR---------VGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGR 218
Cdd:cd05628  154 AHRTefyrnlnhslpsdftfqnmnskrkAETWKRnrrqlafstVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGY 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442620344 219 LPFLG-SGVRLQQSVARGRLSFEAPEWKSISANAKDLVMKmLAANPHHRLSITEV 272
Cdd:cd05628  234 PPFCSeTPQETYKKVMNWKETLIFPPEVPISEKAKDLILR-FCCEWEHRIGAPGV 287
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
72-283 8.48e-16

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 78.96  E-value: 8.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  72 PHIVELLETYSSEGMLYMVFEFMEgsdLCFEVVRRAVAGFVySEAVACHYMRQILEALRYCHEN-DILHRDVRPACALLa 150
Cdd:cd06618   74 PYIVKCYGYFITDSDVFICMELMS---TCLDKLLKRIQGPI-PEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILL- 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 151 tvDNSAPVKLGGFGSAIQLPGTRetieTHGR-VGCPHYMAPEVVTRRLYGK---GCDVWGAGVMLHVLLSGRLPFLGSGV 226
Cdd:cd06618  149 --DESGNVKLCDFGISGRLVDSK----AKTRsAGCAAYMAPERIDPPDNPKydiRADVWSLGISLVELATGQFPYRNCKT 222
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 227 RLQqsVARGRLSFEAPEW---KSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDK 283
Cdd:cd06618  223 EFE--VLTKILNEEPPSLppnEGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRYET 280
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
495-572 1.23e-15

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 72.70  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  495 LVQFQKNTDEPMGITLKMTEDGR---CIVARIMHGGMIHRQAtLHVGDEIREINGQPVQHQSVGQLQRMLREARGSVTFK 571
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGdpgIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                  .
gi 442620344  572 I 572
Cdd:pfam00595  80 I 80
gmk PRK14737
guanylate kinase; Provisional
712-882 1.29e-15

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 76.18  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 712 KTLVLLGAHGVGRRHIKNTLISKYPDKYaYPIPHTTRPAKPEEENGRSYYFVSHDEMMADIGANEYLEYGTHEDAMYGTK 791
Cdd:PRK14737   5 KLFIISSVAGGGKSTIIQALLEEHPDFL-FSISCTTRAPRPGDEEGKTYFFLTIEEFKKGIADGEFLEWAEVHDNYYGTP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 792 LDTIRRIHTEGKMAILDVEPQALKILRtaEFTP---YVVFIAAPS--------LQNIADYDGSLERLAKE--SEMLRQly 858
Cdd:PRK14737  84 KAFIEDAFKEGRSAIMDIDVQGAKIIK--EKFPeriVTIFIEPPSeeeweerlIHRGTDSEESIEKRIENgiIELDEA-- 159
                        170       180
                 ....*....|....*....|....
gi 442620344 859 gHFFDLTIVNNDISETIATLETAI 882
Cdd:PRK14737 160 -NEFDYKIINDDLEDAIADLEAII 182
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
7-277 1.35e-15

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 79.15  E-value: 1.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   7 LFDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIV-DVAKFTAspglstaDLKREATICHMLKH------PHIVELLE 79
Cdd:cd14134    9 LLTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIrNVEKYRE-------AAKIEIDVLETLAEkdpngkSHCVQLRD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  80 TYSSEGMLYMVFEFMeGSDLcFEVVRRAVAGFVYSEAVAcHYMRQILEALRYCHENDILHRDVRPACALLatVDNSAP-- 157
Cdd:cd14134   82 WFDYRGHMCIVFELL-GPSL-YDFLKKNNYGPFPLEHVQ-HIAKQLLEAVAFLHDLKLTHTDLKPENILL--VDSDYVkv 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 158 ----------------VKLGGFGSAI-------QLPGTRetiethgrvgcpHYMAPEVVtrrlYGKG----CDVWGAGVM 210
Cdd:cd14134  157 ynpkkkrqirvpkstdIKLIDFGSATfddeyhsSIVSTR------------HYRAPEVI----LGLGwsypCDVWSIGCI 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 211 LHVLLSGRLPF---------------LGS----------GVRLQQSVARGRL--SFEAPEWKSISANAK----------- 252
Cdd:cd14134  221 LVELYTGELLFqthdnlehlammeriLGPlpkrmirrakKGAKYFYFYHGRLdwPEGSSSGRSIKRVCKplkrlmllvdp 300
                        330       340       350
                 ....*....|....*....|....*....|.
gi 442620344 253 ------DLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14134  301 ehrllfDLIRKMLEYDPSKRITAKEALKHPF 331
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
12-299 2.09e-15

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 78.60  E-value: 2.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKfTASPGLSTADLKREATICHMLK-HPHIVELLE----TYSSEGM 86
Cdd:cd07857    2 YELIKELGQGAYGIVCSARNAETSEEETVAIKKITN-VFSKKILAKRALRELKLLRHFRgHKNITCLYDmdivFPGNFNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEgSDLCfEVVRravAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPAcALLATVDnsAPVKLGGFGSA 166
Cdd:cd07857   81 LYLYEELME-ADLH-QIIR---SGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPG-NLLVNAD--CELKICDFGLA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLPGTRETIETH--GRVGCPHYMAPEV-VTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGS-------------GVRLQQ 230
Cdd:cd07857  153 RGFSENPGENAGFmtEYVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKdyvdqlnqilqvlGTPDEE 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 231 SVAR---------GRLSFEAP----EWKSISAN--AKDLVMKMLAANPHHRLSITEVLDHPWI---RDRDK---LQRT-- 287
Cdd:cd07857  233 TLSRigspkaqnyIRSLPNIPkkpfESIFPNANplALDLLEKLLAFDPTKRISVEEALEHPYLaiwHDPDDepvCQKPfd 312
                        330
                 ....*....|....*
gi 442620344 288 ---HLADTVEELKRY 299
Cdd:cd07857  313 fsfESEDSMEELRDM 327
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
18-211 2.16e-15

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 77.13  E-value: 2.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKftaspglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKMNTLSS-------NRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSAIQLPGTRETIE 177
Cdd:cd14155   74 NLEQLLDSNEP----LSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVVGDFGLAEKIPDYSDGKE 149
                        170       180       190
                 ....*....|....*....|....*....|....
gi 442620344 178 THGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVML 211
Cdd:cd14155  150 KLAVVGSPYWMAPEVLRGEPYNEKADVFSYGIIL 183
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
71-276 2.20e-15

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 77.31  E-value: 2.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  71 HPHIVELLETYSSEGMLYMVFEFMEGSdlCFEVVR--RAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACAL 148
Cdd:cd13982   54 HPNVIRYFCTEKDRQFLYIALELCAAS--LQDLVEspRESKLFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNIL 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 149 LATVD--NSAPVKLGGFGSAIQLPGTRET-IETHGRVGCPHYMAPEV----VTRRLyGKGCDVWGAG-VMLHVLLSGRLP 220
Cdd:cd13982  132 ISTPNahGNVRAMISDFGLCKKLDVGRSSfSRRSGVAGTSGWIAPEMlsgsTKRRQ-TRAVDIFSLGcVFYYVLSGGSHP 210
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344 221 FlGSGVRLQQSVARGRLSFEAP-EWKSISANAKDLVMKMLAANPHHRLSITEVLDHP 276
Cdd:cd13982  211 F-GDKLEREANILKGKYSLDKLlSLGEHGPEAQDLIERMIDFDPEKRPSAEEVLNHP 266
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
10-280 2.23e-15

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 77.81  E-value: 2.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTadlkREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd07869    5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAI----REASLLKGLKHANIVLLHDIIHTKETLTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEgSDLCFEVVRRAvaGFVYSEAVAChYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVKLGGFGSAiql 169
Cdd:cd07869   81 VFEYVH-TDLCQYMDKHP--GGLHPENVKL-FLFQLLRGLSYIHQRYILHRDLKPQNLLIS---DTGELKLADFGLA--- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 pgTRETIETH---GRVGCPHYMAPEVVTRRL-YGKGCDVWGAGVMLHVLLSGRLPFLGSGvRLQQSVARGRLSFEAPE-- 243
Cdd:cd07869  151 --RAKSVPSHtysNEVVTLWYRPPDVLLGSTeYSTCLDMWGVGCIFVEMIQGVAAFPGMK-DIQDQLERIFLVLGTPNed 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620344 244 ---------------------------WKSIS--ANAKDLVMKMLAANPHHRLSITEVLDHPWIRD 280
Cdd:cd07869  228 twpgvhslphfkperftlyspknlrqaWNKLSyvNHAEDLASKLLQCFPKNRLSAQAALSHEYFSD 293
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
12-278 2.47e-15

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 76.99  E-value: 2.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVakftaSPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd06646   11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIKL-----EPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcfEVVRRAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVKLGGFGSAIQLPG 171
Cdd:cd06646   86 EYCGGGSL--QDIYHVTGPL--SELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLT---DNGDVKLADFGVAAKITA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHgrVGCPHYMAPEVVTRRL---YGKGCDVWGAGVMlHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWK--- 245
Cdd:cd06646  159 TIAKRKSF--IGTPYWMAPEVAAVEKnggYNQLCDIWAVGIT-AIELAELQPPMFDLHPMRALFLMSKSNFQPPKLKdkt 235
                        250       260       270
                 ....*....|....*....|....*....|...
gi 442620344 246 SISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06646  236 KWSSTFHNFVKISLTKNPKKRPTAERLLTHLFV 268
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
12-211 2.58e-15

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 77.41  E-value: 2.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftASPGLStaDLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd14046    8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRS--ESKNNS--RILREVMLLSRLNHQHVVRYYQAWIERANLYIQM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcfevvRRAVAGFVYSEAV-ACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSAIQLP 170
Cdd:cd14046   84 EYCEKSTL-----RDLIDSGLFQDTDrLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGN---VKIGDFGLATSNK 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 171 GTRET----------------IETHGRVGCPHYMAPEVV--TRRLYGKGCDVWGAGVML 211
Cdd:cd14046  156 LNVELatqdinkstsaalgssGDLTGNVGTALYVAPEVQsgTKSTYNEKVDMYSLGIIF 214
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
18-278 2.81e-15

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 78.18  E-value: 2.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVK--------IVDvAKFTAspglstadlkREATICHMLKHPHIVELLETYSSEGM--- 86
Cdd:cd07858   13 IGRGAYGIVCSAKNSETNEKVAIKkianafdnRID-AKRTL----------REIKLLRHLDHENVIAIKDIMPPPHReaf 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 --LYMVFEFMEgSDLcFEVVRRavagfvySEAVA---CHY-MRQILEALRYCHENDILHRDVRPACALL-ATVDnsapVK 159
Cdd:cd07858   82 ndVYIVYELMD-TDL-HQIIRS-------SQTLSddhCQYfLYQLLRGLKYIHSANVLHRDLKPSNLLLnANCD----LK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 160 LGGFGSAiqlpgtRETIETHGrvgcphYMAPEVVTRRL-----------YGKGCDVWGAGVMLHVLLsGRLPF------- 221
Cdd:cd07858  149 ICDFGLA------RTTSEKGD------FMTEYVVTRWYrapelllncseYTTAIDVWSVGCIFAELL-GRKPLfpgkdyv 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 222 ---------LGSGVR-----LQQSVAR---------GRLSFeAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd07858  216 hqlklitelLGSPSEedlgfIRNEKARryirslpytPRQSF-ARLFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYL 294
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
12-277 3.38e-15

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 77.04  E-value: 3.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDV-----AKFTASpglstadlkREATICHMLKHPHIVELLETYSSEGM 86
Cdd:cd07844    2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLeheegAPFTAI---------REASLLKDLKHANIVTLHDIIHTKKT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEgSDLCFEVVRRAvaGFVYSEAVAChYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSA 166
Cdd:cd07844   73 LTLVFEYLD-TDLKQYMDDCG--GGLSMHNVRL-FLFQLLRGLAYCHQRRVLHRDLKPQNLL---ISERGELKLADFGLA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 iqlpgTRETIETH---GRVGCPHYMAPEVVT-RRLYGKGCDVWGAGVMLHVLLSGRLPFLGS------------------ 224
Cdd:cd07844  146 -----RAKSVPSKtysNEVVTLWYRPPDVLLgSTEYSTSLDMWGVGCIFYEMATGRPLFPGStdvedqlhkifrvlgtpt 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620344 225 -----GVRLQQSVARGRLSFEAPE-----WKSIS--ANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07844  221 eetwpGVSSNPEFKPYSFPFYPPRplinhAPRLDriPHGEELALKFLQYEPKKRISAAEAMKHPY 285
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
17-282 1.02e-14

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 76.31  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTaspglSTADLKREATICHMLK----HPHIVELLETYSSEGMLYMVFE 92
Cdd:cd05588    2 VIGRGSYAKVLMVELKKTKRIYAMKVIKKELVN-----DDEDIDWVQTEKHVFEtasnHPFLVGLHSCFQTESRLFFVIE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  93 FMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQlpGT 172
Cdd:cd05588   77 FVNGGDLMFHMQRQRR----LPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLL---DSEGHIKLTDYGMCKE--GL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 173 RETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF--LGSGVRLQQSVARG--RLSFEAPEW--KS 246
Cdd:cd05588  148 RPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdiVGSSDNPDQNTEDYlfQVILEKPIRipRS 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 442620344 247 ISANAKDLVMKMLAANPHHRL------SITEVLDHPWIRDRD 282
Cdd:cd05588  228 LSVKAASVLKGFLNKNPAERLgchpqtGFADIQSHPFFRTID 269
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
57-282 1.07e-14

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 76.97  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  57 ADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHEND 136
Cdd:cd05626   46 AHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMEV----FPEVLARFYIAELTLAIESVHKMG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 137 ILHRDVRPACALlatVDNSAPVKLGGFGSAIQLPGTR----------------------------------ETIE----- 177
Cdd:cd05626  122 FIHRDIKPDNIL---IDLDGHIKLTDFGLCTGFRWTHnskyyqkgshirqdsmepsdlwddvsncrcgdrlKTLEqratk 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 178 ------THGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQSVARGRLSFEAPEWKSISAN 250
Cdd:cd05626  199 qhqrclAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQPPFLApTPTETQLKVINWENTLHIPPQVKLSPE 278
                        250       260       270
                 ....*....|....*....|....*....|....
gi 442620344 251 AKDLVMKMLAANPHH--RLSITEVLDHPWIRDRD 282
Cdd:cd05626  279 AVDLITKLCCSAEERlgRNGADDIKAHPFFSEVD 312
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
17-276 1.59e-14

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 74.96  E-value: 1.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCihRESNQQFAVKIVDVAKFTASPGLST----------------ADLKREATICHMLKHPHIVELLET 80
Cdd:cd14000    1 LLGDGGFGSVYRA--SYKGEPVAVKIFNKHTSSNFANVPAdtmlrhlratdamknfRLLRQELTVLSHLHHPSIVYLLGI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  81 YSSEGMLYMVFEFMEGSDLCFEVVRRAVA--GFVYSEAVACHymrqILEALRYCHENDILHRDVRPACALLATVD--NSA 156
Cdd:cd14000   79 GIHPLMLVLELAPLGSLDHLLQQDSRSFAslGRTLQQRIALQ----VADGLRYLHSAMIIYRDLKSHNVLVWTLYpnSAI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 157 PVKLGGFGSAIQlpGTRETIETHGrvGCPHYMAPEVVTRR-LYGKGCDVWGAGVMLHVLLSGRLPFLGsGVRLQQSVA-R 234
Cdd:cd14000  155 IIKIADYGISRQ--CCRMGAKGSE--GTPGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSGGAPMVG-HLKFPNEFDiH 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 442620344 235 GRL-----SFEAPEWKSIsanaKDLVMKMLAANPHHR---LSITEVLDHP 276
Cdd:cd14000  230 GGLrpplkQYECAPWPEV----EVLMKKCWKENPQQRptaVTVVSILNSP 275
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
14-274 1.93e-14

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 74.81  E-value: 1.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  14 LCEVIGKGPFSIVRR--CIHRESNQQFAVKIVDVAKFTASPGLSTaDLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05049    9 LKRELGEGAFGKVFLgeCYNLEPEQDKMLVAVKTLKDASSPDARK-DFEREAELLTNLQHENIVKFYGVCTEGDPLLMVF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLCfEVVRR--AVAGFVYSEAVA---------CHYMRQILEALRYCHENDILHRDvrpacalLAT----VDNSA 156
Cdd:cd05049   88 EYMEHGDLN-KFLRShgPDAAFLASEDSApgeltlsqlLHIAVQIASGMVYLASQHFVHRD-------LATrnclVGTNL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 157 PVKLGGFGSAIQLPGTrETIETHGRVGCP-HYMAPEVVTRRLYGKGCDVWGAGVML-HVLLSGRLPFLG-SGVRLQQSVA 233
Cdd:cd05049  160 VVKIGDFGMSRDIYST-DYYRVGGHTMLPiRWMPPESILYRKFTTESDVWSFGVVLwEIFTYGKQPWFQlSNTEVIECIT 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 442620344 234 RGRLsFEAPEwkSISANAKDLVMKMLAANPHHRLSITEVLD 274
Cdd:cd05049  239 QGRL-LQRPR--TCPSEVYAVMLGCWKREPQQRLNIKDIHK 276
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
12-221 2.25e-14

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 77.86  E-value: 2.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVdvaKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEG--MLYM 89
Cdd:PTZ00266   15 YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAI---SYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFLNKAnqKLYI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   90 VFEFMEGSDLCFEVVR-RAVAGFVYSEAVAcHYMRQILEALRYCHE-------NDILHRDVRPACALLATVD-------- 153
Cdd:PTZ00266   92 LMEFCDAGDLSRNIQKcYKMFGKIEEHAIV-DITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTGIrhigkita 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344  154 -----NSAPV-KLGGFGSAIQLpgtreTIET--HGRVGCPHYMAPEVVTR--RLYGKGCDVWGAGVMLHVLLSGRLPF 221
Cdd:PTZ00266  171 qannlNGRPIaKIGDFGLSKNI-----GIESmaHSCVGTPYYWSPELLLHetKSYDDKSDMWALGCIIYELCSGKTPF 243
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
18-283 2.32e-14

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 74.78  E-value: 2.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAkftASPGLSTADLkREATICHMLKHPHIVELLETYSSE-GMLYMVFEFME- 95
Cdd:cd06620   13 LGAGNGGSVSKVLHIPTGTIMAKKVIHID---AKSSVRKQIL-RELQILHECHSPYIVSFYGAFLNEnNNIIICMEYMDc 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 GSdlcFEVVRRaVAGFVySEAVACHYMRQILEALRYCH-ENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLpgTRE 174
Cdd:cd06620   89 GS---LDKILK-KKGPF-PEEVLGKIAVAVLEGLTYLYnVHRIIHRDIKPSNIL---VNSKGQIKLCDFGVSGEL--INS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 175 TIETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR-------------LQQSVARG--RLsf 239
Cdd:cd06620  159 IADTF--VGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDddgyngpmgildlLQRIVNEPppRL-- 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 442620344 240 eaPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDK 283
Cdd:cd06620  235 --PKDRIFPKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQAVR 276
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
5-306 2.69e-14

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 75.09  E-value: 2.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   5 EILFDDVYElcevIGKGPFSIVRRCIHRESNQQFAVKivdvaKFTASPGLST---ADLKREATICHMLKHPHIVELLETY 81
Cdd:cd06635   24 EKLFSDLRE----IGHGSFGAVYFARDVRTSEVVAIK-----KMSYSGKQSNekwQDIIKEVKFLQRIKHPNSIEYKGCY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  82 SSEGMLYMVFEFMEGS--DLcFEVVRRAVagfvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVK 159
Cdd:cd06635   95 LREHTAWLVMEYCLGSasDL-LEVHKKPL-----QEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLT---EPGQVK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 160 LGGFGSA-IQLPGtretietHGRVGCPHYMAPEVV---TRRLYGKGCDVWGAGVMLHVLLSGRLPF--LGSGVRLQQSVA 233
Cdd:cd06635  166 LADFGSAsIASPA-------NSFVGTPYWMAPEVIlamDEGQYDGKVDVWSLGITCIELAERKPPLfnMNAMSALYHIAQ 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 234 RGRLSFEAPEWKSISANAKDLVMKMLaanPHHRLSITEVLDHPWI-RDR------DKLQRThlADTVEELKRYNARRKLK 306
Cdd:cd06635  239 NESPTLQSNEWSDYFRNFVDSCLQKI---PQDRPTSEELLKHMFVlRERpetvliDLIQRT--KDAVRELDNLQYRKMKK 313
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
11-278 3.00e-14

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 74.27  E-value: 3.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  11 VYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVakftaspglsTADLKRE--ATICHMLKHPHIVELLETYSS----- 83
Cdd:cd06636   17 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV----------TEDEEEEikLEINMLKKYSHHRNIATYYGAfikks 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 ----EGMLYMVFEFMeGSDLCFEVVRRaVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVK 159
Cdd:cd06636   87 ppghDDQLWLVMEFC-GAGSVTDLVKN-TKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT---ENAEVK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 160 LGGFGSAIQLP---GTRETIethgrVGCPHYMAPEVVT-----RRLYGKGCDVWGAGVMLHVLLSGRLPFLG-SGVRLQQ 230
Cdd:cd06636  162 LVDFGVSAQLDrtvGRRNTF-----IGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDmHPMRALF 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 442620344 231 SVARGrlsfEAPEWKSISANAK--DLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd06636  237 LIPRN----PPPKLKSKKWSKKfiDFIEGCLVKNYLSRPSTEQLLKHPFI 282
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
16-274 3.24e-14

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 73.53  E-value: 3.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQ---QFAVKIVDVAKFTASPGLStaDLKREATICHMLKHPHIVELLETYSSEGMLyMVFE 92
Cdd:cd05040    1 EKLGDGSFGVVRRGEWTTPSGkviQVAVKCLKSDVLSQPNAMD--DFLKEVNAMHSLDHPNLIRLYGVVLSSPLM-MVTE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  93 FMEGSDLcFEVVRRAVAGFVYSeaVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSAIQLPGT 172
Cdd:cd05040   78 LAPLGSL-LDRLRKDQGHFLIS--TLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDK---VKIGDFGLMRALPQN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 173 RE--TIETHGRVGCPhYMAPEVVTRRLYGKGCDVWGAGVMLHVLLS-GRLPFLG-SGVRLQQSVARGRLSFEAPEwkSIS 248
Cdd:cd05040  152 EDhyVMQEHRKVPFA-WCAPESLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLGlNGSQILEKIDKEGERLERPD--DCP 228
                        250       260
                 ....*....|....*....|....*.
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEVLD 274
Cdd:cd05040  229 QDIYNVMLQCWAHKPADRPTFVALRD 254
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
12-275 3.40e-14

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 74.14  E-value: 3.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAkftaSPGLSTADLKREATICHMLKHPHIVELLETYSS-------- 83
Cdd:cd14048    8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLP----NNELAREKVLREVRALAKLDHPGIVRYFNAWLErppegwqe 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 ---EGMLYMVFEFMEGSDLcFEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPAcALLATVDNSapVKL 160
Cdd:cd14048   84 kmdEVYLYIQMQLCRKENL-KDWMNRRCTMESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPS-NVFFSLDDV--VKV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 161 GGFGSAIQLPGTRETI---------ETH-GRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLsgrLPFLGSGVRLQQ 230
Cdd:cd14048  160 GDFGLVTAMDQGEPEQtvltpmpayAKHtGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI---YSFSTQMERIRT 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 442620344 231 SVARGRLSFeAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDH 275
Cdd:cd14048  237 LTDVRKLKF-PALFTNKYPEERDMVQQMLSPSPSERPEAHEVIEH 280
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
18-277 3.60e-14

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 74.28  E-value: 3.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTadlkREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEgS 97
Cdd:cd07871   13 LGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAI----REVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLD-S 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DL------CfevvrravaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFG--SAIQL 169
Cdd:cd07871   88 DLkqyldnC---------GNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLL---INEKGELKLADFGlaRAKSV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 PgtreTIETHGRVGCPHYMAPEVVTRRL-YGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPE-WKSI 247
Cdd:cd07871  156 P----TKTYSNEVVTLWYRPPDVLLGSTeYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLLGTPTEEtWPGV 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442620344 248 SANAK--------------------------DLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07871  232 TSNEEfrsylfpqyraqplinhaprldtdgiDLLSSLLLYETKSRISAEAALRHSY 287
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
18-222 3.62e-14

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 74.02  E-value: 3.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAkftaspgLSTADLKR-----EATICHMLKHPHIV------ELLETYSSEGM 86
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQE-------LSPSDKNRerwclEVQIMKKLNHPNVVsardvpPELEKLSPNDL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEGSDLcFEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSA 166
Cdd:cd13989   74 PLLAMEYCSGGDL-RKVLNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIYKLIDLGYA 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442620344 167 IQLPGTRETIEThgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFL 222
Cdd:cd13989  153 KELDQGSLCTSF---VGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFL 205
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
10-277 4.15e-14

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 74.60  E-value: 4.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVdVAKFTASpgLSTADLKREATICHMLKHPHIVELLETYSSEGML-- 87
Cdd:cd07880   15 DRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKL-YRPFQSE--LFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLdr 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 ----YMVFEFMeGSDLcfevvRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACalLAtVDNSAPVKLGGF 163
Cdd:cd07880   92 fhdfYLVMPFM-GTDL-----GKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGN--LA-VNEDCELKILDF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 164 GSAIQLPGtretiETHGRVGCPHYMAPEVVTRRL-YGKGCDVWGAGVMLHVLLSGRLPFLGSG----------------- 225
Cdd:cd07880  163 GLARQTDS-----EMTGYVVTRWYRAPEVILNWMhYTQTVDIWSVGCIMAEMLTGKPLFKGHDhldqlmeimkvtgtpsk 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620344 226 ---VRLQQSVARGRLS----FEAPEWKSISANAKDLVM----KMLAANPHHRLSITEVLDHPW 277
Cdd:cd07880  238 efvQKLQSEDAKNYVKklprFRKKDFRSLLPNANPLAVnvleKMLVLDAESRITAAEALAHPY 300
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
70-279 4.26e-14

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 75.07  E-value: 4.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  70 KHPHIVELLETYSSEGMLYMVFEFMEGSDlcFEVVRRAVAgfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALl 149
Cdd:cd05600   69 NSPWLVKLLYAFQDPENVYLAMEYVPGGD--FRTLLNNSG--ILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFL- 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 150 atVDNSAPVKLGGFG-------------SAIQLPGTRETIET----------------------HGRVGCPHYMAPEVVT 194
Cdd:cd05600  144 --IDSSGHIKLTDFGlasgtlspkkiesMKIRLEEVKNTAFLeltakerrniyramrkedqnyaNSVVGSPDYMAPEVLR 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 195 RRLYGKGCDVWGAGVMLHVLLSGRLPFLGS-------GVRLQQSVARGRLSFEAPEWKSISANAKDLVMKMLaANPHHRL 267
Cdd:cd05600  222 GEGYDLTVDYWSLGCILFECLVGFPPFSGStpnetwaNLYHWKKTLQRPVYTDPDLEFNLSDEAWDLITKLI-TDPQDRL 300
                        250
                 ....*....|...
gi 442620344 268 -SITEVLDHPWIR 279
Cdd:cd05600  301 qSPEQIKNHPFFK 313
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
62-275 5.89e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 74.65  E-value: 5.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  62 EATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGSDLCFEVVRRAVAgfvyseavACHYM---RQILEALRYCHENDIL 138
Cdd:PHA03212 133 EAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKTDLYCYLAAKRNIA--------ICDILaieRSVLRAIQYLHENRII 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 139 HRDVRPACALlatVDNSAPVKLGGFGSAIqLPGTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSG- 217
Cdd:PHA03212 205 HRDIKAENIF---INHPGDVCLGDFGAAC-FPVDINANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCh 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 218 -------------------RLPFLGSGV------------------RLQQSVARGRLSfeAPEWKSISANAKD---LVMK 257
Cdd:PHA03212 281 dslfekdgldgdcdsdrqiKLIIRRSGThpnefpidaqanldeiyiGLAKKSSRKPGS--RPLWTNLYELPIDleyLICK 358
                        250
                 ....*....|....*...
gi 442620344 258 MLAANPHHRLSITEVLDH 275
Cdd:PHA03212 359 MLAFDAHHRPSAEALLDF 376
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
18-277 6.02e-14

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 74.03  E-value: 6.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFA---VKIVDVAKFTASPGLSTAD------LKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAikkVKIIEISNDVTKDRQLVGMcgihftTLRELKIMNEIKHENIMGLVDVYVEGDFIN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEgSDLCfEVVRRAVagFVYSEAVAChYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAiq 168
Cdd:PTZ00024  97 LVMDIMA-SDLK-KVVDRKI--RLTESQVKC-ILLQILNGLNVLHKWYFMHRDLSPANIF---INSKGICKIADFGLA-- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 lpgtretiethGRVGCPHY---------------MAPEVVT-----------RRLYGKGCDVWGAGVMLHVLLSGRLPFL 222
Cdd:PTZ00024 167 -----------RRYGYPPYsdtlskdetmqrreeMTSKVVTlwyrapellmgAEKYHFAVDMWSVGCIFAELLTGKPLFP 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 223 GSGvRLQQsvaRGRLSF-----EAPEW--------------------KSI----SANAKDLVMKMLAANPHHRLSITEVL 273
Cdd:PTZ00024 236 GEN-EIDQ---LGRIFEllgtpNEDNWpqakklplyteftprkpkdlKTIfpnaSDDAIDLLQSLLKLNPLERISAKEAL 311

                 ....
gi 442620344 274 DHPW 277
Cdd:PTZ00024 312 KHEY 315
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
9-283 6.78e-14

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 73.62  E-value: 6.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   9 DDVYELCEvIGKGPFSIVRRCIHRESNQQFAVKIVdvaKFTASPGLSTADLkREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd06615    1 DDFEKLGE-LGAGNGGVVTKVLHRPSGLIMARKLI---HLEIKPAIRNQII-RELKVLHECNSPYIVGFYGAFYSDGEIS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGS--DLCFEVVRRAVAGFVYSEAVAchymrqILEALRYCHEN-DILHRDVRPACALlatVDNSAPVKLGGFGS 165
Cdd:cd06615   76 ICMEHMDGGslDQVLKKAGRIPENILGKISIA------VLRGLTYLREKhKIMHRDVKPSNIL---VNSRGEIKLCDFGV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 166 AIQLpgtretIETHGR--VGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLP---------------FLGSGVRL 228
Cdd:cd06615  147 SGQL------IDSMANsfVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPipppdakeleamfgrPVSEGEAK 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620344 229 QQSVARGRLSFEAPEWKSI--------------------SANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRDK 283
Cdd:cd06615  221 ESHRPVSGHPPDSPRPMAIfelldyivnepppklpsgafSDEFQDFVDKCLKKNPKERADLKELTKHPFIKRAEL 295
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
12-282 7.22e-14

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 73.94  E-value: 7.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLKR-EATICHMLKHPHIVELLETYSSEGMLYMV 90
Cdd:cd05633    7 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERiMLSLVSTGDCPFIVCMTYAFHTPDKLCFI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLP 170
Cdd:cd05633   87 LDLMNGGDLHYHLSQHGV----FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHVRISDLGLACDFS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 171 GTRetieTHGRVGCPHYMAPEVVTR-RLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWKSISA 249
Cdd:cd05633  160 KKK----PHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDSFSP 235
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 442620344 250 NAKDLVMKMLAANPHHRLSI-----TEVLDHPWIRDRD 282
Cdd:cd05633  236 ELKSLLEGLLQRDVSKRLGChgrgaQEVKEHSFFKGID 273
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
7-279 8.82e-14

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 72.48  E-value: 8.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   7 LFDDVYElcevIGKGPFSIVRRCIHRESNQQFAVKivdvaKFTASPGLSTA---DLKREATICHMLKHPHIVELLETYSS 83
Cdd:cd06607    2 IFEDLRE----IGHGSFGAVYYARNKRTSEVVAIK-----KMSYSGKQSTEkwqDIIKEVKFLRQLRHPNTIEYKGCYLR 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGMLYMVFEFMEGS--DLcFEVVRRAVagfvySE---AVACHymrQILEALRYCHENDILHRDVRPACALLAtvdNSAPV 158
Cdd:cd06607   73 EHTAWLVMEYCLGSasDI-VEVHKKPL-----QEveiAAICH---GALQGLAYLHSHNRIHRDVKAGNILLT---EPGTV 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 159 KLGGFGSA-IQLPGTretiethGRVGCPHYMAPEVV---TRRLYGKGCDVWGAGVMLhVLLSGRLP--FLGSGVRLQQSV 232
Cdd:cd06607  141 KLADFGSAsLVCPAN-------SFVGTPYWMAPEVIlamDEGQYDGKVDVWSLGITC-IELAERKPplFNMNAMSALYHI 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 442620344 233 ARGrlsfEAPEWKSI--SANAKDLVMKMLAANPHHRLSITEVLDHPWIR 279
Cdd:cd06607  213 AQN----DSPTLSSGewSDDFRNFVDSCLQKIPQDRPSAEDLLKHPFVT 257
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
18-299 9.92e-14

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 73.40  E-value: 9.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVdvakftASPGLSTADLKR---EATICHMLKHPHIVELLETYSSEGML------Y 88
Cdd:cd07879   23 VGSGAYGSVCSAIDKRTGEKVAIKKL------SRPFQSEIFAKRayrELTLLKHMQHENVIGLLDVFTSAVSGdefqdfY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEgSDLcfevvrRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACalLAtVDNSAPVKLGGFGSAiq 168
Cdd:cd07879   97 LVMPYMQ-TDL------QKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGN--LA-VNEDCELKILDFGLA-- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 lpgTRETIETHGRVGCPHYMAPEVVTRRL-YGKGCDVWGAGVMLHVLLSGRLPFLG-------------SGV-------R 227
Cdd:cd07879  165 ---RHADAEMTGYVVTRWYRAPEVILNWMhYNQTVDIWSVGCIMAEMLTGKTLFKGkdyldqltqilkvTGVpgpefvqK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 228 LQQSVARGRLSF--EAPE------WKSISANAKDLVMKMLAANPHHRLSITEVLDHPW---IRD----------RDKLQR 286
Cdd:cd07879  242 LEDKAAKSYIKSlpKYPRkdfstlFPKASPQAVDLLEKMLELDVDKRLTATEALEHPYfdsFRDadeeteqqpyDDSLEN 321
                        330
                 ....*....|...
gi 442620344 287 THLadTVEELKRY 299
Cdd:cd07879  322 EKL--SVDEWKKH 332
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
12-223 1.23e-13

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 73.05  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVD--VAKFTASpglstadlKREATICHML--------KHpHIVELLETY 81
Cdd:cd14212    1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKnkPAYFRQA--------MLEIAILTLLntkydpedKH-HIVRLLDHF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  82 SSEGMLYMVFEfMEGSDLcFEVVR-RAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVdNSAPVKL 160
Cdd:cd14212   72 MHHGHLCIVFE-LLGVNL-YELLKqNQFRGL--SLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNL-DSPEIKL 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620344 161 GGFGSAIQlpgtrETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLlsgrlpFLG 223
Cdd:cd14212  147 IDFGSACF-----ENYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAEL------FLG 198
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
12-278 1.52e-13

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 72.58  E-value: 1.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLStadlkrEATICHMLKH------PHIVELLETYSSEG 85
Cdd:cd14210   15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKRFHQQALV------EVKILKHLNDndpddkHNIVRYKDSFIFRG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 MLYMVFEfMEGSDLcFEVVR-RAVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSApVKLGGFG 164
Cdd:cd14210   89 HLCIVFE-LLSINL-YELLKsNNFQGL--SLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSS-IKVIDFG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 SA----------IQlpgTRetiethgrvgcpHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGR---------------- 218
Cdd:cd14210  164 SScfegekvytyIQ---SR------------FYRAPEVILGLPYDTAIDMWSLGCILAELYTGYplfpgeneeeqlacim 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 219 ----LP--------------FLGSGVRLQQSVARGRLsfEAPEWKSISANAK-------DLVMKMLAANPHHRLSITEVL 273
Cdd:cd14210  229 evlgVPpkslidkasrrkkfFDSNGKPRPTTNSKGKK--RRPGSKSLAQVLKcddpsflDFLKKCLRWDPSERMTPEEAL 306

                 ....*
gi 442620344 274 DHPWI 278
Cdd:cd14210  307 QHPWI 311
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
8-280 1.72e-13

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 72.89  E-value: 1.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELceviGKGPFSIVRRCIHRESNQQFAVKivdvaKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEG-- 85
Cdd:cd07854    7 YMDLRPL----GCGSNGLVFSAVDSDCDKRVAVK-----KIVLTDPQSVKHALREIKIIRRLDHDNIVKVYEVLGPSGsd 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 ------------MLYMVFEFMEgSDLcfevvRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVD 153
Cdd:cd07854   78 ltedvgsltelnSVYIVQEYME-TDL-----ANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTED 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 154 nsAPVKLGGFGSAiqlpgtretiethgRVGCPH---------------YMAPEVVTR-RLYGKGCDVWGAGVMLHVLLSG 217
Cdd:cd07854  152 --LVLKIGDFGLA--------------RIVDPHyshkgylseglvtkwYRSPRLLLSpNNYTKAIDMWAAGCIFAEMLTG 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 218 RLPFLG------------------------------SGVRLQQSVARGRLSFEAPEwksISANAKDLVMKMLAANPHHRL 267
Cdd:cd07854  216 KPLFAGaheleqmqlilesvpvvreedrnellnvipSFVRNDGGEPRRPLRDLLPG---VNPEALDFLEQILTFNPMDRL 292
                        330
                 ....*....|...
gi 442620344 268 SITEVLDHPWIRD 280
Cdd:cd07854  293 TAEEALMHPYMSC 305
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
495-573 1.92e-13

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467153 [Multi-domain]  Cd Length: 81  Bit Score: 66.41  E-value: 1.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 495 LVQFQKNTDEPMGITLK--MTEDGRCIVARIMHGGMIHRQATLHVGDEIREINGQPVQHQSVGQLQRMLREARGSVTFKI 572
Cdd:cd00136    1 TVTLEKDPGGGLGFSIRggKDGGGGIFVSRVEPGGPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELLKSAGGEVTLTV 80

                 .
gi 442620344 573 V 573
Cdd:cd00136   81 R 81
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
61-279 2.52e-13

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 72.06  E-value: 2.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  61 REATICHMLKHPHIVELLETYSSEGML------YMVFEFMEGSdLCfEVVRR-----AVAGFVYseavachymrQILEAL 129
Cdd:cd07850   48 RELVLMKLVNHKNIIGLLNVFTPQKSLeefqdvYLVMELMDAN-LC-QVIQMdldheRMSYLLY----------QMLCGI 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 130 RYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAiQLPGTRETIETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGV 209
Cdd:cd07850  116 KHLHSAGIIHRDLKPSNIV---VKSDCTLKILDFGLA-RTAGTSFMMTPY--VVTRYYRAPEVILGMGYKENVDIWSVGC 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 210 MLHVLLSGRLPFLGS-------------GV-------RLQQSVA-----RGR---LSFEA--PEW----------KSISA 249
Cdd:cd07850  190 IMGEMIRGTVLFPGTdhidqwnkiieqlGTpsdefmsRLQPTVRnyvenRPKyagYSFEElfPDVlfppdseehnKLKAS 269
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 250 NAKDLVMKMLAANPHHRLSITEVLDHPWIR 279
Cdd:cd07850  270 QARDLLSKMLVIDPEKRISVDDALQHPYIN 299
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
61-277 2.58e-13

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 72.38  E-value: 2.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  61 REATICHMLKHPHIVELLETYSSEGML------YMVFEFMeGSDL-----CFEVVRRAVAGFVYseavachymrQILEAL 129
Cdd:cd07877   65 RELRLLKHMKHENVIGLLDVFTPARSLeefndvYLVTHLM-GADLnnivkCQKLTDDHVQFLIY----------QILRGL 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 130 RYCHENDILHRDVRPACalLAtVDNSAPVKLGGFGSAiqlpgtRETI-ETHGRVGCPHYMAPEVVTRRL-YGKGCDVWGA 207
Cdd:cd07877  134 KYIHSADIIHRDLKPSN--LA-VNEDCELKILDFGLA------RHTDdEMTGYVATRWYRAPEIMLNWMhYNQTVDIWSV 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 208 GVMLHVLLSGRLPFLGSG--------------------VRLQQSVARGRLSF--EAPEWK----SISAN--AKDLVMKML 259
Cdd:cd07877  205 GCIMAELLTGRTLFPGTDhidqlklilrlvgtpgaellKKISSESARNYIQSltQMPKMNfanvFIGANplAVDLLEKML 284
                        250
                 ....*....|....*...
gi 442620344 260 AANPHHRLSITEVLDHPW 277
Cdd:cd07877  285 VLDSDKRITAAQALAHAY 302
PDZ_MPP5-like cd06798
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related ...
494-574 2.73e-13

PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP5, Drosophila Stardust, and related domains. MPP5 (also known as MAGUK p55 subfamily member 1, protein associated with Lin-7 1 or PALS1) and Drosophila Stardust are membrane-associated guanylate kinase (MAGUK)-like proteins that serve as signaling and scaffolding proteins, linking different proteins critical to the formation and maintenance of tight junctions (TJ) and apical-basal polarity. Apical-basal polarity determinants cluster in complexes; in particular, the Crumbs complex (Crb, MPP5, and PATJ) and the PAR/aPKC-complex (PAR-3, PAR-6, aPKC) determine the apical plasma membrane domain. Within the Crumbs complex, Crb is stabilized in the plasma membrane by MPP5, which in turn recruits PATJ and Lin-7 to the complex. MPP5 also links the Crumbs complex with the PAR/aPKC-complex. The Drosophila homolog of the Crumbs complex is the (CRB)-Stardust (Sdt)-Discs Lost (Dlt) complex. MPP5 also acts as an interaction partner for SARS-CoV envelope protein E, which results in delayed formation of TJs and dysregulation of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP5-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467259 [Multi-domain]  Cd Length: 79  Bit Score: 65.83  E-value: 2.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 494 RLVQFQKnTDEPMGITLKmTEDGRCIVARIMHGGMIHRQATLHVGDEIREINGQPVQHQSVGQLQRMLREARGSVTFKIV 573
Cdd:cd06798    1 KIVRIEK-TREPLGATVR-NEGDSVIISRIVKGGAAEKSGLLHEGDEILEINGIEIRGKDVNEVCDLLADMHGTLTFLLI 78

                 .
gi 442620344 574 P 574
Cdd:cd06798   79 P 79
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
10-277 5.64e-13

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 70.80  E-value: 5.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTadlkREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd07873    2 ETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTAI----REVSLLKDLKHANIVTLHDIIHTEKSLTL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGS-----DLCFEVVR-RAVAGFVYseavachymrQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGF 163
Cdd:cd07873   78 VFEYLDKDlkqylDDCGNSINmHNVKLFLF----------QLLRGLAYCHRRKVLHRDLKPQNLL---INERGELKLADF 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 164 G--SAIQLPgtreTIETHGRVGCPHYMAPEVVTRRL-YGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQ----------- 229
Cdd:cd07873  145 GlaRAKSIP----TKTYSNEVVTLWYRPPDILLGSTdYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQlhfifrilgtp 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620344 230 -QSVARGRLSFEA------PEWKS---------ISANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07873  221 tEETWPGILSNEEfksynyPKYRAdalhnhaprLDSDGADLLSKLLQFEGRKRISAEEAMKHPY 284
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
18-222 6.47e-13

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 70.38  E-value: 6.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKivdvakfTASPGLSTADLKR---EATICHMLKHPHIV------ELLETYSSEGMLY 88
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIK-------QCRQELSPKNRERwclEIQIMKRLNHPNVVaardvpEGLQKLAPNDLPL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLcfevvRRAVAGFV----YSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFG 164
Cdd:cd14038   75 LAMEYCQGGDL-----RKYLNQFEnccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLIHKIIDLG 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 165 SAIQLPGTRETIEThgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFL 222
Cdd:cd14038  150 YAKELDQGSLCTSF---VGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFL 204
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
18-275 6.77e-13

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 69.65  E-value: 6.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglstaDLKREATichmLKHPHIVELLETYSSEGMLYMVFEFMEGs 97
Cdd:cd13995   12 IPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPS------DVEIQAC----FRHENIAELYGALLWEETVHLFMEAGEG- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 dlcfevvrravaGFVYSEAVACHYMR---------QILEALRYCHENDILHRDVRPACALLAtvdnSAPVKLGGFGSAIQ 168
Cdd:cd13995   81 ------------GSVLEKLESCGPMRefeiiwvtkHVLKGLDFLHSKNIIHHDIKPSNIVFM----STKAVLVDFGLSVQ 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LpgTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWKSI- 247
Cdd:cd13995  145 M--TEDVYVPKDLRGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLYIIHKQAPPLEDIa 222
                        250       260       270
                 ....*....|....*....|....*....|.
gi 442620344 248 ---SANAKDLVMKMLAANPHHRLSITEVLDH 275
Cdd:cd13995  223 qdcSPAMRELLEAALERNPNHRSSAAELLKH 253
SH3_DLG-like cd11861
Src Homology 3 domain of Disks large homolog proteins; The DLG-like proteins are scaffolding ...
586-643 8.19e-13

Src Homology 3 domain of Disks large homolog proteins; The DLG-like proteins are scaffolding proteins that cluster at synapses and are also called PSD (postsynaptic density)-95 proteins or SAPs (synapse-associated proteins). They play important roles in synaptic development and plasticity, cell polarity, migration and proliferation. They are members of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG-like proteins contain three PDZ domains and varying N-terminal regions. All DLG proteins exist as alternatively-spliced isoforms. Vertebrates contain four DLG proteins from different genes, called DLG1-4. DLG4 and DLG2 are found predominantly at postsynaptic sites and they mediate surface ion channel and receptor clustering. DLG3 is found axons and some presynaptic terminals. DLG1 interacts with AMPA-type glutamate receptors and is critical in their maturation and delivery to synapses. The SH3 domain of DLG4 binds and clusters the kainate subgroup of glutamate receptors via two proline-rich sequences in their C-terminal tail. It also binds AKAP79/150 (A-kinase anchoring protein). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212795 [Multi-domain]  Cd Length: 61  Bit Score: 63.88  E-value: 8.19e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620344 586 FVRAQFDYNPLDDELIPcaQAGISFQVGDILQIISKDDHHWWQARLDTVGGSA---GLIPS 643
Cdd:cd11861    1 YVRALFDYDPSRDSGLP--SQGLSFKFGDILHVTNASDDEWWQARRVTPNGEEeevGVIPS 59
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
7-282 8.87e-13

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 70.47  E-value: 8.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   7 LFDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVdvaKFTASPGLSTaDLKREATICHMLKHPHIVELLETYSSEGM 86
Cdd:cd06650    2 LKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLI---HLEIKPAIRN-QIIRELQVLHECNSPYIVGFYGAFYSDGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEGSDLCfEVVRRAvaGFVySEAVACHYMRQILEALRYCHE-NDILHRDVRPACALlatVDNSAPVKLGGFGS 165
Cdd:cd06650   78 ISICMEHMDGGSLD-QVLKKA--GRI-PEQILGKVSIAVIKGLTYLREkHKIMHRDVKPSNIL---VNSRGEIKLCDFGV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 166 AIQLPGTRetieTHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF---------LGSGVRLQQSVARGR 236
Cdd:cd06650  151 SGQLIDSM----ANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIpppdakeleLMFGCQVEGDAAETP 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 237 LS---------------------FE---------APEWKSI--SANAKDLVMKMLAANPHHRLSITEVLDHPWIRDRD 282
Cdd:cd06650  227 PRprtpgrplssygmdsrppmaiFElldyivnepPPKLPSGvfSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKRSD 304
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
5-306 1.14e-12

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 70.05  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   5 EILFDDVYElcevIGKGPFSIVRRCIHRESNQQFAVKivdvaKFTASPGLST---ADLKREATICHMLKHPHIVELLETY 81
Cdd:cd06634   14 EKLFSDLRE----IGHGSFGAVYFARDVRNNEVVAIK-----KMSYSGKQSNekwQDIIKEVKFLQKLRHPNTIEYRGCY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  82 SSEGMLYMVFEFMEGS--DLcFEVVRRAVagfvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVK 159
Cdd:cd06634   85 LREHTAWLVMEYCLGSasDL-LEVHKKPL-----QEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLT---EPGLVK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 160 LGGFGSA-IQLPGtretietHGRVGCPHYMAPEVV---TRRLYGKGCDVWGAGVMLhVLLSGRLP--FLGSGVRLQQSVA 233
Cdd:cd06634  156 LGDFGSAsIMAPA-------NSFVGTPYWMAPEVIlamDEGQYDGKVDVWSLGITC-IELAERKPplFNMNAMSALYHIA 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 234 RGrlsfEAPEWKS--ISANAKDLVMKMLAANPHHRLSITEVLDHPWI-RDR------DKLQRThlADTVEELKRYNARRK 304
Cdd:cd06634  228 QN----ESPALQSghWSEYFRNFVDSCLQKIPQDRPTSDVLLKHRFLlRERpptvimDLIQRT--KDAVRELDNLQYRKM 301

                 ..
gi 442620344 305 LK 306
Cdd:cd06634  302 KK 303
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
8-278 1.17e-12

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 69.70  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftaspglSTADLK---------REATICHMLKHPHIVELL 78
Cdd:cd14040    4 LNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNK-------SWRDEKkenyhkhacREYRIHKELDHPRIVKLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  79 ETYSSEGMLY-MVFEFMEGSDLCFEVVRRAVAgfvySEAVACHYMRQILEALRYCHE--NDILHRDVRPACALLATVDNS 155
Cdd:cd14040   77 DYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLM----SEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGTAC 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 156 APVKLGGFGSAIQLPGTRETIE----THGRVGCPHYMAPE--VVTRR--LYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR 227
Cdd:cd14040  153 GEIKITDFGLSKIMDDDSYGVDgmdlTSQGAGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQ 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442620344 228 ---LQQSVARGRLSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14040  233 qdiLQENTILKATEVQFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
61-278 1.34e-12

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 70.44  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  61 REATICHMLKHPHIVELLETYSSEGML------YMVFEFMEgSDLCfEVVRRAVagfvySEAVACHYMRQILEALRYCHE 134
Cdd:cd07876   69 RELVLLKCVNHKNIISLLNVFTPQKSLeefqdvYLVMELMD-ANLC-QVIHMEL-----DHERMSYLLYQMLCGIKHLHS 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 135 NDILHRDVRPACALlatVDNSAPVKLGGFGSAiQLPGTRETIETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVL 214
Cdd:cd07876  142 AGIIHRDLKPSNIV---VKSDCTLKILDFGLA-RTACTNFMMTPY--VVTRYYRAPEVILGMGYKENVDIWSVGCIMGEL 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 215 LSGRLPFLGSG--------------------VRLQQSV--------ARGRLSFEA--PEW---------KSISANAKDLV 255
Cdd:cd07876  216 VKGSVIFQGTDhidqwnkvieqlgtpsaefmNRLQPTVrnyvenrpQYPGISFEElfPDWifpseserdKLKTSQARDLL 295
                        250       260
                 ....*....|....*....|...
gi 442620344 256 MKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd07876  296 SKMLVIDPDKRISVDEALRHPYI 318
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
12-277 2.31e-12

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 69.28  E-value: 2.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCI-HRESNQQFAVKIV-DVAKFTASPGLSTADLKREATichmlKHPH----IVELLETYSSEG 85
Cdd:cd14215   14 YEIVSTLGEGTFGRVVQCIdHRRGGARVALKIIkNVEKYKEAARLEINVLEKINE-----KDPEnknlCVQMFDWFDYHG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 MLYMVFEFMEGSDLCFevvRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVD------------ 153
Cdd:cd14215   89 HMCISFELLGLSTFDF---LKENNYLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSDyeltynlekkrd 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 154 ----NSAPVKLGGFGSAIQLPGTRETIethgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVML-----------------H 212
Cdd:cd14215  166 ersvKSTAIRVVDFGSATFDHEHHSTI-----VSTRHYRAPEVILELGWSQPCDVWSIGCIIfeyyvgftlfqthdnreH 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 213 VLLSGRLpfLG-------SGVRLQQSVARGRLSFE--APEWKSISANAK-----------------DLVMKMLAANPHHR 266
Cdd:cd14215  241 LAMMERI--LGpipsrmiRKTRKQKYFYHGRLDWDenTSAGRYVRENCKplrryltseaeehhqlfDLIESMLEYEPSKR 318
                        330
                 ....*....|.
gi 442620344 267 LSITEVLDHPW 277
Cdd:cd14215  319 LTLAAALKHPF 329
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
18-221 2.67e-12

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 68.31  E-value: 2.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTAspglstadlkREATICHMLKHPHIVELLETYSsEGMLYMVF-EFMEG 96
Cdd:cd13991   14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRA----------EELMACAGLTSPRVVPLYGAVR-EGPWVNIFmDLKEG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  97 SDLCFEVVRRAVagfvYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLAtvDNSAPVKLGGFGSAIQL------- 169
Cdd:cd13991   83 GSLGQLIKEQGC----LPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLS--SDGSDAFLCDFGHAECLdpdglgk 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 170 --------PGTretiETHgrvgcphyMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF 221
Cdd:cd13991  157 slftgdyiPGT----ETH--------MAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
18-221 3.02e-12

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 67.67  E-value: 3.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHREsNQQFAVKIVdvakftASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd05112   12 IGSGQFGLVHLGYWLN-KDKVAIKTI------REGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 dlCFEVVRRAVAGFVYSEAVACHYMrQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLPGTRETiE 177
Cdd:cd05112   85 --CLSDYLRTQRGLFSAETLLGMCL-DVCEGMAYLEEASVIHRDLAARNCL---VGENQVVKVSDFGMTRFVLDDQYT-S 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 442620344 178 THGRVGCPHYMAPEVVTRRLYGKGCDVWGAGV-MLHVLLSGRLPF 221
Cdd:cd05112  158 STGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVlMWEVFSEGKIPY 202
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
8-278 3.47e-12

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 68.55  E-value: 3.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTADLK--REATICHMLKHPHIVELLETYSSEG 85
Cdd:cd14041    4 LNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHKHacREYRIHKELDHPRIVKLYDYFSLDT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 MLY-MVFEFMEGSDLCFEVVRRAVAgfvySEAVACHYMRQILEALRYCHE--NDILHRDVRPACALLATVDNSAPVKLGG 162
Cdd:cd14041   84 DSFcTVLEYCEGNDLDFYLKQHKLM----SEKEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLVNGTACGEIKITD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 163 FG-SAIQLPGTRETIE----THGRVGCPHYMAPE--VVTRR--LYGKGCDVWGAGVMLHVLLSGRLPFLGSGVR---LQQ 230
Cdd:cd14041  160 FGlSKIMDDDSYNSVDgmelTSQGAGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQqdiLQE 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 442620344 231 SVARGRLSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14041  240 NTILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
62-216 3.78e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 68.75  E-value: 3.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  62 EATICHMLKHPHIVELLETYSSEGMLYMVFEFMEgSDLCFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRD 141
Cdd:PHA03209 107 EAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYS-SDLYTYLTKRSRP---LPIDQALIIEKQILEGLRYLHAQRIIHRD 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 142 VRPACALLATVDNsapVKLGGFGSAiQLP-------GTRETIETHgrvgcphymAPEVVTRRLYGKGCDVWGAGVMLHVL 214
Cdd:PHA03209 183 VKTENIFINDVDQ---VCIGDLGAA-QFPvvapaflGLAGTVETN---------APEVLARDKYNSKADIWSAGIVLFEM 249

                 ..
gi 442620344 215 LS 216
Cdd:PHA03209 250 LA 251
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
8-278 4.55e-12

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 67.57  E-value: 4.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   8 FDDVYELCEVIGK-----GPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglstadlkrEATICHMLK-HPHIVELLETY 81
Cdd:PHA03390   9 LVQFLKNCEIVKKlklidGKFGKVSVLKHKPTQKLFVQKIIKAKNFNAI----------EPMVHQLMKdNPNFIKLYYSV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  82 SSEGMLYMVFEFMEGSDLcFEVVRRAVAgfvYSEAVACHYMRQILEALRYCHENDILHRDVRpacalLATV---DNSAPV 158
Cdd:PHA03390  79 TTLKGHVLIMDYIKDGDL-FDLLKKEGK---LSEAEVKKIIRQLVEALNDLHKHNIIHNDIK-----LENVlydRAKDRI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 159 KLGGFG--SAIQLPGTRE-TIEthgrvgcphYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPF-LGSGVRLQQSVAR 234
Cdd:PHA03390 150 YLCDYGlcKIIGTPSCYDgTLD---------YFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFkEDEDEELDLESLL 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 442620344 235 GRLSFEAPEWKSISANAKDLVMKMLAANPHHRL-SITEVLDHPWI 278
Cdd:PHA03390 221 KRQQKKLPFIKNVSKNANDFVQSMLKYNINYRLtNYNEIIKHPFL 265
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
492-574 6.53e-12

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 62.01  E-value: 6.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   492 RVRLVQFQKNTdEPMGITLKM--TEDGRCIVARIMHGGMIHRqATLHVGDEIREINGQPVQHQSVGQLQRMLREARGSVT 569
Cdd:smart00228   1 EPRLVELEKGG-GGLGFSLVGgkDEGGGVVVSSVVPGSPAAK-AGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVT 78

                   ....*
gi 442620344   570 FKIVP 574
Cdd:smart00228  79 LTVLR 83
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
10-250 8.34e-12

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 67.32  E-value: 8.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTadlkREATICHMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd07872    6 ETYIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAI----REVSLLKDLKHANIVTLHDIVHTDKSLTL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGS-----DLCfevvrravaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFG 164
Cdd:cd07872   82 VFEYLDKDlkqymDDC---------GNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLL---INERGELKLADFG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 --SAIQLPgtreTIETHGRVGCPHYMAPEVVT-RRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRLSFEA 241
Cdd:cd07872  150 laRAKSVP----TKTYSNEVVTLWYRPPDVLLgSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPT 225
                        250
                 ....*....|
gi 442620344 242 PE-WKSISAN 250
Cdd:cd07872  226 EEtWPGISSN 235
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
18-221 1.01e-11

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 66.75  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHREsnqqfavKIVDVAKFTASPGLSTADLKR----EATICHMLKHPHIVELLeTYSSEG-MLYMVFE 92
Cdd:cd14158   23 LGEGGFGVVFKGYIND-------KNVAVKKLAAMVDISTEDLTKqfeqEIQVMAKCQHENLVELL-GYSCDGpQLCLVYT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  93 FM-EGSDL----CFE----VVRRAVAGFVYSEAVACHYMrqilealrycHENDILHRDVRPACALLatvDNSAPVKLGGF 163
Cdd:cd14158   95 YMpNGSLLdrlaCLNdtppLSWHMRCKIAQGTANGINYL----------HENNHIHRDIKSANILL---DETFVPKISDF 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 164 GSAIQLPGTRETIETHGRVGCPHYMAPEVVTRRLYGKGcDVWGAGVMLHVLLSGRLPF 221
Cdd:cd14158  162 GLARASEKFSQTIMTERIVGTTAYMAPEALRGEITPKS-DIFSFGVVLLEIITGLPPV 218
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
12-266 1.02e-11

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 66.30  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHReSNQQFAVKIVdvakfTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05148    8 FTLERKLGSGYFGEVWEGLWK-NRVRVAIKIL-----KSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIIT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcfEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLpg 171
Cdd:cd05148   82 ELMEKGSL--LAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNIL---VGEDLVCKVADFGLARLI-- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 tRETIETHGRVGCPH-YMAPEVVTRRLYGKGCDVWGAGVMLHVLLS-GRLPFLGSGVR--LQQsVARGrlsFEAPEWKSI 247
Cdd:cd05148  155 -KEDVYLSSDKKIPYkWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHevYDQ-ITAG---YRMPCPAKC 229
                        250
                 ....*....|....*....
gi 442620344 248 SANAKDLVMKMLAANPHHR 266
Cdd:cd05148  230 PQEIYKIMLECWAAEPEDR 248
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
5-220 1.09e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 67.38  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   5 EILFDDVYELCEvIGKGPFSIVRRCIHRESNQQFAVKIVDVAkftASPGLSTaDLKREATICHMLKHPHIVELLETYSSE 84
Cdd:cd06649    1 ELKDDDFERISE-LGAGNGGVVTKVQHKPSGLIMARKLIHLE---IKPAIRN-QIIRELQVLHECNSPYIVGFYGAFYSD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  85 GMLYMVFEFMEGS--DLCFEVVRRAVAGFVYSEAVAchymrqILEALRYCHE-NDILHRDVRPACALlatVDNSAPVKLG 161
Cdd:cd06649   76 GEISICMEHMDGGslDQVLKEAKRIPEEILGKVSIA------VLRGLAYLREkHQIMHRDVKPSNIL---VNSRGEIKLC 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 162 GFGSAIQLPGTRetieTHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLP 220
Cdd:cd06649  147 DFGVSGQLIDSM----ANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYP 201
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
18-277 1.30e-11

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 67.00  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVdvakftASPGLSTADLKR---EATICHMLKHPHIVELLETYSSEGML------Y 88
Cdd:cd07878   23 VGSGAYGSVCSAYDTRLRQKVAVKKL------SRPFQSLIHARRtyrELRLLKHMKHENVIGLLDVFTPATSIenfnevY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMeGSDL-----CFEVVRRAVAGFVYseavachymrQILEALRYCHENDILHRDVRPACallATVDNSAPVKLGGF 163
Cdd:cd07878   97 LVTNLM-GADLnnivkCQKLSDEHVQFLIY----------QLLRGLKYIHSAGIIHRDLKPSN---VAVNEDCELRILDF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 164 GSAIQLPGtretiETHGRVGCPHYMAPEVVTRRL-YGKGCDVWGAGVMLHVLLSGRLPFLG------------------S 224
Cdd:cd07878  163 GLARQADD-----EMTGYVATRWYRAPEIMLNWMhYNQTVDIWSVGCIMAELLKGKALFPGndyidqlkrimevvgtpsP 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620344 225 GVRLQQSVARGRLSFEA------PEWKSI--SAN--AKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07878  238 EVLKKISSEHARKYIQSlphmpqQDLKKIfrGANplAIDLLEKMLVLDSDKRISASEALAHPY 300
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
12-235 1.37e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 67.56  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVkIVDVAKFTASPGlstadlkREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:PHA03207  94 YNILSSLTPGSEGEVFVCTKHGDEQRKKV-IVKAVTGGKTPG-------REIDILKTISHRAIINLIHAYRWKSTVCMVM 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEgSDLcfevvrravagFVYSEAV-------ACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFG 164
Cdd:PHA03207 166 PKYK-CDL-----------FTYVDRSgplpleqAITIQRRLLEALAYLHGRGIIHRDVKTENIFL---DEPENAVLGDFG 230
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620344 165 SAIQLPGTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARG 235
Cdd:PHA03207 231 AACKLDAHPDTPQCYGWSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTLFGKQVKSSSSQLRS 301
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
13-221 1.48e-11

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 65.77  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  13 ELCEVIGKGPFSIVRRCIHResNQQFAVKIVdvaKFTASPGLSTAdlkrEATICHMLKHPHIVELLETYSSE-GMLYMVF 91
Cdd:cd05082    9 KLLQTIGKGEFGDVMLGDYR--GNKVAVKCI---KNDATAQAFLA----EASVMTQLRHSNLVQLLGVIVEEkGGLYIVT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFM-EGSDLCFEVVR-RAVAGfvySEAVaCHYMRQILEALRYCHENDILHRDVrPACALLATVDNSApvKLGGFGSaiql 169
Cdd:cd05082   80 EYMaKGSLVDYLRSRgRSVLG---GDCL-LKFSLDVCEAMEYLEGNNFVHRDL-AARNVLVSEDNVA--KVSDFGL---- 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442620344 170 pgTRETIETHGRVGCP-HYMAPEVVTRRLYGKGCDVWGAGVMLHVLLS-GRLPF 221
Cdd:cd05082  149 --TKEASSTQDTGKLPvKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
87-280 1.48e-11

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 67.08  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEgSDLCFEVVRRA------VAGFVYseavachymrQILEALRYCHENDILHRDVRPACALlatVDNSAPVKL 160
Cdd:cd07853   79 IYVVTELMQ-SDLHKIIVSPQplssdhVKVFLY----------QILRGLKYLHSAGILHRDIKPGNLL---VNSNCVLKI 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 161 GGFGSAiQLPGTRETIETHGRVGCPHYMAPEVVT-RRLYGKGCDVWGAGVMLHVLLSGRLPF---------------LG- 223
Cdd:cd07853  145 CDFGLA-RVEEPDESKHMTQEVVTQYYRAPEILMgSRHYTSAVDIWSVGCIFAELLGRRILFqaqspiqqldlitdlLGt 223
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 224 ---SGVRLQQSVARGRLSFEAPEWKSISA----------NAKDLVMKMLAANPHHRLSITEVLDHPWIRD 280
Cdd:cd07853  224 pslEAMRSACEGARAHILRGPHKPPSLPVlytlssqathEAVHLLCRMLVFDPDKRISAADALAHPYLDE 293
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
586-643 1.69e-11

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 59.86  E-value: 1.69e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344   586 FVRAQFDYNP-LDDELipcaqagiSFQVGDILQIISKDDHHWWQARLDtvGGSAGLIPS 643
Cdd:smart00326   4 QVRALYDYTAqDPDEL--------SFKKGDIITVLEKSDDGWWKGRLG--RGKEGLFPS 52
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
12-267 2.38e-11

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 66.04  E-value: 2.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVD----------VAKFTASPGLSTAD----------LKREATICHMLKH 71
Cdd:cd13977    2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRcnapenvelaLREFWALSSIQRQHpnviqleecvLQRDGLAQRMSHG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  72 PHI----VELLET---------YSSEGMLYMVFEFMEGSDLCFEVVRRAVagfvySEAVACHYMRQILEALRYCHENDIL 138
Cdd:cd13977   82 SSKsdlyLLLVETslkgercfdPRSACYLWFVMEFCDGGDMNEYLLSRRP-----DRQTNTSFMLQLSSALAFLHRNQIV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 139 HRDVRPACALLATVDNSAPVKLGGFGSAIQLPGTRETIETHGRV---------GCPHYMAPEVVTRRlYGKGCDVWGAGV 209
Cdd:cd13977  157 HRDLKPDNILISHKRGEPILKVADFGLSKVCSGSGLNPEEPANVnkhflssacGSDFYMAPEVWEGH-YTAKADIFALGI 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344 210 MLHVLLSgRLPF---------LGSGV-RLQQSVARGRLSFEAPEWK---------SISANAKDLVMKMLAANPHHRL 267
Cdd:cd13977  236 IIWAMVE-RITFrdgetkkelLGTYIqQGKEIVPLGEALLENPKLElqiplkkkkSMNDDMKQLLRDMLAANPQERP 311
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
183-275 2.60e-11

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 65.50  E-value: 2.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 183 GCPHYMAPEVVTRRLY-GKGCDVWGAGVMLHVLLSGRLPFLGSgvrLQQSVARG--RLSFEAPEWKSISANAKDLVMKML 259
Cdd:cd13974  195 GSPAYISPDVLSGKPYlGKPSDMWALGVVLFTMLYGQFPFYDS---IPQELFRKikAAEYTIPEDGRVSENTVCLIRKLL 271
                         90
                 ....*....|....*.
gi 442620344 260 AANPHHRLSITEVLDH 275
Cdd:cd13974  272 VLNPQKRLTASEVLDS 287
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
12-277 3.18e-11

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 65.80  E-value: 3.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCI-HRESNQQFAVKIV-DVAKFTASPGLSTADLKR-------EATICHMLKhphivellETYS 82
Cdd:cd14214   15 YEIVGDLGEGTFGKVVECLdHARGKSQVALKIIrNVGKYREAARLEINVLKKikekdkeNKFLCVLMS--------DWFN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  83 SEGMLYMVFEFMEGSdlCFEVVRRAvaGFV-YSEAVACHYMRQILEALRYCHENDILHRDVRPACALLA----------- 150
Cdd:cd14214   87 FHGHMCIAFELLGKN--TFEFLKEN--NFQpYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVnsefdtlynes 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 151 ------TVDNSApVKLGGFGSAIQLPGTRETIethgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVML------------- 211
Cdd:cd14214  163 ksceekSVKNTS-IRVADFGSATFDHEHHTTI-----VATRHYRPPEVILELGWAQPCDVWSLGCILfeyyrgftlfqth 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 212 ----HVLLS----GRLP-FLGSGVRLQQSVARGRLSFE--APEWKSISANAK-----------------DLVMKMLAANP 263
Cdd:cd14214  237 enreHLVMMekilGPIPsHMIHRTRKQKYFYKGSLVWDenSSDGRYVSENCKplmsymlgdslehtqlfDLLRRMLEFDP 316
                        330
                 ....*....|....
gi 442620344 264 HHRLSITEVLDHPW 277
Cdd:cd14214  317 ALRITLKEALLHPF 330
gmk PRK14738
guanylate kinase; Provisional
714-886 3.60e-11

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 63.60  E-value: 3.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 714 LVLLGAHGVGRRHIKNTLISKYPDkYAYPIPHTTRPAKPEEENGRSYYFVSHDEMMADIGANEYLEYGTHEDAMYGTKLD 793
Cdd:PRK14738  16 VVISGPSGVGKDAVLARMRERKLP-FHFVVTATTRPKRPGEIDGVDYHFVTPEEFREMISQNELLEWAEVYGNYYGVPKA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 794 TIRRIHTEGKMAILDVEPQ-ALKILRTAeftPYVVFI--AAPSLQNIA---------DYDGSLERLAKESEMLRQLYGhf 861
Cdd:PRK14738  95 PVRQALASGRDVIVKVDVQgAASIKRLV---PEAVFIflAPPSMDELTrrlelrrteSPEELERRLATAPLELEQLPE-- 169
                        170       180       190
                 ....*....|....*....|....*....|.
gi 442620344 862 FDLTIVN--NDISETIATLETAID----RVH 886
Cdd:PRK14738 170 FDYVVVNpeDRLDEAVAQIMAIISaeksRVH 200
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
61-221 4.01e-11

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 64.05  E-value: 4.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  61 REATICHM--LKHPHIVELLETYSSEGMLYMVFEFMEGSDLcFEVVRravAGFVYSEAVACHYMRQILEALRYCHENDIL 138
Cdd:cd14059   28 KETDIKHLrkLNHPNIIKFKGVCTQAPCYCILMEYCPYGQL-YEVLR---AGREITPSLLVDWSKQIASGMNYLHLHKII 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 139 HRDVRPACALLATVDNsapVKLGGFGSAIQLPGTRETIETHGRVGcphYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGR 218
Cdd:cd14059  104 HRDLKSPNVLVTYNDV---LKISDFGTSKELSEKSTKMSFAGTVA---WMAPEVIRNEPCSEKVDIWSFGVVLWELLTGE 177

                 ...
gi 442620344 219 LPF 221
Cdd:cd14059  178 IPY 180
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
13-221 4.45e-11

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 65.01  E-value: 4.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  13 ELCEVIGKGPFSIVRRCIHR-ESNQQF-AVKIVDVAKftaspgLSTADLKR---EATICHMLKHPHIVELLETYSSEGML 87
Cdd:cd08216    1 ELLYEIGKCFKGGGVVHLAKhKPTNTLvAVKKINLES------DSKEDLKFlqqEILTSRQLQHPNILPYVTSFVVDNDL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  88 YMVFEFME-GSdlCFEVVRRA-VAGFvySEAVACHYMRQILEALRYCHENDILHRDVRpACALLATVDNSapVKLGGFGS 165
Cdd:cd08216   75 YVVTPLMAyGS--CRDLLKTHfPEGL--PELAIAFILRDVLNALEYIHSKGYIHRSVK-ASHILISGDGK--VVLSGLRY 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 166 AIQLpgtretIETHGRVGCPH-----------YMAPEVVTRRL--YGKGCDVWGAGVMLHVLLSGRLPF 221
Cdd:cd08216  148 AYSM------VKHGKRQRVVHdfpksseknlpWLSPEVLQQNLlgYNEKSDIYSVGITACELANGVVPF 210
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
18-221 4.92e-11

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 64.82  E-value: 4.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFtaspgLSTADL-KREATICHMLKHPHIVELL--ETYSSEGMLYMVFEFM 94
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSF-----MRPLDVqMREFEVLKKLNHKNIVKLFaiEEELTTRHKVLVMELC 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  95 EGSDLcFEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPV-KLGGFGSAIQLPGTR 173
Cdd:cd13988   76 PCGSL-YTVLEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVyKLTDFGAARELEDDE 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442620344 174 ETIETHGrvgCPHYMAPEVVTR--------RLYGKGCDVWGAGVMLHVLLSGRLPF 221
Cdd:cd13988  155 QFVSLYG---TEEYLHPDMYERavlrkdhqKKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
16-275 5.06e-11

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 64.61  E-value: 5.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftaSPGLSTadLKREATICHMLK-HPHIVELLETY--SSEGMLYMVF- 91
Cdd:cd14037    9 KYLAEGGFAHVYLVKTSNGGNRAALKRVYVND---EHDLNV--CKREIEIMKRLSgHKNIVGYIDSSanRSGNGVYEVLl 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 --EFMEGSDLCFEVVRRAVAGFVYSEAVacHYMRQILEALRYCHEND--ILHRDVRPACALLATVDNsapVKLGGFGSA- 166
Cdd:cd14037   84 lmEYCKGGGVIDLMNQRLQTGLTESEIL--KIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGN---YKLCDFGSAt 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 --IQLPGTR-------ETIETHGrvgCPHYMAPEVVTrrLY-GKG----CDVWGAGVMLHVLLSGRLPFLGSGVRLQQSV 232
Cdd:cd14037  159 tkILPPQTKqgvtyveEDIKKYT---TLQYRAPEMID--LYrGKPitekSDIWALGCLLYKLCFYTTPFEESGQLAILNG 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 442620344 233 argrlSFEAPEWKSISANAKDLVMKMLAANPHHRLSITEVLDH 275
Cdd:cd14037  234 -----NFTFPDNSRYSKRLHKLIRYMLEEDPEKRPNIYQVSYE 271
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
18-272 1.37e-10

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 62.75  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQqfavKIVDVAKFTASPGLSTADLK---REATICHMLKHPHIVELLETYSSEGMLyMVFEFM 94
Cdd:cd05060    3 LGHGNFGSVRKGVYLMKSG----KEVEVAVKTLKQEHEKAGKKeflREASVMAQLDHPCIVRLIGVCKGEPLM-LVMELA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  95 E-GSDLCFEVVRRAVagfvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFG--SAIQLPG 171
Cdd:cd05060   78 PlGPLLKYLKKRREI-----PVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQ---AKISDFGmsRALGAGS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHGRVGCPHYmAPEVVTRRLYGKGCDVWGAGVMLHVLLS-GRLPFLG-SGVRLQQSVARG-RLsfEAPEwkSIS 248
Cdd:cd05060  150 DYYRATTAGRWPLKWY-APECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGEmKGPEVIAMLESGeRL--PRPE--ECP 224
                        250       260
                 ....*....|....*....|....
gi 442620344 249 ANAKDLVMKMLAANPHHRLSITEV 272
Cdd:cd05060  225 QEIYSIMLSCWKYRPEDRPTFSEL 248
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
12-277 1.54e-10

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 63.13  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQF-AVKIVDVAkfTASPGLSTADLKREATICHM--LKHPHIVELLETYS-----S 83
Cdd:cd07862    3 YECVAEIGEGAYGKVFKARDLKNGGRFvALKRVRVQ--TGEEGMPLSTIREVAVLRHLetFEHPNVVRLFDVCTvsrtdR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGMLYMVFEFMEgSDLCFEVVRRAVAGfVYSEAVAcHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGF 163
Cdd:cd07862   81 ETKLTLVFEHVD-QDLTTYLDKVPEPG-VPTETIK-DMMFQLLRGLDFLHSHRVVHRDLKPQNIL---VTSSGQIKLADF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 164 GSA----IQLPGTRETIETHgrvgcphYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQ---------- 229
Cdd:cd07862  155 GLAriysFQMALTSVVVTLW-------YRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQlgkildvigl 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 230 -------QSVARGRLSFEAPEWKSISA-------NAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd07862  228 pgeedwpRDVALPRQAFHSKSAQPIEKfvtdideLGKDLLLKCLTFNPAKRISAYSALSHPY 289
SH3_DLG3 cd12029
Src Homology 3 domain of Disks Large homolog 3; DLG3, also called synapse-associated protein ...
585-648 1.78e-10

Src Homology 3 domain of Disks Large homolog 3; DLG3, also called synapse-associated protein 102 (SAP102), is a scaffolding protein that clusters at synapses and plays an important role in synaptic development and plasticity. Mutations in DLG3 cause midgestational embryonic lethality in mice and may be associated with nonsyndromic X-linked mental retardation in humans. It interacts with the NEDD4 (neural precursor cell-expressed developmentally downregulated 4) family of ubiquitin ligases and promotes apical tight junction formation. DLG3 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG3 contains three PDZ domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212962  Cd Length: 67  Bit Score: 57.40  E-value: 1.78e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344 585 IFVRAQFDYNPLDDELIPcaQAGISFQVGDILQIISKDDHHWWQARLDTVGGSA---GLIPSPELQE 648
Cdd:cd12029    3 LYVRALFDYDRTRDSCLP--SQGLSFSYGDILHVINASDDEWWQARLVTPHGESeqiGVIPSKKRVE 67
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
18-277 2.18e-10

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 62.43  E-value: 2.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSS----EGMLYMVFEF 93
Cdd:cd14031   18 LGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKA---EQQRFKEEAEMLKGLQHPNIVRFYDSWESvlkgKKCIVLVTEL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  94 MEGSDLCFEVVRRAVAgfvySEAVACHYMRQILEALRYCHEND--ILHRDVRpaCALLATVDNSAPVKLGGFGSAIQLpg 171
Cdd:cd14031   95 MTSGTLKTYLKRFKVM----KPKVLRSWCRQILKGLQFLHTRTppIIHRDLK--CDNIFITGPTGSVKIGDLGLATLM-- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 trETIETHGRVGCPHYMAPEVVTRRlYGKGCDVWGAGVMLHVLLSGRLPF--LGSGVRLQQSVARG--RLSFEapewKSI 247
Cdd:cd14031  167 --RTSFAKSVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEYPYseCQNAAQIYRKVTSGikPASFN----KVT 239
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 248 SANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14031  240 DPEVKEIIEGCIRQNKSERLSIKDLLNHAF 269
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
18-259 2.20e-10

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 62.34  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRcihRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVeLLETYSSEGMLYMVFEFMEGS 97
Cdd:cd14150    8 IGTGSFGTVFR---GKWHGDVAVKILKVTEPTPE---QLQAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQWCEGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLC---------FEVVRRA-VAgfvyseavachymRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAI 167
Cdd:cd14150   81 SLYrhlhvtetrFDTMQLIdVA-------------RQTAQGMDYLHAKNIIHRDLKSNNIFL---HEGLTVKIGDFGLAT 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 ---QLPGTRETIETHGRVgcpHYMAPEVVTRR---LYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQ--SVARGRLSf 239
Cdd:cd14150  145 vktRWSGSQQVEQPSGSI---LWMAPEVIRMQdtnPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQIifMVGRGYLS- 220
                        250       260
                 ....*....|....*....|
gi 442620344 240 eaPEWKSISANAKDLVMKML 259
Cdd:cd14150  221 --PDLSKLSSNCPKAMKRLL 238
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
61-278 2.76e-10

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 63.18  E-value: 2.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  61 REATICHMLKHPHIVELLETYSSEGML------YMVFEFMEgSDLCfEVVRRAVagfvySEAVACHYMRQILEALRYCHE 134
Cdd:cd07874   65 RELVLMKCVNHKNIISLLNVFTPQKSLeefqdvYLVMELMD-ANLC-QVIQMEL-----DHERMSYLLYQMLCGIKHLHS 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 135 NDILHRDVRPACALlatVDNSAPVKLGGFGSAiQLPGTRETIETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVL 214
Cdd:cd07874  138 AGIIHRDLKPSNIV---VKSDCTLKILDFGLA-RTAGTSFMMTPY--VVTRYYRAPEVILGMGYKENVDIWSVGCIMGEM 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 215 LSGRLPFLGSGVRLQQSVARGRLSFEAPEW---------------------------------------KSISANAKDLV 255
Cdd:cd07874  212 VRHKILFPGRDYIDQWNKVIEQLGTPCPEFmkklqptvrnyvenrpkyagltfpklfpdslfpadsehnKLKASQARDLL 291
                        250       260
                 ....*....|....*....|...
gi 442620344 256 MKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd07874  292 SKMLVIDPAKRISVDEALQHPYI 314
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
18-211 2.89e-10

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 62.67  E-value: 2.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRC----IHRESNQQFAVKIVDVAKFTASPGlSTADLKREATICHML-KHPHIVELLETYSSEGMLYMVFE 92
Cdd:cd05099   20 LGEGCFGQVVRAeaygIDKSRPDQTVTVAVKMLKDNATDK-DLADLISEMELMKLIgKHKNIINLLGVCTQEGPLYVIVE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  93 FME--------------GSDLCFEVVRRAVAGFVYSEAVACHYmrQILEALRYCHENDILHRDVrPACALLATVDNSapV 158
Cdd:cd05099   99 YAAkgnlreflrarrppGPDYTFDITKVPEEQLSFKDLVSCAY--QVARGMEYLESRRCIHRDL-AARNVLVTEDNV--M 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442620344 159 KLGGFGSAI---QLPGTRETieTHGRVGCpHYMAPEVVTRRLYGKGCDVWGAGVML 211
Cdd:cd05099  174 KIADFGLARgvhDIDYYKKT--SNGRLPV-KWMAPEALFDRVYTHQSDVWSFGILM 226
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
18-211 3.19e-10

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 61.90  E-value: 3.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKivDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMK--ELIRFDEE---TQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLcFEVVRRAVAGFVYSEAVAchYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLPGTRETIE 177
Cdd:cd14221   76 TL-RGIIKSMDSHYPWSQRVS--FAKDIASGMAYLHSMNIIHRDLNSHNCL---VRENKSVVVADFGLARLMVDEKTQPE 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 442620344 178 THGR------------VGCPHYMAPEVVTRRLYGKGCDVWGAGVML 211
Cdd:cd14221  150 GLRSlkkpdrkkrytvVGNPYWMAPEMINGRSYDEKVDVFSFGIVL 195
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
10-274 3.46e-10

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 61.98  E-value: 3.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHRESNQqfavkivdVAKFTASPG-LSTADLKREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd05072    7 ESIKLVKKLGAGQFGEVWMGYYNNSTK--------VAVKTLKPGtMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFM-EGSDLCFevvRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAI 167
Cdd:cd05072   79 IITEYMaKGSLLDF---LKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVL---VSESLMCKIADFGLAR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLpgtrETIETHGRVGCP---HYMAPEVVTRRLYGKGCDVWGAGVMLHVLLS-GRLPFLG-SGVRLQQSVARGrlsFEAP 242
Cdd:cd05072  153 VI----EDNEYTAREGAKfpiKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGmSNSDVMSALQRG---YRMP 225
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442620344 243 EWKSISANAKDLVMKMLAANPHHRLS---ITEVLD 274
Cdd:cd05072  226 RMENCPDELYDIMKTCWKEKAEERPTfdyLQSVLD 260
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
16-274 3.47e-10

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 61.69  E-value: 3.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQQFAVKivdVAKFTASPglstaDLKR----EATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05041    1 EKIGRGNFGDVYRGVLKPDNTEVAVK---TCRETLPP-----DLKRkflqEARILKQYDHPNIVKLIGVCVQKQPIMIVM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLC---------------FEVVRRAVAGFVYSEAVAChymrqilealrychendiLHRDVrPACALLATVDNSa 156
Cdd:cd05041   73 ELVPGGSLLtflrkkgarltvkqlLQMCLDAAAGMEYLESKNC------------------IHRDL-AARNCLVGENNV- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 157 pVKLGGFGSAIQLPGTrETIETHGRVGCP-HYMAPEVVTRRLYGKGCDVWGAGVMLHVLLS-GRLPFLG-SGVRLQQSVA 233
Cdd:cd05041  133 -LKISDFGMSREEEDG-EYTVSDGLKQIPiKWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPYPGmSNQQTREQIE 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 442620344 234 RG-RLSfeAPEwkSISANAKDLVMKMLAANPHHRLSITEVLD 274
Cdd:cd05041  211 SGyRMP--APE--LCPEAVYRLMLQCWAYDPENRPSFSEIYN 248
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
12-220 3.60e-10

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 61.50  E-value: 3.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVdvAKFTASPGLS--TADLKReatichMLKHPHIVELLETYSSEGMLYM 89
Cdd:cd14017    2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVE--SKSQPKQVLKmeVAVLKK------LQGKPHFCRLIGCGRTERYNYI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VfefME--GSDLcfEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPA-CALLATVDNSAPVKLGGFGSA 166
Cdd:cd14017   74 V---MTllGPNL--AELRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSnFAIGRGPSDERTVYILDFGLA 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 167 IQL-----PGTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLP 220
Cdd:cd14017  149 RQYtnkdgEVERPPRNAAGFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLP 207
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
12-278 3.90e-10

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 62.41  E-value: 3.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIV-DVAKF--TASPGLSTADL--KREATICHmlkhpHIVELLETYSSEGM 86
Cdd:cd14225   45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIrNKKRFhhQALVEVKILDAlrRKDRDNSH-----NVIHMKEYFYFRNH 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMeGSDLcFEVVRR-AVAGFvySEAVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSApVKLGGFGS 165
Cdd:cd14225  120 LCITFELL-GMNL-YELIKKnNFQGF--SLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQSS-IKVIDFGS 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 166 AIQlpgTRETIETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG----------------VRLQ 229
Cdd:cd14225  195 SCY---EHQRVYTY--IQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENeveqlacimevlglppPELI 269
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 230 QSVARGRLSFEA----------------PEWKSISANAK-------DLVMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14225  270 ENAQRRRLFFDSkgnprcitnskgkkrrPNSKDLASALKtsdplflDFIRRCLEWDPSKRMTPDEALQHEWI 341
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
586-643 4.53e-10

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 55.93  E-value: 4.53e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 586 FVRAQFDYNP-LDDELipcaqagiSFQVGDILQIISKDDHHWWQARLDtvGGSAGLIPS 643
Cdd:cd00174    1 YARALYDYEAqDDDEL--------SFKKGDIITVLEKDDDGWWEGELN--GGREGLFPA 49
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
7-224 4.64e-10

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 62.34  E-value: 4.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   7 LFDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAKftasPGLSTADLkrEATICHML-KHP-----HIVELLET 80
Cdd:cd14226   10 KWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKK----AFLNQAQI--EVRLLELMnKHDtenkyYIVRLKRH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  81 YSSEGMLYMVFEFMEGS--DLCFEVVRRAVagfvySEAVACHYMRQILEALRYCHEND--ILHRDVRPACALLATVDNSA 156
Cdd:cd14226   84 FMFRNHLCLVFELLSYNlyDLLRNTNFRGV-----SLNLTRKFAQQLCTALLFLSTPElsIIHCDLKPENILLCNPKRSA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 157 pVKLGGFGSAIQLpGTR--ETIETHgrvgcpHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGS 224
Cdd:cd14226  159 -IKIIDFGSSCQL-GQRiyQYIQSR------FYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGA 220
L27 pfam02828
L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.
347-396 4.76e-10

L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.


Pssm-ID: 460717  Cd Length: 52  Bit Score: 55.89  E-value: 4.76e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 442620344  347 VQRILDCLDDIYSLQDAHVDADVLRDMLRDNRLHQFLQLFDRIAATVVTS 396
Cdd:pfam02828   1 VELVLELLEDLQPLSEASEDLAELQKLLQSPHLQALLEAHDKVAQKVYEP 50
SH3_DLG1 cd12031
Src Homology 3 domain of Disks Large homolog 1; DLG1, also called synapse-associated protein ...
585-643 5.54e-10

Src Homology 3 domain of Disks Large homolog 1; DLG1, also called synapse-associated protein 97 (SAP97), is a scaffolding protein that clusters at synapses and plays an important role in synaptic development and plasticity. DLG1 plays roles in regulating cell polarity, proliferation, migration, and cycle progression. It interacts with AMPA-type glutamate receptors and is critical in their maturation and delivery to synapses. It also interacts with PKCalpha and promotes wound healing. DLG1 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG1 contains three PDZ domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212964  Cd Length: 67  Bit Score: 56.24  E-value: 5.54e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 585 IFVRAQFDYNPLDDELIPcaQAGISFQVGDILQIISKDDHHWWQARLDTVGGSA---GLIPS 643
Cdd:cd12031    3 LYVRALFDYDKTKDSGLP--SQGLNFKFGDILHVVNASDDEWWQARQVTADGESeeiGVIPS 62
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
7-278 5.58e-10

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 61.82  E-value: 5.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   7 LFDDVYELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAK-FTAspglsTA-D----LK--REATICHMLKHpHIVELL 78
Cdd:cd14136    7 VYNGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQhYTE-----AAlDeiklLKcvREADPKDPGRE-HVVQLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  79 ETYSSEGM----LYMVFEFMeGSDLCFEVVRRAVAGfVYSEAVAChYMRQILEALRYCHEN-DILHRDVRPACALLATVD 153
Cdd:cd14136   81 DDFKHTGPngthVCMVFEVL-GPNLLKLIKRYNYRG-IPLPLVKK-IARQVLQGLDYLHTKcGIIHTDIKPENVLLCISK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 154 nsAPVKLGGFGSA----------IQlpgTREtiethgrvgcphYMAPEVVTRRLYGKGCDVWGAGVML------------ 211
Cdd:cd14136  158 --IEVKIADLGNAcwtdkhftedIQ---TRQ------------YRSPEVILGAGYGTPADIWSTACMAfelatgdylfdp 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 212 -----------HVL----LSGRLP--FLGSG----------------VRLQ----QSVARGRLSFEAPEWKSISanakDL 254
Cdd:cd14136  221 hsgedysrdedHLAliieLLGRIPrsIILSGkysreffnrkgelrhiSKLKpwplEDVLVEKYKWSKEEAKEFA----SF 296
                        330       340
                 ....*....|....*....|....
gi 442620344 255 VMKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd14136  297 LLPMLEYDPEKRATAAQCLQHPWL 320
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
18-260 5.72e-10

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 61.23  E-value: 5.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRcihRESNQQFAVKIVDVakfTASPGLSTADLKREATICHMLKHPHIVeLLETYSSEGMLYMVFEFMEGS 97
Cdd:cd14151   16 IGSGSFGTVYK---GKWHGDVAVKMLNV---TAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLcFEVVRRAVAGFVYSEAVacHYMRQILEALRYCHENDILHRDVRPACALLATvDNSapVKLGGFGSAI---QLPGTRE 174
Cdd:cd14151   89 SL-YHHLHIIETKFEMIKLI--DIARQTAQGMDYLHAKSIIHRDLKSNNIFLHE-DLT--VKIGDFGLATvksRWSGSHQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 175 TIETHGRVgcpHYMAPEVV---TRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQ--QSVARGRLSfeaPEWKSISA 249
Cdd:cd14151  163 FEQLSGSI---LWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQiiFMVGRGYLS---PDLSKVRS 236
                        250
                 ....*....|.
gi 442620344 250 NAKDLVMKMLA 260
Cdd:cd14151  237 NCPKAMKRLMA 247
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
18-215 7.06e-10

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 60.98  E-value: 7.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASPGLSTAdlkREATICHMLKHPHIVELLETYSS--EGMLYMVFEFME 95
Cdd:cd14049   14 LGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVL---REVKVLAGLQHPNIVGYHTAWMEhvQLMLYIQMQLCE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 GS----------DLCFEVVRRAVAGFVYSEaVACHYMRQILEALRYCHENDILHRDVRPACALLATVDNSapVKLGGFG- 164
Cdd:cd14049   91 LSlwdwivernkRPCEEEFKSAPYTPVDVD-VTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDIH--VRIGDFGl 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 165 --------SAIQLPGTRETIETHG-RVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLL 215
Cdd:cd14049  168 acpdilqdGNDSTTMSRLNGLTHTsGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF 227
SH3_CRK_N cd11758
N-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins; CRK adaptor ...
585-648 7.39e-10

N-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins; CRK adaptor proteins consists of SH2 and SH3 domains, which bind tyrosine-phosphorylated peptides and proline-rich motifs, respectively. They function downstream of protein tyrosine kinases in many signaling pathways started by various extracellular signals, including growth and differentiation factors. Cellular CRK (c-CRK) contains a single SH2 domain, followed by N-terminal and C-terminal SH3 domains. It is involved in the regulation of many cellular processes including cell growth, motility, adhesion, and apoptosis. CRK has been implicated in the malignancy of various human cancers. The N-terminal SH3 domain of CRK binds a number of target proteins including DOCK180, C3G, SOS, and cABL. The CRK family includes two alternatively spliced protein forms, CRKI and CRKII, that are expressed by the CRK gene, and the CRK-like (CRKL) protein, which is expressed by a distinct gene (CRKL). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212692 [Multi-domain]  Cd Length: 55  Bit Score: 55.45  E-value: 7.39e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620344 585 IFVRAQFDYNPLDDELIPcaqagisFQVGDILQIISKDDHHWWQARLDTvgGSAGLIPSPELQE 648
Cdd:cd11758    1 EYVRALFDFPGNDDEDLP-------FKKGEILTVIRKPEEQWWNARNSE--GKTGMIPVPYVEK 55
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
16-216 9.35e-10

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 60.80  E-value: 9.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHrESNQQFAVKIVDVAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGM--LYMVFEF 93
Cdd:cd14205   10 QQLGKGNFGSVEMCRY-DPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRrnLRLIMEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  94 MEGSDLcFEVVRRAVAGFVYSEAVacHYMRQILEALRYCHENDILHRDvrpacalLAT----VDNSAPVKLGGFGSAIQL 169
Cdd:cd14205   89 LPYGSL-RDYLQKHKERIDHIKLL--QYTSQICKGMEYLGTKRYIHRD-------LATrnilVENENRVKIGDFGLTKVL 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 442620344 170 PGTRETIETHGRVGCP-HYMAPEVVTRRLYGKGCDVWGAGVMLHVLLS 216
Cdd:cd14205  159 PQDKEYYKVKEPGESPiFWYAPESLTESKFSVASDVWSFGVVLYELFT 206
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
348-397 9.71e-10

domain in receptor targeting proteins Lin-2 and Lin-7;


Pssm-ID: 197794  Cd Length: 53  Bit Score: 54.82  E-value: 9.71e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 442620344   348 QRILDCLDDIYSLQDAHVDADVLRDMLRDNRLHQFLQLFDRIAATVVTSN 397
Cdd:smart00569   1 QRLLELLEELQSLLSPSEDLQELRRLLQSPHLQALLKIHDKVAETELDPP 50
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
12-282 1.05e-09

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 61.59  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKivdvaKFTASPGLSTadlkREATICHMLKHPHIVELLETYSSEGM----- 86
Cdd:PTZ00036  68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIK-----KVLQDPQYKN----RELLIMKNLNHINIIFLKDYYYTECFkknek 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 ---LYMVFEFMEgsdlcfEVVRRAVAGFVYSEA-----VACHYMRQILEALRYCHENDILHRDVRPACALLATvdNSAPV 158
Cdd:PTZ00036 139 nifLNVVMEFIP------QTVHKYMKHYARNNHalplfLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDP--NTHTL 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 159 KLGGFGSAIQLPGTRETIEThgrVGCPHYMAPEVVTRRL-YGKGCDVWGAGVMLHVLLSGRLPFLGSG-----VRLQQSV 232
Cdd:PTZ00036 211 KLCDFGSAKNLLAGQRSVSY---ICSRFYRAPELMLGATnYTTHIDLWSLGCIIAEMILGYPIFSGQSsvdqlVRIIQVL 287
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 233 A---RGRLSFEAPEW------------------KSISANAKDLVMKMLAANPHHRLSITEVLDHPWIRD-RD 282
Cdd:PTZ00036 288 GtptEDQLKEMNPNYadikfpdvkpkdlkkvfpKGTPDDAINFISQFLKYEPLKRLNPIEALADPFFDDlRD 359
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
57-272 1.37e-09

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 59.82  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  57 ADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGSDLcFEVVRRAVAGFvyseAVACHYMRQILEALRYCHEND 136
Cdd:cd14027   36 EALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNL-MHVLKKVSVPL----SVKGRIILEIIEGMAYLHGKG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 137 ILHRDVRPACALlatVDNSAPVKLGGFGSAIQLPGTRETIETHGR-----------VGCPHYMAPEVVtRRLYGKGC--- 202
Cdd:cd14027  111 VIHKDLKPENIL---VDNDFHIKIADLGLASFKMWSKLTKEEHNEqrevdgtakknAGTLYYMAPEHL-NDVNAKPTeks 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620344 203 DVWGAGVMLHVLLSGRLPFlgSGVRLQQSVARGRLSFEAPEWKSISAN----AKDLVMKMLAANPHHRLSITEV 272
Cdd:cd14027  187 DVYSFAIVLWAIFANKEPY--ENAINEDQIIMCIKSGNRPDVDDITEYcpreIIDLMKLCWEANPEARPTFPGI 258
SH3_DLG2 cd12032
Src Homology 3 domain of Disks Large homolog 2; DLG2, also called postsynaptic density-93 ...
585-643 1.44e-09

Src Homology 3 domain of Disks Large homolog 2; DLG2, also called postsynaptic density-93 (PSD93) or Channel-associated protein of synapse-110 (chapsyn 110), is a scaffolding protein that clusters at synapses and plays an important role in synaptic development and plasticity. The DLG2 delta isoform binds inwardly rectifying potassium Kir2 channels, which determine resting membrane potential in neurons. It regulates the spatial and temporal distribution of Kir2 channels within neuronal membranes. DLG2 is a member of the MAGUK (membrane-associated guanylate kinase) protein family, which is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain. DLG2 contains three PDZ domains. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212965  Cd Length: 74  Bit Score: 55.09  E-value: 1.44e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 585 IFVRAQFDYNPLDDELIPcaQAGISFQVGDILQIISKDDHHWWQARLDTVGGSA---GLIPS 643
Cdd:cd12032    6 LYVRAMFDYEKSKDSGLP--SQGLSFRYGDILHVINASDDEWWQARRVTPDGDSeemGVIPS 65
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
16-211 1.48e-09

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 60.37  E-value: 1.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRC-------IHRESNQQFAVKIVDVA-KFTASPGLSTA--DLKREATICHMLKHPHIVELLETYSSEG 85
Cdd:cd05097   11 EKLGEGQFGEVHLCeaeglaeFLGEGAPEFDGQPVLVAvKMLRADVTKTArnDFLKEIKIMSRLKNPNIIRLLGVCVSDD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  86 MLYMVFEFMEGSDLCFEVVRRAV-AGFVYSEAVAC-------HYMRQILEALRYCHENDILHRDVRPACALlatVDNSAP 157
Cdd:cd05097   91 PLCMITEYMENGDLNQFLSQREIeSTFTHANNIPSvsianllYMAVQIASGMKYLASLNFVHRDLATRNCL---VGNHYT 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442620344 158 VKLGGFGSAIQLPgTRETIETHGRVGCP-HYMAPEVVTRRLYGKGCDVWGAGVML 211
Cdd:cd05097  168 IKIADFGMSRNLY-SGDYYRIQGRAVLPiRWMAWESILLGKFTTASDVWAFGVTL 221
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
59-280 1.50e-09

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 60.03  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  59 LKREATicHM--LKHPHIVELLETY-SSEGMLYMVFEFMEGSdlCFEVVRRAV---------AGFVYSEAVACHYMRQIL 126
Cdd:cd14011   49 LKRGVK--QLtrLRHPRILTVQHPLeESRESLAFATEPVFAS--LANVLGERDnmpspppelQDYKLYDVEIKYGLLQIS 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 127 EALRYCHEN-DILHRDVRPAcallATVDNSAPV-KLGGFGSAIQLPGTR--ETIETHGRVGCPH-------YMAPEVVTR 195
Cdd:cd14011  125 EALSFLHNDvKLVHGNICPE----SVVINSNGEwKLAGFDFCISSEQATdqFPYFREYDPNLPPlaqpnlnYLAPEYILS 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 196 RLYGKGCDVWGAGVMLHVLLS-GRLPFlgsGVRLQQSVARGRLS----FEAPEWKSISANAKDLVMKMLAANPHHRLSIT 270
Cdd:cd14011  201 KTCDPASDMFSLGVLIYAIYNkGKPLF---DCVNNLLSYKKNSNqlrqLSLSLLEKVPEELRDHVKTLLNVTPEVRPDAE 277
                        250
                 ....*....|
gi 442620344 271 EVLDHPWIRD 280
Cdd:cd14011  278 QLSKIPFFDD 287
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
18-235 1.66e-09

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 59.38  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESnqqfavkiVDVAKFTASPG-LSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEG 96
Cdd:cd05059   12 LGSGQFGVVHLGKWRGK--------IDVAIKMIKEGsMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMAN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  97 SdlCFEVVRRAVAGFVYSEAV--AChymRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSA-------- 166
Cdd:cd05059   84 G--CLLNYLRERRGKFQTEQLleMC---KDVCEAMEYLESNGFIHRDLAARNCL---VGEQNVVKVSDFGLAryvlddey 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620344 167 IQLPGTRETIEthgrvgcphYMAPEVVTRRLYGKGCDVWGAGV-MLHVLLSGRLPFLG-SGVRLQQSVARG 235
Cdd:cd05059  156 TSSVGTKFPVK---------WSPPEVFMYSKFSSKSDVWSFGVlMWEVFSEGKMPYERfSNSEVVEHISQG 217
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
12-144 1.89e-09

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 59.39  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIvdVAKFTASPGlstadLKREATICHMLK-HPHIVELLETYSSEGMLYMV 90
Cdd:cd14016    2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKI--EKKDSKHPQ-----LEYEAKVYKLLQgGPGIPRLYWFGQEGDYNVMV 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442620344  91 FEFMeGSDLcfEVVRRAVaGFVYSEAVACHYMRQILEALRYCHENDILHRDVRP 144
Cdd:cd14016   75 MDLL-GPSL--EDLFNKC-GRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKP 124
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
61-278 2.04e-09

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 60.44  E-value: 2.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  61 REATICHMLKHPHIVELLETYSSEGML------YMVFEFMEgSDLCfEVVRRAVagfvySEAVACHYMRQILEALRYCHE 134
Cdd:cd07875   72 RELVLMKCVNHKNIIGLLNVFTPQKSLeefqdvYIVMELMD-ANLC-QVIQMEL-----DHERMSYLLYQMLCGIKHLHS 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 135 NDILHRDVRPACALlatVDNSAPVKLGGFGSAiQLPGTRETIETHgrVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVL 214
Cdd:cd07875  145 AGIIHRDLKPSNIV---VKSDCTLKILDFGLA-RTAGTSFMMTPY--VVTRYYRAPEVILGMGYKENVDIWSVGCIMGEM 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 215 LSGRLPFLGSGVRLQQSVARGRLSFEAPEW---------------------------------------KSISANAKDLV 255
Cdd:cd07875  219 IKGGVLFPGTDHIDQWNKVIEQLGTPCPEFmkklqptvrtyvenrpkyagysfeklfpdvlfpadsehnKLKASQARDLL 298
                        250       260
                 ....*....|....*....|...
gi 442620344 256 MKMLAANPHHRLSITEVLDHPWI 278
Cdd:cd07875  299 SKMLVIDASKRISVDEALQHPYI 321
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
29-211 2.06e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 61.06  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  29 CIHRESNQQFAVKIVDVAKFTASPglstadlKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEgSDLCFEVVRRAV 108
Cdd:PHA03211 184 CVFESSHPDYPQRVVVKAGWYASS-------VHEARLLRRLSHPAVLALLDVRVVGGLTCLVLPKYR-SDLYTYLGARLR 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 109 A-GFVYSEAVAchymRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSAIQLPGTRETIETHGRVGCPHY 187
Cdd:PHA03211 256 PlGLAQVTAVA----RQLLSAIDYIHGEGIIHRDIKTENVLVNGPED---ICLGDFGAACFARGSWSTPFHYGIAGTVDT 328
                        170       180
                 ....*....|....*....|....
gi 442620344 188 MAPEVVTRRLYGKGCDVWGAGVML 211
Cdd:PHA03211 329 NAPEVLAGDPYTPSVDIWSAGLVI 352
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
58-272 2.23e-09

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 59.59  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  58 DLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGSDLCFEVVRRAVAGFVY--SEAVAC---------HYMRQIL 126
Cdd:cd05092   53 DFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMRHGDLNRFLRSHGPDAKILdgGEGQAPgqltlgqmlQIASQIA 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 127 EALRYCHENDILHRDvrpacalLAT----VDNSAPVKLGGFGSAIQLPGTrETIETHGRVGCP-HYMAPEVVTRRLYGKG 201
Cdd:cd05092  133 SGMVYLASLHFVHRD-------LATrnclVGQGLVVKIGDFGMSRDIYST-DYYRVGGRTMLPiRWMPPESILYRKFTTE 204
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620344 202 CDVWGAGVML-HVLLSGRLPFLG-SGVRLQQSVARGRlSFEAPewKSISANAKDLVMKMLAANPHHRLSITEV 272
Cdd:cd05092  205 SDIWSFGVVLwEIFTYGKQPWYQlSNTEAIECITQGR-ELERP--RTCPPEVYAIMQGCWQREPQQRHSIKDI 274
L27 pfam02828
L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.
406-462 2.42e-09

L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.


Pssm-ID: 460717  Cd Length: 52  Bit Score: 53.58  E-value: 2.42e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344  406 VGRCRDVLEQLSSTSGGNSlggkyAKEELMRLLAAPHMQALLHSHDVVARDVYGEEA 462
Cdd:pfam02828   1 VELVLELLEDLQPLSEASE-----DLAELQKLLQSPHLQALLEAHDKVAQKVYEPPS 52
SH3_CACNB cd11863
Src Homology 3 domain of Voltage-dependent L-type calcium channel subunit beta; ...
587-644 2.45e-09

Src Homology 3 domain of Voltage-dependent L-type calcium channel subunit beta; Voltage-dependent calcium channels (Ca(V)s) are multi-protein complexes that regulate the entry of calcium into cells. They impact muscle contraction, neuronal migration, hormone and neurotransmitter release, and the activation of calcium-dependent signaling pathways. They are composed of four subunits: alpha1, alpha2delta, beta, and gamma. The beta subunit is a soluble and intracellular protein that interacts with the transmembrane alpha1 subunit. It facilitates the trafficking and proper localization of the alpha1 subunit to the cellular plasma membrane. Vertebrates contain four different beta subunits from distinct genes (beta1-4); each exists as multiple splice variants. All are expressed in the brain while other tissues show more specific expression patterns. The beta subunits show similarity to MAGUK (membrane-associated guanylate kinase) proteins in that they contain SH3 and inactive guanylate kinase (GuK) domains; however, they do not appear to contain a PDZ domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212797 [Multi-domain]  Cd Length: 62  Bit Score: 54.21  E-value: 2.45e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 587 VRAQFDYNPLDDELIPCAQAGISFQVGDILQIISKDDHHWWQARLDTVGGSAGLIPSP 644
Cdd:cd11863    3 VRTNVGYDGSLDDDSPVPGYAVSFEAKDFLHIKEKYNNDWWIGRLVKEGCDIGFIPSP 60
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
18-216 2.57e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 59.32  E-value: 2.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHR-ESNQQFAVKIVDVAKfTASPGLSTADLKREATICHMLKHPHIVELleTYSSEGM----LYMVFE 92
Cdd:cd05038   12 LGEGHFGSVELCRYDpLGDNTGEQVAVKSLQ-PSGEEQHMSDFKREIEILRTLDHEYIVKY--KGVCESPgrrsLRLIME 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  93 FMEGSDLcFEVVRRAVAGFVYSEAVAchYMRQILEALRYCHENDILHRDvrpacalLAT----VDNSAPVKLGGFGSAIQ 168
Cdd:cd05038   89 YLPSGSL-RDYLQRHRDQIDLKRLLL--FASQICKGMEYLGSQRYIHRD-------LAArnilVESEDLVKISDFGLAKV 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442620344 169 LPGTREtietHGRVGCP-----HYMAPEVV-TRRLYGKGcDVWGAGVMLHVLLS 216
Cdd:cd05038  159 LPEDKE----YYYVKEPgespiFWYAPECLrESRFSSAS-DVWSFGVTLYELFT 207
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
41-235 2.66e-09

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 58.83  E-value: 2.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  41 KIVDVAKFTASPG-LSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFME-GSDLCFevvRRAVAGFVYSEAVA 118
Cdd:cd05034   18 GTTKVAVKTLKPGtMSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSkGSLLDY---LRTGEGRALRLPQL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 119 CHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSA------IQLP--GTRETIEthgrvgcphYMAP 190
Cdd:cd05034   95 IDMAAQIASGMAYLESRNYIHRDLAARNIL---VGENNVCKVADFGLArlieddEYTAreGAKFPIK---------WTAP 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 442620344 191 EVVTRRLYGKGCDVWGAGVMLHVLLS-GRLPFLGSGVR--LQQsVARG 235
Cdd:cd05034  163 EAALYGRFTIKSDVWSFGILLYEIVTyGRVPYPGMTNRevLEQ-VERG 209
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
408-458 2.99e-09

domain in receptor targeting proteins Lin-2 and Lin-7;


Pssm-ID: 197794  Cd Length: 53  Bit Score: 53.67  E-value: 2.99e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 442620344   408 RCRDVLEQLSSTSGGNSLggkyaKEELMRLLAAPHMQALLHSHDVVARDVY 458
Cdd:smart00569   2 RLLELLEELQSLLSPSED-----LQELRRLLQSPHLQALLKIHDKVAETEL 47
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
588-643 3.37e-09

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 53.36  E-value: 3.37e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344  588 RAQFDYNPLD-DELipcaqagiSFQVGDILQIISKDDHHWWQARLDtvGGSAGLIPS 643
Cdd:pfam00018   1 VALYDYTAQEpDEL--------SFKKGDIIIVLEKSEDGWWKGRNK--GGKEGLIPS 47
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
5-223 4.28e-09

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 58.59  E-value: 4.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   5 EILFDDVyELCEVIGKGPFSIVRRCI-HRESNQQFAVKiVDVAKFTASPGLSTADLKrEATICHMLKHPHIVELLETYSS 83
Cdd:cd05056    2 EIQREDI-TLGRCIGEGQFGDVYQGVyMSPENEKIAVA-VKTCKNCTSPSVREKFLQ-EAYIMRQFDHPHIVKLIGVITE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGMlYMVFEFMEGSDLcfevvRRAVAGFVYSEAVA--CHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLG 161
Cdd:cd05056   79 NPV-WIVMELAPLGEL-----RSYLQVNKYSLDLAslILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDC---VKLG 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620344 162 GFGSAIQLpgTRETIETHGRVGCP-HYMAPEVVTRRLYGKGCDVWGAGV-MLHVLLSGRLPFLG 223
Cdd:cd05056  150 DFGLSRYM--EDESYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVcMWEILMLGVKPFQG 211
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
17-274 4.37e-09

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 58.68  E-value: 4.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAVKIVdvakftaspgLSTADLKREATI---CHMLK---HPHIVELLE--TYSSEGMLY 88
Cdd:cd14036    7 VIAEGGFAFVYEAQDVGTGKEYALKRL----------LSNEEEKNKAIIqeiNFMKKlsgHPNIVQFCSaaSIGKEESDQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLC----FEVVRRAVAGFVYSEAVACHYMRQILEALRYCHEND--ILHRDVRPACALLAtvdNSAPVKLGG 162
Cdd:cd14036   77 GQAEYLLLTELCkgqlVDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIG---NQGQIKLCD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 163 FGSAIQLP---------GTRETIETH-GRVGCPHYMAPEVVTrrLY-----GKGCDVWGAGVMLHVLLSGRLPFlGSGVR 227
Cdd:cd14036  154 FGSATTEAhypdyswsaQKRSLVEDEiTRNTTPMYRTPEMID--LYsnypiGEKQDIWALGCILYLLCFRKHPF-EDGAK 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 442620344 228 LQQSVARGRLSFEAPEWKSISanakDLVMKMLAANPHHRLSITEVLD 274
Cdd:cd14036  231 LRIINAKYTIPPNDTQYTVFH----DLIRSTLKVNPEERLSITEIVE 273
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
13-221 4.64e-09

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 58.13  E-value: 4.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  13 ELCEVIGKGPFSIVRRCIHResNQQFAVKIV-DVAKFTASpglstadLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05039    9 KLGELIGKGEFGDVMLGDYR--GQKVAVKCLkDDSTAAQA-------FLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLcFEVVR---RAVAGFvyseAVACHYMRQILEALRYCHENDILHRDVrPACALLATVDNSApvKLGGFGSA-- 166
Cdd:cd05039   80 EYMAKGSL-VDYLRsrgRAVITR----KDQLGFALDVCEGMEYLESKKFVHRDL-AARNVLVSEDNVA--KVSDFGLAke 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 167 --IQLPGTRETIEthgrvgcphYMAPEVVTRRLYGKGCDVWGAGVMLHVLLS-GRLPF 221
Cdd:cd05039  152 asSNQDGGKLPIK---------WTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
18-222 4.71e-09

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 58.78  E-value: 4.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAkftaspgLSTADLKR---EATICHMLKHPHIVELLETysSEGMLYMV---- 90
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKSCRLE-------LSVKNKDRwchEIQIMKKLNHPNVVKACDV--PEEMNFLVndvp 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 ---FEFMEGSDLcfevvRRAV------AGFVYSEAVAchYMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLG 161
Cdd:cd14039   72 llaMEYCSGGDL-----RKLLnkpencCGLKESQVLS--LLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVHKII 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 162 GFGSAIQL-PGTRETiethGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFL 222
Cdd:cd14039  145 DLGYAKDLdQGSLCT----SFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFL 202
PDZ6_GRIP1-2-like cd06683
PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ...
496-572 4.76e-09

PDZ domain 6 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ6 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467171 [Multi-domain]  Cd Length: 85  Bit Score: 53.85  E-value: 4.76e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 496 VQFQKNTDePMGITLKMTED--GRCIVARIMHGGMIHRQATLHVGDEIREINGQPVQHQSVGQLQRMLREARGSVTFKI 572
Cdd:cd06683    6 VELKRYGG-PLGITISGTEEpfDPIVISGLTEGGLAERTGAIHVGDRILAINGESLRGKPLSEAIHLLQNAGDTVTLKI 83
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
18-235 5.26e-09

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 57.95  E-value: 5.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHReSNQQFAVKIVDVAkftaspGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFME-G 96
Cdd:cd05114   12 LGSGLFGVVRLGKWR-AQYKVAIKAIREG------AMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMEnG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  97 SDLCFEVVRRAvagfVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAiQLPGTRETI 176
Cdd:cd05114   85 CLLNYLRQRRG----KLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCL---VNDTGVVKVSDFGMT-RYVLDDQYT 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620344 177 ETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGV-MLHVLLSGRLPFLG-SGVRLQQSVARG 235
Cdd:cd05114  157 SSSGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVlMWEVFTEGKMPFESkSNYEVVEMVSRG 217
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
57-223 5.53e-09

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 58.88  E-value: 5.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  57 ADLKREATICHML-KHPHIVELLETYSSEGMLYMVFEFME--------------GSDLCFEVVRRAVAGFVYSEAVACHY 121
Cdd:cd05100   62 SDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYVLVEYASkgnlreylrarrppGMDYSFDTCKLPEEQLTFKDLVSCAY 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 122 mrQILEALRYCHENDILHRDVrPACALLATVDNSapVKLGGFGSAIQLPGT---RETieTHGRVGCpHYMAPEVVTRRLY 198
Cdd:cd05100  142 --QVARGMEYLASQKCIHRDL-AARNVLVTEDNV--MKIADFGLARDVHNIdyyKKT--TNGRLPV-KWMAPEALFDRVY 213
                        170       180
                 ....*....|....*....|....*.
gi 442620344 199 GKGCDVWGAGVML-HVLLSGRLPFLG 223
Cdd:cd05100  214 THQSDVWSFGVLLwEIFTLGGSPYPG 239
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
41-266 6.88e-09

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 57.73  E-value: 6.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  41 KIVDVAKFTASPG-LSTADLKREATICHMLKHPHIVELLETYSSEGmLYMVFEFME-GSDLCFevvRRAVAGFVYSEAVA 118
Cdd:cd05073   34 KHTKVAVKTMKPGsMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEP-IYIITEFMAkGSLLDF---LKSDEGSKQPLPKL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 119 CHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAiQLPGTRETIETHGRVGCPHYMAPEVVTRRLY 198
Cdd:cd05073  110 IDFSAQIAEGMAFIEQRNYIHRDLRAANIL---VSASLVCKIADFGLA-RVIEDNEYTAREGAKFPIKWTAPEAINFGSF 185
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 199 GKGCDVWGAGVMLHVLLS-GRLPFLG-SGVRLQQSVARGrlsFEAPEWKSISANAKDLVMKMLAANPHHR 266
Cdd:cd05073  186 TIKSDVWSFGILLMEIVTyGRIPYPGmSNPEVIRALERG---YRMPRPENCPEELYNIMMRCWKNRPEER 252
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
17-223 7.48e-09

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 57.81  E-value: 7.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHR---ESNQ-QFAVKIVDvakfTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLyMVFE 92
Cdd:cd05057   14 VLGSGAFGTVYKGVWIpegEKVKiPVAIKVLR----EETGPKANEEILDEAYVMASVDHPHLVRLLGICLSSQVQ-LITQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  93 FME-GSDLcfEVVRRAvAGFVYSEAVaCHYMRQILEALRYCHENDILHRDVRPACALLATVDNsapVKLGGFGSAIQLP- 170
Cdd:cd05057   89 LMPlGCLL--DYVRNH-RDNIGSQLL-LNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNH---VKITDFGLAKLLDv 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442620344 171 GTRETIETHGRVgcP-HYMAPEVVTRRLYGKGCDVWGAGVMLHVLLS-GRLPFLG 223
Cdd:cd05057  162 DEKEYHAEGGKV--PiKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYEG 214
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
12-217 9.96e-09

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 58.22  E-value: 9.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCIHRESNQQFAVKIVDVAK-FTASPglstadlKREATICHMLKHP------HIVELLETYSSE 84
Cdd:cd14224   67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKrFHRQA-------AEEIRILEHLKKQdkdntmNVIHMLESFTFR 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  85 GMLYMVFEFMegSDLCFEVVRR-AVAGF----VYSEAvacHYMRQILEALrycHENDILHRDVRPACALLATVDNSApVK 159
Cdd:cd14224  140 NHICMTFELL--SMNLYELIKKnKFQGFslqlVRKFA---HSILQCLDAL---HRNKIIHCDLKPENILLKQQGRSG-IK 210
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 160 LGGFGSAiqlpgTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSG 217
Cdd:cd14224  211 VIDFGSS-----CYEHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTG 263
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
57-223 1.31e-08

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 57.33  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  57 ADLKREATICHML-KHPHIVELLETYSSEGMLYMVFEFMEGSDL--------------CFEVVRRAVAGFVYSEAVACHY 121
Cdd:cd05098   63 SDLISEMEMMKMIgKHKNIINLLGACTQDGPLYVIVEYASKGNLreylqarrppgmeyCYNPSHNPEEQLSSKDLVSCAY 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 122 mrQILEALRYCHENDILHRDVrPACALLATVDNSapVKLGGFGSAIQLPGT---RETieTHGRVGCpHYMAPEVVTRRLY 198
Cdd:cd05098  143 --QVARGMEYLASKKCIHRDL-AARNVLVTEDNV--MKIADFGLARDIHHIdyyKKT--TNGRLPV-KWMAPEALFDRIY 214
                        170       180
                 ....*....|....*....|....*.
gi 442620344 199 GKGCDVWGAGVML-HVLLSGRLPFLG 223
Cdd:cd05098  215 THQSDVWSFGVLLwEIFTLGGSPYPG 240
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
57-223 1.35e-08

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 57.33  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  57 ADLKREATICHML-KHPHIVELLETYSSEGMLYMVFEFME--------------GSDLCFEVVRRAVAGFVYSEAVACHY 121
Cdd:cd05101   74 SDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYVIVEYASkgnlreylrarrppGMEYSYDINRVPEEQMTFKDLVSCTY 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 122 mrQILEALRYCHENDILHRDVrPACALLATVDNSapVKLGGFGSAIQLPGT---RETieTHGRVGCpHYMAPEVVTRRLY 198
Cdd:cd05101  154 --QLARGMEYLASQKCIHRDL-AARNVLVTENNV--MKIADFGLARDINNIdyyKKT--TNGRLPV-KWMAPEALFDRVY 225
                        170       180
                 ....*....|....*....|....*.
gi 442620344 199 GKGCDVWGAGV-MLHVLLSGRLPFLG 223
Cdd:cd05101  226 THQSDVWSFGVlMWEIFTLGGSPYPG 251
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
18-161 1.37e-08

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 54.37  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKftaspGLSTADLKREATICHMLK--HPHIVELLETYSSEGMLYMVFEFME 95
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKIGDDVN-----NEEGEDLESEMDILRRLKglELNIPKVLVTEDVDGPNILLMELVK 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620344  96 GsDLCFEVVRRAVAGFVYSEAVachyMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLG 161
Cdd:cd13968   76 G-GTLIAYTQEEELDEKDVESI----MYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
SH3_Intersectin_5 cd11840
Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor ...
587-643 1.41e-08

Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The fifth SH3 domain (or SH3E) of ITSN1 has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212774 [Multi-domain]  Cd Length: 53  Bit Score: 51.65  E-value: 1.41e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 587 VRAQFDYNPL-DDELipcaqagiSFQVGDILQIISKDDHHWWQARLDtvgGSAGLIPS 643
Cdd:cd11840    2 VIALFPYTAQnEDEL--------SFQKGDIINVLSKDDPDWWRGELN---GQTGLFPS 48
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
13-216 2.32e-08

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 56.58  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  13 ELCEVIGKGPFSIVRRCihreSNQQFAVKI-VDVAKFTASpglstADLKREATICHMLKHPHIVELLETYSSEGMLYMVF 91
Cdd:cd05051   28 GLSDLTSDDFIGNDNKD----EPVLVAVKMlRPDASKNAR-----EDFLKEVKIMSQLKDPNIVRLLGVCTRDEPLCMIV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  92 EFMEGSDLC--------FEVVRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDvrpacalLAT----VDNSAPVK 159
Cdd:cd05051   99 EYMENGDLNqflqkheaETQGASATNSKTLSYGTLLYMATQIASGMKYLESLNFVHRD-------LATrnclVGPNYTIK 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620344 160 LGGFGSAIQLPgTRETIETHGRVGCP-HYMAPEVVtrrLYGK---GCDVWGAGVMLHVLLS 216
Cdd:cd05051  172 IADFGMSRNLY-SGDYYRIEGRAVLPiRWMAWESI---LLGKfttKSDVWAFGVTLWEILT 228
SH3_OSTF1 cd11772
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or ...
586-643 2.54e-08

Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or SH3P2, is a signaling protein containing SH3 and ankyrin-repeat domains. It acts through a Src-related pathway to enhance the formation of osteoclasts and bone resorption. It also acts as a negative regulator of cell motility. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212706 [Multi-domain]  Cd Length: 53  Bit Score: 50.76  E-value: 2.54e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620344 586 FVRAQFDYNPL-DDELipcaqagiSFQVGDILQIISKDDHHWWQARLdtvGGSAGLIPS 643
Cdd:cd11772    1 VFRALYDYEAQhPDEL--------SFEEGDLLYISDKSDPNWWKATC---GGKTGLIPS 48
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
45-225 2.76e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 57.40  E-value: 2.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  45 VAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLYMV--------FEFMEGSDLCFE-----VVRRAVagf 111
Cdd:PHA03210 196 IAKRVKAGSRAAIQLENEILALGRLNHENILKIEEILRSEANTYMItqkydfdlYSFMYDEAFDWKdrpllKQTRAI--- 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 112 vyseavachyMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAIQLPGTRETIEtHGRVGCPHYMAPE 191
Cdd:PHA03210 273 ----------MKQLLCAVEYIHDKKLIHRDIKLENIFL---NCDGKIVLGDFGTAMPFEKEREAFD-YGWVGTVATNSPE 338
                        170       180       190
                 ....*....|....*....|....*....|....
gi 442620344 192 VVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLGSG 225
Cdd:PHA03210 339 ILAGDGYCEITDIWSCGLILLDMLSHDFCPIGDG 372
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
10-266 3.05e-08

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 56.05  E-value: 3.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHReSNQQFAVKIVDVAKFTASPGLSTADLKREatichmLKHPHIVELLETYSSEGmLYM 89
Cdd:cd05067    7 ETLKLVERLGAGQFGEVWMGYYN-GHTKVAIKSLKQGSMSPDAFLAEANLMKQ------LQHQRLVRLYAVVTQEP-IYI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFME-GSDLCFevvRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQ 168
Cdd:cd05067   79 ITEYMEnGSLVDF---LKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANIL---VSDTLSCKIADFGLARL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 169 LPGTRETIETHGRVGCpHYMAPEVVTRRLYGKGCDVWGAGVML-HVLLSGRLPFLG-SGVRLQQSVARGrlsFEAPEWKS 246
Cdd:cd05067  153 IEDNEYTAREGAKFPI-KWTAPEAINYGTFTIKSDVWSFGILLtEIVTHGRIPYPGmTNPEVIQNLERG---YRMPRPDN 228
                        250       260
                 ....*....|....*....|
gi 442620344 247 ISANAKDLVMKMLAANPHHR 266
Cdd:cd05067  229 CPEELYQLMRLCWKERPEDR 248
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
18-211 3.71e-08

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 55.59  E-value: 3.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKivDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMK--ELIRFDEE---AQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLCfEVVRRAVAGFVYSEAVacHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFG------------S 165
Cdd:cd14154   76 TLK-DVLKDMARPLPWAQRV--RFAKDIASGMAYLHSMNIIHRDLNSHNCL---VREDKTVVVADFGlarliveerlpsG 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442620344 166 AIQLPGTRETIETHGR------VGCPHYMAPEVVTRRLYGKGCDVWGAGVML 211
Cdd:cd14154  150 NMSPSETLRHLKSPDRkkrytvVGNPYWMAPEMLNGRSYDEKVDIFSFGIVL 201
PDZ6_MUPP1-like cd06670
PDZ domain 6 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
500-564 4.08e-08

PDZ domain 6 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 6 of multi-PDZ-domain protein 1 (MUPP1). MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, PDZ9, and PDZ13. This MuPP1-like PDZ6 domain is therefore absent from PATJ. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ6 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467158 [Multi-domain]  Cd Length: 87  Bit Score: 51.49  E-value: 4.08e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620344 500 KNTDEPMGITLKMTEDGR-CIVARIMHGGMIHRQATLHVGDEIREINGQPVQHQSVGQLQRMLREA 564
Cdd:cd06670   10 VKGNSSLGITVSADKDGNgCIVKSIIHGGAVSRDGRISVGDFIVSINNESLRNVTNAQARAILRRA 75
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
16-221 4.67e-08

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 55.46  E-value: 4.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQqfavKIVDVAKFTASPGLST---ADLKREATICHMLKHPHIVELLETYSSEGMLYMVFE 92
Cdd:cd05033   10 KVIGGGEFGEVCSGSLKLPGK----KEIDVAIKTLKSGYSDkqrLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  93 FMEGSDLcFEVVRRAVAGFVYSEAVAchYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLPGT 172
Cdd:cd05033   86 YMENGSL-DKFLRENDGKFTVTQLVG--MLRGIASGMKYLSEMNYVHRDLAARNIL---VNSDLVCKVSDFGLSRRLEDS 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 442620344 173 RETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAG-VMLHVLLSGRLPF 221
Cdd:cd05033  160 EATYTTKGGKIPIRWTAPEAIAYRKFTSASDVWSFGiVMWEVMSYGERPY 209
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
18-272 4.78e-08

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 55.43  E-value: 4.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIV--RRCIHRESNQQFAVKIVDVAKFTASPGlsTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFME 95
Cdd:cd05093   13 LGEGAFGKVflAECYNLCPEQDKILVAVKTLKDASDNA--RKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 GSDLCFEVVRRAVAGFVYSE---------AVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSA 166
Cdd:cd05093   91 HGDLNKFLRAHGPDAVLMAEgnrpaeltqSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCL---VGENLLVKIGDFGMS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLPGTrETIETHGRVGCP-HYMAPEVVTRRLYGKGCDVWGAGVML-HVLLSGRLPFLG-SGVRLQQSVARGRLsFEAPe 243
Cdd:cd05093  168 RDVYST-DYYRVGGHTMLPiRWMPPESIMYRKFTTESDVWSLGVVLwEIFTYGKQPWYQlSNNEVIECITQGRV-LQRP- 244
                        250       260
                 ....*....|....*....|....*....
gi 442620344 244 wKSISANAKDLVMKMLAANPHHRLSITEV 272
Cdd:cd05093  245 -RTCPKEVYDLMLGCWQREPHMRLNIKEI 272
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
18-238 5.57e-08

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 55.09  E-value: 5.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCihrESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVeLLETYSSEGMLYMVFEFMEGS 97
Cdd:cd14062    1 IGSGSFGTVYKG---RWHGDVAVKKLNVTDPTPS---QLQAFKNEVAVLRKTRHVNIL-LFMGYMTKPQLAIVTQWCEGS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLcFEVVRRAVAGFVYSEAVacHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAiqlpgtreTIE 177
Cdd:cd14062   74 SL-YKHLHVLETKFEMLQLI--DIARQTAQGMDYLHAKNIIHRDLKSNNIFL---HEDLTVKIGDFGLA--------TVK 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620344 178 THGRVGCPH--------YMAPEVVtrRL-----YGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQ--SVARGRLS 238
Cdd:cd14062  140 TRWSGSQQFeqptgsilWMAPEVI--RMqdenpYSFQSDVYAFGIVLYELLTGQLPYSHINNRDQIlfMVGRGYLR 213
PDZ3_harmonin cd06739
PDZ domain 3 of harmonin isoforms a and b, and related domains; PDZ (PSD-95 (Postsynaptic ...
493-582 5.66e-08

PDZ domain 3 of harmonin isoforms a and b, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of harmonin isoforms a and b, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This harmonin family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467221 [Multi-domain]  Cd Length: 94  Bit Score: 51.16  E-value: 5.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 493 VRLVQFQKNTdePMGITLKMTED----GRCIVARIMHGGMIHRQATLHVGDEIREINGQPVQHQSVGQLQRMLREARGSV 568
Cdd:cd06739    3 VRLLRIKKNG--PLDLALEGGIDsplgGKIVVSAVYEGGAADKHGGIVKGDQIMMVNGKSLTDVTLAEAEAALQRAMNSG 80
                         90
                 ....*....|....
gi 442620344 569 TFKIVPSYRSAPPP 582
Cdd:cd06739   81 GDWIDLVIAVAPPK 94
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
41-272 5.80e-08

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 55.40  E-value: 5.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  41 KIVDVAKFTASPGLST-ADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGSDLCFEVVRRAVAGFVYSE---- 115
Cdd:cd05094   35 KMLVAVKTLKDPTLAArKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEYMKHGDLNKFLRAHGPDAMILVDgqpr 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 116 --------AVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLPGTrETIETHGRVGCP-H 186
Cdd:cd05094  115 qakgelglSQMLHIATQIASGMVYLASQHFVHRDLATRNCL---VGANLLVKIGDFGMSRDVYST-DYYRVGGHTMLPiR 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 187 YMAPEVVTRRLYGKGCDVWGAGVML-HVLLSGRLP-FLGSGVRLQQSVARGRLsFEAPewKSISANAKDLVMKMLAANPH 264
Cdd:cd05094  191 WMPPESIMYRKFTTESDVWSFGVILwEIFTYGKQPwFQLSNTEVIECITQGRV-LERP--RVCPKEVYDIMLGCWQREPQ 267

                 ....*...
gi 442620344 265 HRLSITEV 272
Cdd:cd05094  268 QRLNIKEI 275
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
45-235 6.22e-08

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 54.54  E-value: 6.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  45 VAKFTASPG-LSTADLKREATICHMLKHPHIVELLETYSSEGmLYMVFEFM-EGSDLCFevvRRAVAGFVYSEAVACHYM 122
Cdd:cd14203   22 VAIKTLKPGtMSPEAFLEEAQIMKKLRHDKLVQLYAVVSEEP-IYIVTEFMsKGSLLDF---LKDGEGKYLKLPQLVDMA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 123 RQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAiQLPGTRETIETHGRVGCPHYMAPEVVtrrLYGK-- 200
Cdd:cd14203   98 AQIASGMAYIERMNYIHRDLRAANIL---VGDNLVCKIADFGLA-RLIEDNEYTARQGAKFPIKWTAPEAA---LYGRft 170
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 442620344 201 -GCDVWGAGVMLHVLLS-GRLPFLGSGVR--LQQsVARG 235
Cdd:cd14203  171 iKSDVWSFGILLTELVTkGRVPYPGMNNRevLEQ-VERG 208
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
12-277 6.45e-08

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 55.63  E-value: 6.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  12 YELCEVIGKGPFSIVRRCI-HRESNQQFAVKIVdvakftaspglSTADLKREATICHMLKHPHI-----------VELLE 79
Cdd:cd14213   14 YEIVDTLGEGAFGKVVECIdHKMGGMHVAVKIV-----------KNVDRYREAARSEIQVLEHLnttdpnstfrcVQMLE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  80 TYSSEGMLYMVFEFMEGSDLCFeVVRRAVAGFVYSEAVACHYmrQILEALRYCHENDILHRDVRPACALLATVD------ 153
Cdd:cd14213   83 WFDHHGHVCIVFELLGLSTYDF-IKENSFLPFPIDHIRNMAY--QICKSVNFLHHNKLTHTDLKPENILFVQSDyvvkyn 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 154 ----------NSAPVKLGGFGSAiqlpgTRETIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVML------------ 211
Cdd:cd14213  160 pkmkrdertlKNPDIKVVDFGSA-----TYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILieyylgftvfqt 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 212 -----HVLLSGRLPFLGSGVRLQQSVARGRLSFEAPEWKSISANAK------------------------DLVMKMLAAN 262
Cdd:cd14213  235 hdskeHLAMMERILGPLPKHMIQKTRKRKYFHHDQLDWDEHSSAGRyvrrrckplkefmlsqdvdheqlfDLIQKMLEYD 314
                        330
                 ....*....|....*
gi 442620344 263 PHHRLSITEVLDHPW 277
Cdd:cd14213  315 PAKRITLDEALKHPF 329
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
18-275 6.87e-08

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 54.62  E-value: 6.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKftaspgLSTADLKREATICHMLK---HPHIVELLETYSS----EGMLYMV 90
Cdd:cd14033    9 IGRGSFKTVYRGLDTETTVEVAWCELQTRK------LSKGERQRFSEEVEMLKglqHPNIVRFYDSWKStvrgHKCIILV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  91 FEFMEGSDLcfevvRRAVAGFVYSE-AVACHYMRQILEALRYCHEN--DILHRDVRpaCALLATVDNSAPVKLGGFGsai 167
Cdd:cd14033   83 TELMTSGTL-----KTYLKRFREMKlKLLQRWSRQILKGLHFLHSRcpPILHRDLK--CDNIFITGPTGSVKIGDLG--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 qLPGTRETIETHGRVGCPHYMAPEVVTRRlYGKGCDVWGAGVMLHVLLSGRLPF--LGSGVRLQQSVARGRL--SF---E 240
Cdd:cd14033  153 -LATLKRASFAKSVIGTPEFMAPEMYEEK-YDEAVDVYAFGMCILEMATSEYPYseCQNAAQIYRKVTSGIKpdSFykvK 230
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 442620344 241 APEWKSIsanakdlVMKMLAANPHHRLSITEVLDH 275
Cdd:cd14033  231 VPELKEI-------IEGCIRTDKDERFTIQDLLEH 258
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
16-192 7.61e-08

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 54.75  E-value: 7.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCihRESNQQFAVKIVDVAKFtaspglstADLKREATICH--MLKHPHIVELL---ETYSSEGM-LYM 89
Cdd:cd13998    1 EVIGKGRFGEVWKA--SLKNEPVAVKIFSSRDK--------QSWFREKEIYRtpMLKHENILQFIaadERDTALRTeLWL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  90 VFEFMEGSDLCfEVVRRAVAGFVYSeavaCHYMRQILEALRYCHEN---------DILHRDVRPACALlatVDNSAPVKL 160
Cdd:cd13998   71 VTAFHPNGSL*-DYLSLHTIDWVSL----CRLALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNIL---VKNDGTCCI 142
                        170       180       190
                 ....*....|....*....|....*....|....
gi 442620344 161 GGFGSAIQLPGTRET--IETHGRVGCPHYMAPEV 192
Cdd:cd13998  143 ADFGLAVRLSPSTGEedNANNGQVGTKRYMAPEV 176
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
18-277 7.63e-08

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 54.70  E-value: 7.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTAspgLSTADLKREATICHMLKHPHIVELLETYSSEGM----LYMVFEF 93
Cdd:cd14032    9 LGRGSFKTVYKGLDTETWVEVAWCELQDRKLTK---VERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrcIVLVTEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  94 MEGSDLCFEVVRRAVAgfvySEAVACHYMRQILEALRYCHEND--ILHRDVRpaCALLATVDNSAPVKLGGFGsaiqLPG 171
Cdd:cd14032   86 MTSGTLKTYLKRFKVM----KPKVLRSWCRQILKGLLFLHTRTppIIHRDLK--CDNIFITGPTGSVKIGDLG----LAT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHGRVGCPHYMAPEVVTRRlYGKGCDVWGAGVMLHVLLSGRLPF--LGSGVRLQQSVARG--RLSFEapewKSI 247
Cdd:cd14032  156 LKRASFAKSVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEYPYseCQNAAQIYRKVTCGikPASFE----KVT 230
                        250       260       270
                 ....*....|....*....|....*....|
gi 442620344 248 SANAKDLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14032  231 DPEIKEIIGECICKNKEERYEIKDLLSHAF 260
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
17-216 8.07e-08

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 54.90  E-value: 8.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHRESNQQFAvKIVDVAKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGM--LYMVFEFM 94
Cdd:cd05081   11 QLGKGNFGSVELCRYDPLGDNTG-ALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGRrsLRLVMEYL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  95 -EGSDLCFEVVRRAVAGfvyseavACH---YMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLP 170
Cdd:cd05081   90 pSGCLRDFLQRHRARLD-------ASRlllYSSQICKGMEYLGSRRCVHRDLAARNIL---VESEAHVKIADFGLAKLLP 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 442620344 171 GTRETIETHGRVGCP-HYMAPEVVTRRLYGKGCDVWGAGVMLHVLLS 216
Cdd:cd05081  160 LDKDYYVVREPGQSPiFWYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
13-274 8.13e-08

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 54.66  E-value: 8.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  13 ELCEVIGKGPFSIVRRCI-HRESnqqfAVKIVDVAkftaspGLSTADL---KREATICHMLKHPHIVELLETYSSEGMLY 88
Cdd:cd14063    3 EIKEVIGKGRFGRVHRGRwHGDV----AIKLLNID------YLNEEQLeafKEEVAAYKNTRHDNLVLFMGACMDPPHLA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFMEGSDLcFEVVRRAVAGFVYSEAVacHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPV--KLGGFGSA 166
Cdd:cd14063   73 IVTSLCKGRTL-YSLIHERKEKFDFNKTV--QIAQQICQGMGYLHAKGIIHKDLKSKNIFL---ENGRVVitDFGLFSLS 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 167 IQLPGTREtietHGRVGCPH----YMAPEVVtRRL-----------YGKGCDVWGAGVMLHVLLSGRLPF---------- 221
Cdd:cd14063  147 GLLQPGRR----EDTLVIPNgwlcYLAPEII-RALspdldfeeslpFTKASDVYAFGTVWYELLAGRWPFkeqpaesiiw 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 442620344 222 -LGSGvrLQQSVARGRLSFEapewksisanAKDLVMKMLAANPHHRLSITEVLD 274
Cdd:cd14063  222 qVGCG--KKQSLSQLDIGRE----------VKDILMQCWAYDPEKRPTFSDLLR 263
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
18-220 8.25e-08

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 54.45  E-value: 8.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKI----VDVAKFTaspglstadlkREATICHMLKHPHIVELLETYSSEGMLYMVFEF 93
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIykndVDQHKIV-----------REISLLQKLSHPNIVRYLGICVKDEKLHPILEY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  94 MEGSDLCfEVVRRAVAGFVYSEAV--AChymrQILEALRYCHENDILHRDVRPACALLATVDNSAPVKLGGFGSAiqlpg 171
Cdd:cd14156   70 VSGGCLE-ELLAREELPLSWREKVelAC----DISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAVVTDFGLA----- 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344 172 tRETIETHGR--------VGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLsGRLP 220
Cdd:cd14156  140 -REVGEMPANdperklslVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL-ARIP 194
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
4-221 8.82e-08

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 54.57  E-value: 8.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   4 DEILFDDVyELceviGKGPFSIVRRCIHRESNQQFAVKIvDVAKFTASPGLsTADLKREATICHMLKHPHIVELLETYSS 83
Cdd:cd05115    3 DNLLIDEV-EL----GSGNFGCVKKGVYKMRKKQIDVAI-KVLKQGNEKAV-RDEMMREAQIMHQLDNPYIVRMIGVCEA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGMLyMVFEFMEGSDLC-FEVVRRAVagfVYSEAVAcHYMRQILEALRYCHENDILHRDVRPACALLAtvdNSAPVKLGG 162
Cdd:cd05115   76 EALM-LVMEMASGGPLNkFLSGKKDE---ITVSNVV-ELMHQVSMGMKYLEEKNFVHRDLAARNVLLV---NQHYAKISD 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620344 163 FG--SAIQLPGTRETIETHGRVGCPHYmAPEVVTRRLYGKGCDVWGAGV-MLHVLLSGRLPF 221
Cdd:cd05115  148 FGlsKALGADDSYYKARSAGKWPLKWY-APECINFRKFSSRSDVWSYGVtMWEAFSYGQKPY 208
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
58-211 9.45e-08

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 54.35  E-value: 9.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  58 DLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGSDLcFEVVRRAVAGFVysEAVACHYM-RQILEALRYCHEND 136
Cdd:cd05052   48 EFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNL-LDYLRECNREEL--NAVVLLYMaTQIASAMEYLEKKN 124
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620344 137 ILHRDVRPACALLAtvDNSApVKLGGFGSAIQLPGtrETIETHGRVGCP-HYMAPEVVTRRLYGKGCDVWGAGVML 211
Cdd:cd05052  125 FIHRDLAARNCLVG--ENHL-VKVADFGLSRLMTG--DTYTAHAGAKFPiKWTAPESLAYNKFSIKSDVWAFGVLL 195
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
18-280 1.14e-07

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 54.29  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSS----EGMLYMVFEF 93
Cdd:cd14030   33 IGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKS---ERQRFKEEAGMLKGLQHPNIVRFYDSWEStvkgKKCIVLVTEL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  94 MEGSDLCFEVVRRAVAGFvyseAVACHYMRQILEALRYCHEND--ILHRDVRpaCALLATVDNSAPVKLGGFGsaiqLPG 171
Cdd:cd14030  110 MTSGTLKTYLKRFKVMKI----KVLRSWCRQILKGLQFLHTRTppIIHRDLK--CDNIFITGPTGSVKIGDLG----LAT 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 172 TRETIETHGRVGCPHYMAPEVVTRRlYGKGCDVWGAGVMLHVLLSGRLPF--LGSGVRLQQSVARG--RLSFEapewKSI 247
Cdd:cd14030  180 LKRASFAKSVIGTPEFMAPEMYEEK-YDESVDVYAFGMCMLEMATSEYPYseCQNAAQIYRRVTSGvkPASFD----KVA 254
                        250       260       270
                 ....*....|....*....|....*....|...
gi 442620344 248 SANAKDLVMKMLAANPHHRLSITEVLDHPWIRD 280
Cdd:cd14030  255 IPEVKEIIEGCIRQNKDERYAIKDLLNHAFFQE 287
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
10-266 1.40e-07

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 53.92  E-value: 1.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  10 DVYELCEVIGKGPFSIVRRCIHrESNQQFAVKivdvakfTASPG-LSTADLKREATICHMLKHPHIVELLETYSSEGmLY 88
Cdd:cd05070    9 ESLQLIKRLGNGQFGEVWMGTW-NGNTKVAIK-------TLKPGtMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEP-IY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  89 MVFEFM-EGSDLCFevvRRAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAi 167
Cdd:cd05070   80 IVTEYMsKGSLLDF---LKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANIL---VGNGLICKIADFGLA- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLPGTRETIETHGRVGCPHYMAPEVVtrrLYGK---GCDVWGAGVMLHVLLS-GRLPFLGSGVR-LQQSVARGrlsFEAP 242
Cdd:cd05070  153 RLIEDNEYTARQGAKFPIKWTAPEAA---LYGRftiKSDVWSFGILLTELVTkGRVPYPGMNNReVLEQVERG---YRMP 226
                        250       260
                 ....*....|....*....|....
gi 442620344 243 EWKSISANAKDLVMKMLAANPHHR 266
Cdd:cd05070  227 CPQDCPISLHELMIHCWKKDPEER 250
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
3-230 1.45e-07

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 54.15  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344   3 EDEILFDDVYELCEVIGKGPFSIVRRCIHRESN---QQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVELLE 79
Cdd:cd05074    2 KDVLIQEQQFTLGRMLGKGEFGSVREAQLKSEDgsfQKVAVKMLKADIFSSS---DIEEFLREAACMKEFDHPNVIKLIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  80 T---YSSEGML---YMVFEFMEGSDL-CFEVVRR-AVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLat 151
Cdd:cd05074   79 VslrSRAKGRLpipMVILPFMKHGDLhTFLLMSRiGEEPFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCML-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 152 vDNSAPVKLGGFGSAIQLPGTretieTHGRVGCP-----HYMAPEVVTRRLYGKGCDVWGAGV-MLHVLLSGRLPFLG-- 223
Cdd:cd05074  157 -NENMTVCVADFGLSKKIYSG-----DYYRQGCAsklpvKWLALESLADNVYTTHSDVWAFGVtMWEIMTRGQTPYAGve 230
                        250
                 ....*....|....*.
gi 442620344 224 ---------SGVRLQQ 230
Cdd:cd05074  231 nseiynyliKGNRLKQ 246
SH3_Src_like cd11845
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ...
586-643 1.51e-07

Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, Yes, and Brk. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). However, Brk lacks the N-terminal myristoylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells, and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, Lyn, and Brk show a limited expression pattern. This subfamily also includes Drosophila Src42A, Src oncogene at 42A (also known as Dsrc41) which accumulates at sites of cell-cell or cell-matrix adhesion, and participates in Drosphila development and wound healing. It has been shown to promote tube elongation in the tracheal system, is essential for proper cell-cell matching during dorsal closure, and regulates cell-cell contacts in developing Drosophila eyes. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212779 [Multi-domain]  Cd Length: 52  Bit Score: 48.73  E-value: 1.51e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 586 FVRAQFDYNPL-DDELipcaqagiSFQVGDILQIISKDDHHWWQAR-LDTvgGSAGLIPS 643
Cdd:cd11845    1 IYVALYDYEARtDDDL--------SFKKGDRLQILDDSDGDWWLARhLST--GKEGYIPS 50
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
122-277 1.63e-07

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 54.37  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 122 MRQILEALRYCHENDILHRDVRPACALLATVDNSapVKLGGFGSAIQLpgtretiethgRVGC----------PHYMAPE 191
Cdd:cd14013  126 MRQILVALRKLHSTGIVHRDVKPQNIIVSEGDGQ--FKIIDLGAAADL-----------RIGInyipkeflldPRYAPPE 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 192 VV-----TRR---------------LYGKG--CDVWGAGVMlhvLLSGRLPFLGSGVRLQQSVAR-GRLSFEAPEWKS-- 246
Cdd:cd14013  193 QYimstqTPSappapvaaalspvlwQMNLPdrFDMYSAGVI---LLQMAFPNLRSDSNLIAFNRQlKQCDYDLNAWRMlv 269
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 442620344 247 ---ISANAK--------------DLVMKMLAANPHHRLSITEVLDHPW 277
Cdd:cd14013  270 eprASADLRegfeildlddgagwDLVTKLIRYKPRGRLSASAALAHPY 317
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
18-211 1.67e-07

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 53.79  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHRESNQQFAVKivDVAKFTASpglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGS 97
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMK--ELIRCDEE---TQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLcfEVVRRAVAGFVYSEAVAchYMRQILEALRYCHENDILHRDVRPACALLaTVDNSAPVKLGGFGSAI---------- 167
Cdd:cd14222   76 TL--KDFLRADDPFPWQQKVS--FAKGIASGMAYLHSMSIIHRDLNSHNCLI-KLDKTVVVADFGLSRLIveekkkpppd 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 442620344 168 QLPGTRETIETHGR------VGCPHYMAPEVVTRRLYGKGCDVWGAGVML 211
Cdd:cd14222  151 KPTTKKRTLRKNDRkkrytvVGNPYWMAPEMLNGKSYDEKVDIFSFGIVL 200
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
13-223 1.87e-07

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 53.53  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  13 ELCEVIGKGPFSIVRRcIH------RESNQQFAVKIVdvaKFTASPGLSTaDLKREATICHMLKHPHIVELLETYSSEGM 86
Cdd:cd05048    8 RFLEELGEGAFGKVYK-GEllgpssEESAISVAIKTL---KENASPKTQQ-DFRREAELMSDLQHPNIVCLLGVCTKEQP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  87 LYMVFEFMEGSDLCFEVVRRAVA---GFVYSEAVACHYMR---------QILEALRYCHENDILHRDvrpacalLAT--- 151
Cdd:cd05048   83 QCMLFEYMAHGDLHEFLVRHSPHsdvGVSSDDDGTASSLDqsdflhiaiQIAAGMEYLSSHHYVHRD-------LAArnc 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 152 -VDNSAPVKLGGFGSaiqlpgTREtIETHGRVGCPH-------YMAPEVVtrrLYGK---GCDVWGAGVMLHVLLS-GRL 219
Cdd:cd05048  156 lVGDGLTVKISDFGL------SRD-IYSSDYYRVQSksllpvrWMPPEAI---LYGKfttESDVWSFGVVLWEIFSyGLQ 225

                 ....
gi 442620344 220 PFLG 223
Cdd:cd05048  226 PYYG 229
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
18-243 1.93e-07

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 53.43  E-value: 1.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRCIHR--ESNQQFAVKIVdvaKFTASPGLSTADLKREATICHMLKHPHIVELLETYSSEGMLyMVFEFME 95
Cdd:cd05116    3 LGSGNFGTVKKGYYQmkKVVKTVAVKIL---KNEANDPALKDELLREANVMQQLDNPYIVRMIGICEAESWM-LVMEMAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 GSDLC-FEVVRRAVAGFVYSEAVachymRQILEALRYCHENDILHRDVRPACALLATvDNSAPVKLGGFGSAIQLPGTRE 174
Cdd:cd05116   79 LGPLNkFLQKNRHVTEKNITELV-----HQVSMGMKYLEESNFVHRDLAARNVLLVT-QHYAKISDFGLSKALRADENYY 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620344 175 TIETHGRVGCPHYmAPEVVTRRLYGKGCDVWGAGVMLHVLLS-GRLPFLG-SGVRLQQSVARGRlSFEAPE 243
Cdd:cd05116  153 KAQTHGKWPVKWY-APECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKGmKGNEVTQMIEKGE-RMECPA 221
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
18-262 1.95e-07

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 53.50  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  18 IGKGPFSIVRRcihRESNQQFAVKIVDVAKFTASpglSTADLKREATICHMLKHPHIVeLLETYSSEGMLYMVFEFMEGS 97
Cdd:cd14149   20 IGSGSFGTVYK---GKWHGDVAVKILKVVDPTPE---QFQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  98 DLCFEVvrrAVAGFVYSEAVACHYMRQILEALRYCHENDILHRDVRPACALLatvDNSAPVKLGGFGSAI---QLPGTRE 174
Cdd:cd14149   93 SLYKHL---HVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL---HEGLTVKIGDFGLATvksRWSGSQQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 175 TIETHGRVgcpHYMAPEVVTRR---LYGKGCDVWGAGVMLHVLLSGRLPFLGSGVRLQQSVARGRlSFEAPEWKSISANA 251
Cdd:cd14149  167 VEQPTGSI---LWMAPEVIRMQdnnPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGR-GYASPDLSKLYKNC 242
                        250
                 ....*....|.
gi 442620344 252 KDlVMKMLAAN 262
Cdd:cd14149  243 PK-AMKRLVAD 252
pknD PRK13184
serine/threonine-protein kinase PknD;
61-271 2.01e-07

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 55.16  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  61 REATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGSDL---------CfEVVRRAVAgfvYSEAVAChYMR---QILEA 128
Cdd:PRK13184  51 REAKIAADLIHPGIVPVYSICSDGDPVYYTMPYIEGYTLksllksvwqK-ESLSKELA---EKTSVGA-FLSifhKICAT 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 129 LRYCHENDILHRDVRPacallatvDNsapVKLGGFGSAIQLP-GTRETIETH----------------------GR-VGC 184
Cdd:PRK13184 126 IEYVHSKGVLHRDLKP--------DN---ILLGLFGEVVILDwGAAIFKKLEeedlldidvdernicyssmtipGKiVGT 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 185 PHYMAPEvvtrRLYG----KGCDVWGAGVMLHVLLSGRLPFLGSgvRLQQSVARGRLSF--EAPEWKSISANAKDLVMKM 258
Cdd:PRK13184 195 PDYMAPE----RLLGvpasESTDIYALGVILYQMLTLSFPYRRK--KGRKISYRDVILSpiEVAPYREIPPFLSQIAMKA 268
                        250
                 ....*....|....
gi 442620344 259 LAANPHHRL-SITE 271
Cdd:PRK13184 269 LAVDPAERYsSVQE 282
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
17-274 2.50e-07

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 53.03  E-value: 2.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  17 VIGKGPFSIVRRCIHResNQQFAVKIVDvaKFTaspglSTADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEG 96
Cdd:cd14068    1 LLGDGGFGSVYRAVYR--GEDVAVKIFN--KHT-----SFRLLRQELVVLSHLHHPSLVALLAAGTAPRMLVMELAPKGS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  97 SDLCFEVvRRAVAGFVYSEAVACHymrqILEALRYCHENDILHRDVRPACALLATVDNSAPV--KLGGFGSAIQLpgTRE 174
Cdd:cd14068   72 LDALLQQ-DNASLTRTLQHRIALH----VADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCAIiaKIADYGIAQYC--CRM 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 175 TIEThgRVGCPHYMAPEVVTRRL-YGKGCDVWGAGVMLHVLLSG--------RLPFLGSGVRLQQSVARGRLSFEAPEWK 245
Cdd:cd14068  145 GIKT--SEGTPGFRAPEVARGNViYNQQADVYSFGLLLYDILTCgeriveglKFPNEFDELAIQGKLPDPVKEYGCAPWP 222
                        250       260
                 ....*....|....*....|....*....
gi 442620344 246 SISAnakdLVMKMLAANPHHRLSITEVLD 274
Cdd:cd14068  223 GVEA----LIKDCLKENPQCRPTSAQVFD 247
SH3_CACNB1 cd12041
Src Homology 3 domain of Voltage-dependent L-type calcium channel subunit beta-1; The beta1 ...
582-644 2.51e-07

Src Homology 3 domain of Voltage-dependent L-type calcium channel subunit beta-1; The beta1 subunit of voltage-dependent calcium channels (Ca(V)s) is one of four beta subunits present in vertebrates. It is the only beta subunit, as the beta1a variant, expressed in skeletal muscle; the beta1b variant is also widely expressed in other tissues including the heart and brain. Knockout of the beta1 gene in mice results in embryonic lethality, demonstrating its importance in development. Ca(V)s are multi-protein complexes that regulate the entry of calcium into cells. They impact muscle contraction, neuronal migration, hormone and neurotransmitter release, and the activation of calcium-dependent signaling pathways. They are composed of four subunits: alpha1, alpha2delta, beta, and gamma. The beta subunit is a soluble and intracellular protein that interacts with the transmembrane alpha1 subunit. It facilitates the trafficking and proper localization of the alpha1 subunit to the cellular plasma membrane. Vertebrates contain four different beta subunits from distinct genes (beta1-4); each exists as multiple splice variants. All are expressed in the brain while other tissues show more specific expression patterns. The beta subunits show similarity to MAGUK (membrane-associated guanylate kinase) proteins in that they contain SH3 and inactive guanylate kinase (GuK) domains; however, they do not appear to contain a PDZ domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212974  Cd Length: 68  Bit Score: 48.82  E-value: 2.51e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620344 582 PCEIFVRAQFDYNPLDDELIPCAQAGISFQVGDILQIISKDDHHWWQARLDTVGGSAGLIPSP 644
Cdd:cd12041    2 PVAFAVRTNVGYNPSPGDDVPVQGMAISFEPKDFLHIKEKYNNDWWIGRLVKEGCEVGFIPSP 64
SH3_GRAP_C cd11951
C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ...
586-642 3.10e-07

C-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domains (SH3c) of the related proteins, GRB2 and GRAP2, have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212884  Cd Length: 53  Bit Score: 47.87  E-value: 3.10e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344 586 FVRAQFDYNPLDdelipcaQAGISFQVGDILQIISKDDHHWWQARldtVGGSAGLIP 642
Cdd:cd11951    1 FVQAQYDFSAED-------PSQLSFRRGDIIEVLDCPDPNWWRGR---ISGRVGFFP 47
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
14-275 3.10e-07

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 52.78  E-value: 3.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  14 LCEVIGKGPFSIVR----RCIHRESNQ-QFAVKIVdvakftasPGLSTA----DLKREATICHMLKHPHIVELLETYSSE 84
Cdd:cd05036   10 LIRALGQGAFGEVYegtvSGMPGDPSPlQVAVKTL--------PELCSEqdemDFLMEALIMSKFNHPNIVRCIGVCFQR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  85 GMLYMVFEFMEGSDL-CFEVVRRAVAG----FVYSEAVAChyMRQILEALRYCHENDILHRDVRPACALLATVDNSAPVK 159
Cdd:cd05036   82 LPRFILLELMAGGDLkSFLRENRPRPEqpssLTMLDLLQL--AQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPGRVAK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 160 LGGFGSAiqlpgtRETIETH-----GRVGCP-HYMAPEVVTRRLYGKGCDVWGAGVMLHVLLS-GRLPFLGSGVR--LQQ 230
Cdd:cd05036  160 IGDFGMA------RDIYRADyyrkgGKAMLPvKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSlGYMPYPGKSNQevMEF 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 442620344 231 SVARGRLsfEAPEwksisaNAKDLVMKMLAA----NPHHRLSITEVLDH 275
Cdd:cd05036  234 VTSGGRM--DPPK------NCPGPVYRIMTQcwqhIPEDRPNFSTILER 274
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
124-268 3.21e-07

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 53.27  E-value: 3.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 124 QILEALRYCHENDILHRDVRPACALLATVDNSAPV-KLGGFGSAI-------QLPGTRETIETHGRvGCphYMAPEVVTR 195
Cdd:cd14018  146 QLLEGVDHLVRHGIAHRDLKSDNILLELDFDGCPWlVIADFGCCLaddsiglQLPFSSWYVDRGGN-AC--LMAPEVSTA 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 196 RL-------YGKGcDVWGAGVMLHVLLSGRLPFLGSGvrlqQSVARGRlSFEAPEWKSISAN----AKDLVMKMLAANPH 264
Cdd:cd14018  223 VPgpgvvinYSKA-DAWAVGAIAYEIFGLSNPFYGLG----DTMLESR-SYQESQLPALPSAvppdVRQVVKDLLQRDPN 296

                 ....
gi 442620344 265 HRLS 268
Cdd:cd14018  297 KRVS 300
SH3_CACNB3 cd12042
Src Homology 3 domain of Voltage-dependent L-type calcium channel subunit beta3; The beta3 ...
582-648 5.15e-07

Src Homology 3 domain of Voltage-dependent L-type calcium channel subunit beta3; The beta3 subunit of voltage-dependent calcium channels (Ca(V)s) is one of four beta subunits present in vertebrates. It is the main beta subunit present in smooth muscles and is strongly expressed in the brain; it is predominant in the olfactory bulb, cortex, and hippocampus. It may play a role in regulating the NMDAR (N-methyl-d-aspartate receptor) activity in the hippocampus and thus, activity-dependent synaptic plasticity and cognitive behaviors. Ca(V)s are multi-protein complexes that regulate the entry of calcium into cells. They impact muscle contraction, neuronal migration, hormone and neurotransmitter release, and the activation of calcium-dependent signaling pathways. They are composed of four subunits: alpha1, alpha2delta, beta, and gamma. The beta subunit is a soluble and intracellular protein that interacts with the transmembrane alpha1 subunit. It facilitates the trafficking and proper localization of the alpha1 subunit to the cellular plasma membrane. Vertebrates contain four different beta subunits from distinct genes (beta1-4); each exists as multiple splice variants. All are expressed in the brain while other tissues show more specific expression patterns. The beta subunits show similarity to MAGUK (membrane-associated guanylate kinase) proteins in that they contain SH3 and inactive guanylate kinase (GuK) domains; however, they do not appear to contain a PDZ domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212975  Cd Length: 68  Bit Score: 47.71  E-value: 5.15e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620344 582 PCEIFVRAQFDYNPLDDELIPCAQAGISFQVGDILQIISKDDHHWWQARLDTVGGSAGLIPSPELQE 648
Cdd:cd12042    2 PVAFAVRTNVSYCGALDEECPVQGAAINFEAKDFLHIKEKYSNDWWIGRLVKEGGDIAFIPSPQRLE 68
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
32-223 5.22e-07

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 52.27  E-value: 5.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  32 RESNQQFAVKIVDVAKFTASPGLST----------------ADLKREATICHMLKHPHIVELLETysSEGMLYMVFEFME 95
Cdd:cd14067   14 RYQGQPVAVKRFHIKKCKKRTDGSAdtmlkhlraadamknfSEFRQEASMLHSLQHPCIVYLIGI--SIHPLCFALELAP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  96 GSDLCFEVVRRAVA------GFVYSEAVAchymRQILEALRYCHENDILHRDVRPACALLATVD--NSAPVKLGGFGSai 167
Cdd:cd14067   92 LGSLNTVLEENHKGssfmplGHMLTFKIA----YQIAAGLAYLHKKNIIFCDLKSDNILVWSLDvqEHINIKLSDYGI-- 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 168 qlpgTRETIE--THGRVGCPHYMAPEVVTRRLYGKGCDVWGAGVMLHVLLSGRLPFLG 223
Cdd:cd14067  166 ----SRQSFHegALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRPSLG 219
SH3_MyoIe_If_like cd11827
Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If ...
587-643 7.39e-07

Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If (MyoIf) are nonmuscle, unconventional, long tailed, class I myosins containing an N-terminal motor domain and a myosin tail with TH1, TH2, and SH3 domains. MyoIe interacts with the endocytic proteins, dynamin and synaptojanin-1, through its SH3 domain; it may play a role in clathrin-dependent endocytosis. In the kidney, MyoIe is critical for podocyte function and normal glomerular filtration. Mutations in MyoIe is associated with focal segmental glomerulosclerosis, a disease characterized by massive proteinuria and progression to end-stage kidney disease. MyoIf is predominantly expressed in the immune system; it plays a role in immune cell motility and innate immunity. Mutations in MyoIf may be associated with the loss of hearing. The MyoIf gene has also been found to be fused to the MLL (Mixed lineage leukemia) gene in infant acute myeloid leukemias (AML). SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212761 [Multi-domain]  Cd Length: 53  Bit Score: 46.64  E-value: 7.39e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 587 VRAQFDYNPLD-DELipcaqagiSFQVGDILQIISKDDHHWWQARLdtvGGSAGLIPS 643
Cdd:cd11827    2 CKALYAYDAQDtDEL--------SFNEGDIIEILKEDPSGWWTGRL---RGKEGLFPG 48
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
16-221 8.86e-07

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 51.51  E-value: 8.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRCIHRESNQqfavKIVDVAKFTASPGLSTA---DLKREATICHMLKHPHIVELLETYSSEGMLYMVFE 92
Cdd:cd05063   11 KVIGAGEFGEVFRGILKMPGR----KEVAVAIKTLKPGYTEKqrqDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  93 FMEGSDLCfEVVRRAVAGFVYSEAVAchYMRQILEALRYCHENDILHRDVRPACALlatVDNSAPVKLGGFGSAIQLPGT 172
Cdd:cd05063   87 YMENGALD-KYLRDHDGEFSSYQLVG--MLRGIAAGMKYLSDMNYVHRDLAARNIL---VNSNLECKVSDFGLSRVLEDD 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 442620344 173 RE-TIETHGRVGCPHYMAPEVVTRRLYGKGCDVWGAG-VMLHVLLSGRLPF 221
Cdd:cd05063  161 PEgTYTTSGGKIPIRWTAPEAIAYRKFTSASDVWSFGiVMWEVMSFGERPY 211
SH3_CACNB4 cd12043
Src Homology 3 domain of Voltage-dependent L-type calcium channel subunit beta4; The beta4 ...
582-644 9.38e-07

Src Homology 3 domain of Voltage-dependent L-type calcium channel subunit beta4; The beta4 subunit of voltage-dependent calcium channels (Ca(V)s) is one of four beta subunits present in vertebrates. It is the only beta subunit expressed in the cochlea and is highly expressed in the brain, predominantly in the cerebellum. Ca(V)s are multi-protein complexes that regulate the entry of calcium into cells. They impact muscle contraction, neuronal migration, hormone and neurotransmitter release, and the activation of calcium-dependent signaling pathways. They are composed of four subunits: alpha1, alpha2delta, beta, and gamma. The beta subunit is a soluble and intracellular protein that interacts with the transmembrane alpha1 subunit. It facilitates the trafficking and proper localization of the alpha1 subunit to the cellular plasma membrane. Vertebrates contain four different beta subunits from distinct genes (beta1-4); each exists as multiple splice variants. All are expressed in the brain while other tissues show more specific expression patterns. The beta subunits show similarity to MAGUK (membrane-associated guanylate kinase) proteins in that they contain SH3 and inactive guanylate kinase (GuK) domains; however, they do not appear to contain a PDZ domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212976  Cd Length: 68  Bit Score: 46.90  E-value: 9.38e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620344 582 PCEIFVRAQFDYNPLDDELIPCAQAGISFQVGDILQIISKDDHHWWQARLDTVGGSAGLIPSP 644
Cdd:cd12043    2 PVAFAVRTNVSYCGALDEDVPVPGTAISFDAKDFLHIKEKYNNDWWIGRLVKEGCEIGFIPSP 64
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
16-211 9.45e-07

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 51.53  E-value: 9.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  16 EVIGKGPFSIVRRC----IHRESNQQFAVK-------IVDVAKFTASPGLST-ADLKREATICHMLKHPHIVELLETYSS 83
Cdd:cd05095   11 EKLGEGQFGEVHLCeaegMEKFMDKDFALEvsenqpvLVAVKMLRADANKNArNDFLKEIKIMSRLKDPNIIRLLAVCIT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  84 EGMLYMVFEFMEGSDLCFEVVRRAVAGFVYSEAVA--------CHYMRQILEALRYCHENDILHRDVRPACALlatVDNS 155
Cdd:cd05095   91 DDPLCMITEYMENGDLNQFLSRQQPEGQLALPSNAltvsysdlRFMAAQIASGMKYLSSLNFVHRDLATRNCL---VGKN 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620344 156 APVKLGGFGSAIQL-PGTRETIEthGRVGCP-HYMAPEVVTRRLYGKGCDVWGAGVML 211
Cdd:cd05095  168 YTIKIADFGMSRNLySGDYYRIQ--GRAVLPiRWMSWESILLGKFTTASDVWAFGVTL 223
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
57-274 9.45e-07

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 51.26  E-value: 9.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344  57 ADLKREATICHMLKHPHIVELLETYSSEGMLYMVFEFMEGSD-LCF----EVVRRAVAGFVYSEAVA--------CHYmr 123
Cdd:cd05044   44 AEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELMEGGDlLSYlraaRPTAFTPPLLTLKDLLSicvdvakgCVY-- 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 124 qiLEALRYchendiLHRDVrPACALLATVDNSAP--VKLGGFGSAIQLPgTRETIETHGRVGCP-HYMAPEVVTRRLYGK 200
Cdd:cd05044  122 --LEDMHF------VHRDL-AARNCLVSSKDYRErvVKIGDFGLARDIY-KNDYYRKEGEGLLPvRWMAPESLVDGVFTT 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620344 201 GCDVWGAGVML-HVLLSGRLPFLG-SGVRLQQSV-ARGRLsfEAPEwksisaNAKD----LVMKMLAANPHHRLSITEVL 273
Cdd:cd05044  192 QSDVWAFGVLMwEILTLGQQPYPArNNLEVLHFVrAGGRL--DQPD------NCPDdlyeLMLRCWSTDPEERPSFARIL 263

                 .
gi 442620344 274 D 274
Cdd:cd05044  264 E 264
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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