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Conserved domains on  [gi|548961101|ref|NP_001271434|]
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peripheral plasma membrane protein CASK isoform 3 [Mus musculus]

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 ...
8-307 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: 618.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGML 87
Cdd:cd14094    1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGML 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAI 167
Cdd:cd14094   81 YMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISE 247
Cdd:cd14094  161 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISE 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 248 SAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGA 307
Cdd:cd14094  241 SAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRIHLPETVEQLRKFNARRKLKGA 300
Guanylate_kin pfam00625
Guanylate kinase;
732-905 6.79e-74

Guanylate kinase;


:

Pssm-ID: 395500  Cd Length: 182  Bit Score: 240.36  E-value: 6.79e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  732 KRKTLVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYG 811
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  812 TKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTItPGLNE------DESLQRLQKESDVLQRTYAHY-F 884
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSL-KVLQRrlkgrgKEQEEKINKRMAAAEQEFQHYeF 159
                         170       180
                  ....*....|....*....|.
gi 548961101  885 DLTIINNEIDETIRHLEEAVE 905
Cdd:pfam00625 160 DVIIVNDDLEEAYKKLKEALE 180
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
483-563 1.35e-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: 186.15  E-value: 1.35e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 483 RLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIV 562
Cdd:cd10831    1 RLVQFQKNTDEPMGITLKMNEDGRCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREARGSITFKIV 80

                 .
gi 548961101 563 P 563
Cdd:cd10831   81 P 81
SH3_CASK cd12081
Src Homology 3 domain of Calcium/calmodulin-dependent Serine protein Kinase; CASK is a ...
610-671 1.50e-38

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: 137.34  E-value: 1.50e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 610 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPEL 671
Cdd:cd12081    1 YVRAQFEYDPLKDDLIPCKQAGIRFRVGDILQIISKDDHNWWQAKLENSKNGTAGLIPSPEL 62
L27 pfam02828
L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.
400-450 3.00e-14

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


:

Pssm-ID: 460717  Cd Length: 52  Bit Score: 67.84  E-value: 3.00e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 548961101  400 VQRAKEVLEEISCYPE-NNDAKELKRILTQPHFMALLQTHDVVAHEVYSDEA 450
Cdd:pfam02828   1 VELVLELLEDLQPLSEaSEDLAELQKLLQSPHLQALLEAHDKVAQKVYEPPS 52
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
342-395 1.29e-10

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


:

Pssm-ID: 197794  Cd Length: 53  Bit Score: 57.52  E-value: 1.29e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 548961101   342 SQVLDSLEEIHALTDCSEkDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNP 395
Cdd:smart00569   1 QRLLELLEELQSLLSPSE-DLQELRRLLQSPHLQALLKIHDKVAETELDPPLPE 53
 
Name Accession Description Interval E-value
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
8-307 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: 618.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGML 87
Cdd:cd14094    1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGML 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAI 167
Cdd:cd14094   81 YMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISE 247
Cdd:cd14094  161 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISE 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 248 SAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGA 307
Cdd:cd14094  241 SAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRIHLPETVEQLRKFNARRKLKGA 300
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-276 1.33e-96

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 303.68  E-value: 1.33e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101    12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDR----ERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101    92 EFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 171
Cdd:smart00220  77 EYCEGGDLFDLLKKRG----RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH---VKLADFGLARQLDP 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   172 SGLvAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG--TKERLFEGIIKGKYKMNPRQWShISESA 249
Cdd:smart00220 150 GEK-LTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGddQLLELFKKIGKPKPPFPPPEWD-ISPEA 227
                          250       260
                   ....*....|....*....|....*..
gi 548961101   250 KDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:smart00220 228 KDLIRKLLVKDPEKRLTAEEALQHPFF 254
Guanylate_kin pfam00625
Guanylate kinase;
732-905 6.79e-74

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 240.36  E-value: 6.79e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  732 KRKTLVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYG 811
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  812 TKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTItPGLNE------DESLQRLQKESDVLQRTYAHY-F 884
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSL-KVLQRrlkgrgKEQEEKINKRMAAAEQEFQHYeF 159
                         170       180
                  ....*....|....*....|.
gi 548961101  885 DLTIINNEIDETIRHLEEAVE 905
Cdd:pfam00625 160 DVIIVNDDLEEAYKKLKEALE 180
Pkinase pfam00069
Protein kinase domain;
12-276 1.87e-65

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 218.65  E-value: 1.87e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKK---KDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   92 EFMDGADLcFEIVKRadaGFVYSEAVASHYMRQILEALRYCHDNNIihrdvkphcvllaskensapvklggfgvaiqlge 171
Cdd:pfam00069  78 EYVEGGSL-FDLLSE---KGAFSEREAKFIMKQILEGLESGSSLTT---------------------------------- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  172 sglvaggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYkMNPRQWSHISESAK 250
Cdd:pfam00069 120 -------FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNeIYELIIDQPY-AFPELPSNLSEEAK 191
                         250       260
                  ....*....|....*....|....*.
gi 548961101  251 DLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:pfam00069 192 DLLKKLLKKDPSKRLTATQALQHPWF 217
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
742-908 2.70e-59

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: 200.21  E-value: 2.70e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   742 HGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLETIRKIH 821
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   822 EQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTITPGLNE-----DESLQRLQKESDVLQRTYAHY--FDLTIINNEID 894
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRlrqrgTETSERIQKRLAAAQKEAQEYhlFDYVIVNDDLE 160
                          170
                   ....*....|....
gi 548961101   895 ETIRHLEEAVELVC 908
Cdd:smart00072 161 DAYEELKEILEAEQ 174
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
483-563 1.35e-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: 186.15  E-value: 1.35e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 483 RLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIV 562
Cdd:cd10831    1 RLVQFQKNTDEPMGITLKMNEDGRCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREARGSITFKIV 80

                 .
gi 548961101 563 P 563
Cdd:cd10831   81 P 81
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
12-264 4.82e-53

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 192.92  E-value: 4.82e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvAKFTSSPGLStEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLR-PELAADPEAR-ERFRREARALARLNHPNIVRVYDVGEEDGRPYLVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 171
Cdd:COG0515   87 EYVEGESLA-DLLRRRGP---LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGR---VKLIDFGIARALGG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGL-VAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISESA 249
Cdd:COG0515  160 ATLtQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGdSPAELLRAHLREPPPPPSELRPDLPPAL 239
                        250
                 ....*....|....*
gi 548961101 250 KDLVRRMLMLDPAER 264
Cdd:COG0515  240 DAIVLRALAKDPEER 254
SH3_CASK cd12081
Src Homology 3 domain of Calcium/calmodulin-dependent Serine protein Kinase; CASK is a ...
610-671 1.50e-38

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: 137.34  E-value: 1.50e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 610 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPEL 671
Cdd:cd12081    1 YVRAQFEYDPLKDDLIPCKQAGIRFRVGDILQIISKDDHNWWQAKLENSKNGTAGLIPSPEL 62
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
12-294 1.57e-37

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 143.80  E-value: 1.57e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIV---DVAKFTSspglsTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLkkrEILKMKQ-----VQHVAQEKSILMELSHPFIVNMMCSFQDENRVY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQ 168
Cdd:PTZ00263  95 FLLEFVVGGEL-FTHLRKAGR---FPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGH---VKVTDFGFAKK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnPRqWshISE 247
Cdd:PTZ00263 168 VPDRTFTL---CGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDdTPFRIYEKILAGRLKF-PN-W--FDG 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 548961101 248 SAKDLVRRMLMLDPAERI-----TVYEALNHPWLKERD---RYAYKIHLPETVEQ 294
Cdd:PTZ00263 241 RARDLVKGLLQTDHTKRLgtlkgGVADVKNHPYFHGANwdkLYARYYPAPIPVRV 295
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
736-904 8.22e-30

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: 116.44  E-value: 8.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  736 LVLLGAHGVGRRHIKNTLITKHPDrFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLE 815
Cdd:TIGR03263   3 IVISGPSGAGKSTLVKALLEEDPN-LKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTPKS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  816 TIRKIHEQGLIAILDVEPQ-ALKVLRTAEFAPFvVFIAAPTItpglneDESLQRLQK-----ESDVLQR--------TYA 881
Cdd:TIGR03263  82 PVEEALAAGKDVLLEIDVQgARQVKKKFPDAVS-IFILPPSL------EELERRLRKrgtdsEEVIERRlakakkeiAHA 154
                         170       180
                  ....*....|....*....|...
gi 548961101  882 HYFDLTIINNEIDETIRHLEEAV 904
Cdd:TIGR03263 155 DEFDYVIVNDDLEKAVEELKSII 177
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
736-901 5.25e-28

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: 109.93  E-value: 5.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 736 LVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLE 815
Cdd:cd00071    2 IVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSKA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 816 TIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPtitpglnedeslqrlqkesdvlqrtyahyfDLTIINNEIDE 895
Cdd:cd00071   82 AVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP------------------------------DYVIVNDDLEK 131

                 ....*.
gi 548961101 896 TIRHLE 901
Cdd:cd00071  132 AYEELK 137
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
736-905 1.55e-27

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 110.54  E-value: 1.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 736 LVLLGAHGVGRRHIKNTLITKHPDrFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLE 815
Cdd:COG0194    5 IVLSGPSGAGKTTLVKALLERDPD-LRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGTPKA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 816 TIRKIHEQGLIAILDVEPQ-ALKVLRTAEFAPFvVFIAAPTItpglneDESLQRL----QKESDVLQR---------TYA 881
Cdd:COG0194   84 EVEEALAAGKDVLLEIDVQgARQVKKKFPDAVS-IFILPPSL------EELERRLrgrgTDSEEVIERrlakareelAHA 156
                        170       180
                 ....*....|....*....|....
gi 548961101 882 HYFDLTIINNEIDETIRHLEEAVE 905
Cdd:COG0194  157 DEFDYVVVNDDLDRAVEELKAIIR 180
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
12-221 1.96e-24

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 108.73  E-value: 1.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRR--CI--NRETgqqfAVKIVD---------VAKFtsspglstedlKREA----SichmLKHPHI 74
Cdd:NF033483   9 YEIGERIGRGGMAEVYLakDTrlDRDV----AVKVLRpdlardpefVARF-----------RREAqsaaS----LSHPNI 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  75 VELLETYSSDGMLYMVFEFMDGADLcFEIVkRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeN 154
Cdd:NF033483  70 VSVYDVGEDGGIPYIVMEYVDGRTL-KDYI-REHGPLSPEEAV--EIMIQILSALEHAHRNGIVHRDIKPQNILIT---K 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101 155 SAPVKLGGFGVAIQLGESGLVAGGRV-GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 221
Cdd:NF033483 143 DGRVKVTDFGIARALSSTTMTQTNSVlGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDG 210
gmk PRK00300
guanylate kinase; Provisional
736-901 4.29e-24

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 100.93  E-value: 4.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 736 LVLLGAHGVGrrhiKNTLIT---KHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGT 812
Cdd:PRK00300   8 IVLSGPSGAG----KSTLVKallERDPNLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYYGT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 813 KLETIRKIHEQGLIAILDVEPQ-ALKVLRTAEFAPFvVFIAAPTItpglneDESLQRLQK---ES-DVLQR--------- 878
Cdd:PRK00300  84 PRSPVEEALAAGKDVLLEIDWQgARQVKKKMPDAVS-IFILPPSL------EELERRLRGrgtDSeEVIARrlakareei 156
                        170       180
                 ....*....|....*....|...
gi 548961101 879 TYAHYFDLTIINNEIDETIRHLE 901
Cdd:PRK00300 157 AHASEYDYVIVNDDLDTALEELK 179
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
33-296 8.91e-21

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 98.76  E-value: 8.91e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101    33 ETGQQFAVKIV---------DVAKFtsspglstedlKREASICHMLKHPHIVELLET-YSSDGMLYMVFEFMDGADLcfe 102
Cdd:TIGR03903    1 MTGHEVAIKLLrtdapeeehQRARF-----------RRETALCARLYHPNIVALLDSgEAPPGLLFAVFEYVPGRTL--- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   103 iVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGR--- 179
Cdd:TIGR03903   67 -REVLAADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIGTLLPGVRDADVATltr 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   180 ----VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG--TKERLFEGIIKGKYKMNPRQWSHiseSAKDLV 253
Cdd:TIGR03903  146 ttevLGTPTYCAPEQLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGasVAEILYQQLSPVDVSLPPWIAGH---PLGQVL 222
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 548961101   254 RRMLMLDPAERitvyeALNHPWLKERDRyayKIHLPETVEQLR 296
Cdd:TIGR03903  223 RKALNKDPRQR-----AASAPALAERFR---ALELCALVGILR 257
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
484-561 3.23e-17

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 76.94  E-value: 3.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  484 LVQFQKNTDEPMGITLKMNELNH---CIVARIMHGGMIHRQGtLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFK 560
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGdpgIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                  .
gi 548961101  561 I 561
Cdd:pfam00595  80 I 80
L27 pfam02828
L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.
400-450 3.00e-14

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


Pssm-ID: 460717  Cd Length: 52  Bit Score: 67.84  E-value: 3.00e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 548961101  400 VQRAKEVLEEISCYPE-NNDAKELKRILTQPHFMALLQTHDVVAHEVYSDEA 450
Cdd:pfam02828   1 VELVLELLEDLQPLSEaSEDLAELQKLLQSPHLQALLEAHDKVAQKVYEPPS 52
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
481-563 1.25e-13

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: 67.02  E-value: 1.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   481 RVRLVQFQKNTdEPMGITLKMN--ELNHCIVARIMHGGMIHRQGtLHVGDEIREINGISVANQTVEQLQKMLREMRGSIT 558
Cdd:smart00228   1 EPRLVELEKGG-GGLGFSLVGGkdEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVT 78

                   ....*
gi 548961101   559 FKIVP 563
Cdd:smart00228  79 LTVLR 83
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
401-449 2.78e-12

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


Pssm-ID: 197794  Cd Length: 53  Bit Score: 62.14  E-value: 2.78e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 548961101   401 QRAKEVLEEISCYPE-NNDAKELKRILTQPHFMALLQTHDVVAHEVYSDE 449
Cdd:smart00569   1 QRLLELLEELQSLLSpSEDLQELRRLLQSPHLQALLKIHDKVAETELDPP 50
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
610-668 1.97e-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: 1.97e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101   610 YVRAQFEYDPAKDDlipckeaGIRFRVGDIIQIISKDDHNWWQGKLensKNGTAGLIPS 668
Cdd:smart00326   4 QVRALYDYTAQDPD-------ELSFKKGDIITVLEKSDDGWWKGRL---GRGKEGLFPS 52
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
342-395 1.29e-10

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


Pssm-ID: 197794  Cd Length: 53  Bit Score: 57.52  E-value: 1.29e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 548961101   342 SQVLDSLEEIHALTDCSEkDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNP 395
Cdd:smart00569   1 QRLLELLEELQSLLSPSE-DLQELRRLLQSPHLQALLKIHDKVAETELDPPLPE 53
L27 pfam02828
L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.
341-388 3.76e-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: 53.20  E-value: 3.76e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 548961101  341 VSQVLDSLEEIHALTDCSEkDLDFLHSVFQDQHLHTLLDLYDKINTKS 388
Cdd:pfam02828   1 VELVLELLEDLQPLSEASE-DLAELQKLLQSPHLQALLEAHDKVAQKV 47
 
Name Accession Description Interval E-value
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
8-307 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: 618.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGML 87
Cdd:cd14094    1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGML 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAI 167
Cdd:cd14094   81 YMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISE 247
Cdd:cd14094  161 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISE 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 248 SAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGA 307
Cdd:cd14094  241 SAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRIHLPETVEQLRKFNARRKLKGA 300
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
11-275 1.64e-122

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: 371.81  E-value: 1.64e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSE---DEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLCFEIVKRadagFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLG 170
Cdd:cd05117   78 MELCTGGELFDRIVKK----GSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFGLAKIFE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 EsGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISESA 249
Cdd:cd05117  154 E-GEKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGeTEQELFEKILKGKYSFDSPEWKNVSEEA 232
                        250       260
                 ....*....|....*....|....*.
gi 548961101 250 KDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd05117  233 KDLIKRLLVVDPKKRLTAAEALNHPW 258
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-307 1.94e-117

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: 359.81  E-value: 1.94e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd14086    1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSAR---DHQKLEREARICRLLKHPNIVRLHDSISEEGFHYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQL 169
Cdd:cd14086   78 VFDLVTGGELFEDIVARE----FYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT-KERLFEGIIKGKYKMNPRQWSHISES 248
Cdd:cd14086  154 QGDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEdQHRLYAQIKAGAYDYPSPEWDTVTPE 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGA 307
Cdd:cd14086  234 AKDLINQMLTVNPAKRITAAEALKHPWICQRDRVASMVHRQETVDCLKKFNARRKLKGA 292
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-276 1.33e-96

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 303.68  E-value: 1.33e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101    12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDR----ERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101    92 EFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 171
Cdd:smart00220  77 EYCEGGDLFDLLKKRG----RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH---VKLADFGLARQLDP 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   172 SGLvAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG--TKERLFEGIIKGKYKMNPRQWShISESA 249
Cdd:smart00220 150 GEK-LTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGddQLLELFKKIGKPKPPFPPPEWD-ISPEA 227
                          250       260
                   ....*....|....*....|....*..
gi 548961101   250 KDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:smart00220 228 KDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
12-275 1.41e-79

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: 258.22  E-value: 1.41e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14003    2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEE---IEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLgE 171
Cdd:cd14003   79 EYASGGEL-FDYIVNNGR---LSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGN---LKIIDFGLSNEF-R 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMnprqWSHISESA 249
Cdd:cd14003  151 GGSLLKTFCGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSkLFRKILKGKYPI----PSHLSPDA 226
                        250       260
                 ....*....|....*....|....*.
gi 548961101 250 KDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd14003  227 RDLIRRMLVVDPSKRITIEEILNHPW 252
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
8-276 6.80e-75

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: 246.50  E-value: 6.80e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDL---KREASICHML-KHPHIVELLETYSS 83
Cdd:cd14093    1 FYAKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSENEAEELReatRREIEILRQVsGHPNIIELHDVFES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLYMVFEFMDGADLcF----EIVKradagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVK 159
Cdd:cd14093   81 PTFIFLVFELCRKGEL-FdyltEVVT-------LSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLN---VK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 160 LGGFGVAIQLGEsGLVAGGRVGTPHFMAPEVVKR------EPYGKPVDVWGCGVILFILLSGCLPFYGTKERL-FEGIIK 232
Cdd:cd14093  150 ISDFGFATRLDE-GEKLRELCGTPGYLAPEVLKCsmydnaPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVmLRNIME 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 548961101 233 GKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14093  229 GKYEFGSPEWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
Guanylate_kin pfam00625
Guanylate kinase;
732-905 6.79e-74

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 240.36  E-value: 6.79e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  732 KRKTLVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYG 811
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  812 TKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTItPGLNE------DESLQRLQKESDVLQRTYAHY-F 884
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSL-KVLQRrlkgrgKEQEEKINKRMAAAEQEFQHYeF 159
                         170       180
                  ....*....|....*....|.
gi 548961101  885 DLTIINNEIDETIRHLEEAVE 905
Cdd:pfam00625 160 DVIIVNDDLEEAYKKLKEALE 180
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
12-310 2.79e-70

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: 234.84  E-value: 2.79e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFtsspglsteDLKREASIchMLK---HPHIVELLETYSSDGMLY 88
Cdd:cd14091    2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKR---------DPSEEIEI--LLRygqHPNIITLRDVYDDGNSVY 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAP-VKLGGFGVAI 167
Cdd:cd14091   71 LVTELLRGGELLDRILRQKF----FSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDPEsLRICDFGFAK 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QL-GESGLVAggrvgTPH----FMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF-YG---TKERLFEGIIKGKYKMN 238
Cdd:cd14091  147 QLrAENGLLM-----TPCytanFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFaSGpndTPEVILARIGSGKIDLS 221
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 239 PRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDryaykiHLPETveQLRKFNARRKLKGAVLA 310
Cdd:cd14091  222 GGNWDHVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRD------SLPQR--QLTDPQDAALVKGAVAA 285
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
9-275 7.37e-70

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: 232.26  E-value: 7.37e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakfTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd14083    2 RDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCID----KKALKGKEDSLENEIAVLRKIKHPNIVQLLDIYESKSHLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAiQ 168
Cdd:cd14083   78 LVMELVTGGELFDRIVEKG----SYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISDFGLS-K 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAGGrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQWSHISE 247
Cdd:cd14083  153 MEDSGVMSTA-CGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDsKLFAQILKAEYEFDSPYWDDISD 231
                        250       260
                 ....*....|....*....|....*...
gi 548961101 248 SAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd14083  232 SAKDFIRHLMEKDPNKRYTCEQALEHPW 259
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
8-276 1.99e-68

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: 229.20  E-value: 1.99e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTS---SPGLSTEDLKREASICHMLKHPHIVELLETYSSD 84
Cdd:cd14084    4 LRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIgsrREINKPRNIETEIEILKKLSHPCIIKIEDFFDAE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  85 GMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFG 164
Cdd:cd14084   84 DDYYIVLELMEGGELFDRVVSNK----RLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECLIKITDFG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 165 VAIQLGESGLVAGgRVGTPHFMAPEVVK---REPYGKPVDVWGCGVILFILLSGCLPFYG--TKERLFEGIIKGKYKMNP 239
Cdd:cd14084  160 LSKILGETSLMKT-LCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEeyTQMSLKEQILSGKYTFIP 238
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 548961101 240 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14084  239 KAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
8-313 1.72e-66

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: 224.32  E-value: 1.72e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglSTEDLK---REASICHMLKHPHIVELLETYSSD 84
Cdd:cd14085    1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLK----------KTVDKKivrTEIGVLLRLSHPNIIKLKEIFETP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  85 GMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFG 164
Cdd:cd14085   71 TEISLVLELVTGGELFDRIVEKG----YYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 165 VAiQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG--TKERLFEGIIKGKYKMNPRQW 242
Cdd:cd14085  147 LS-KIVDQQVTMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDerGDQYMFKRILNCDYDFVSPWW 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548961101 243 SHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDryAYKIHLPETVEQLRKFNARRKLKGAVLAAVS 313
Cdd:cd14085  226 DDVSLNAKDLVKKLIVLDPKKRLTTQQALQHPWVTGKA--ANFAHMDTAQKKLQEFNARRKLKAAVKAVVA 294
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
12-275 1.42e-65

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: 220.66  E-value: 1.42e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLstedLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14095    2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHM----IENEVAILRRVKHPNIVQLIEEYDTDTELYLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEN-SAPVKLGGFGVAIQLG 170
Cdd:cd14095   78 ELVKGGDL-FDAITSSTK---FTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDgSKSLKLADFGLATEVK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY---GTKERLFEGIIKGKYKMNPRQWSHISE 247
Cdd:cd14095  154 EPLFTV---CGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRspdRDQEELFDLILAGEFEFLSPYWDNISD 230
                        250       260
                 ....*....|....*....|....*...
gi 548961101 248 SAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd14095  231 SAKDLISRMLVVDPEKRYSAGQVLDHPW 258
Pkinase pfam00069
Protein kinase domain;
12-276 1.87e-65

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 218.65  E-value: 1.87e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKK---KDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   92 EFMDGADLcFEIVKRadaGFVYSEAVASHYMRQILEALRYCHDNNIihrdvkphcvllaskensapvklggfgvaiqlge 171
Cdd:pfam00069  78 EYVEGGSL-FDLLSE---KGAFSEREAKFIMKQILEGLESGSSLTT---------------------------------- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  172 sglvaggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYkMNPRQWSHISESAK 250
Cdd:pfam00069 120 -------FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNeIYELIIDQPY-AFPELPSNLSEEAK 191
                         250       260
                  ....*....|....*....|....*.
gi 548961101  251 DLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:pfam00069 192 DLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
18-275 1.68e-64

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: 217.14  E-value: 1.68e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAvkivdvAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFA------AKFIPKRDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLCFEIVKRadagFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGFGVAIQLGEsGLVAG 177
Cdd:cd14006   75 ELLDRLAER----GSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQ-IKIIDFGLARKLNP-GEELK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 178 GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRM 256
Cdd:cd14006  149 EIFGTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGeDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKL 228
                        250
                 ....*....|....*....
gi 548961101 257 LMLDPAERITVYEALNHPW 275
Cdd:cd14006  229 LVKEPRKRPTAQEALQHPW 247
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
11-276 6.15e-64

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: 215.97  E-value: 6.15e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKF-TSSPGLSTEdlkREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd14081    2 PYRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLsKESVLMKVE---REIAIMKLIEHPNVLKLYDVYENKKYLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVA-IQ 168
Cdd:cd14081   79 VLEYVSGGELFDYLVKKG----RLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNN---IKIADFGMAsLQ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAGgrVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMnPrqwSHIS 246
Cdd:cd14081  152 PEGSLLETS--CGSPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRqLLEKVKRGVFHI-P---HFIS 225
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 247 ESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14081  226 PDAQDLLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
12-274 1.72e-63

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: 214.63  E-value: 1.72e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd08215    2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEK---EREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 171
Cdd:cd08215   79 EYADGGDLAQKIKKQKKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGV---VKLGDFGISKVLES 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNPRQWshiSESAK 250
Cdd:cd08215  156 TTDLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPaLVYKIVKGQYPPIPSQY---SSELR 232
                        250       260
                 ....*....|....*....|....
gi 548961101 251 DLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd08215  233 DLVNSMLQKDPEKRPSANEILSSP 256
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
18-276 6.47e-63

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: 213.57  E-value: 6.47e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVD---------VAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGM-- 86
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFNksrlrkrreGKNDRGKIKNALDDVRREIAIMKKLDHPNIVRLYEVIDDPESdk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 LYMVFEFMDGADLcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVA 166
Cdd:cd14008   81 LYLVLEYCEGGPV--MELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGT---VKISDFGVS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQLGESGLVAGGRVGTPHFMAPEV--VKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNPRqw 242
Cdd:cd14008  156 EMFEDGNDTLQKTAGTPAFLAPELcdGDSKTYsGKAADIWALGVTLYCLVFGRLPFNGDNILeLYEAIQNQNDEFPIP-- 233
                        250       260       270
                 ....*....|....*....|....*....|....
gi 548961101 243 SHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14008  234 PELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-303 1.73e-62

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: 213.32  E-value: 1.73e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakfTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd14166    3 ETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCI-----KKSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAiQL 169
Cdd:cd14166   78 VMQLVSGGELFDRILERG----VYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMITDFGLS-KM 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAGGrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISES 248
Cdd:cd14166  153 EQNGIMSTA-CGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEeTESRLFEKIKEGYYEFESPFWDDISES 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNHPWLK-----ERDRYaykihlPETVEQLRKFNARRK 303
Cdd:cd14166  232 AKDFIRHLLEKNPSKRYTCEKALSHPWIIgntalHRDIY------PSVSEQIQKNFAKSK 285
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
9-276 2.83e-62

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: 211.96  E-value: 2.83e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSP-GLSTEDLKREASICHMLKHPHIVELLETYSSDGML 87
Cdd:cd14105    4 EDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASRrGVSREDIEREVSILRQVLHPNIITLHDVFENKTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAP-VKLGGFGVA 166
Cdd:cd14105   84 VLILELVAGGEL-FDFLAEKES---LSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPIPrIKLIDFGLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHI 245
Cdd:cd14105  160 HKI-EDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGdTKQETLANITAVNYDFDDEYFSNT 238
                        250       260       270
                 ....*....|....*....|....*....|.
gi 548961101 246 SESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14105  239 SELAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
10-275 1.54e-61

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: 210.73  E-value: 1.54e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELC-EVIGKGPFSVVRRCINRETGQQFAVKIVDvakftSSPGLSTEDLKREASICHMLK-HPHIVELLETYSSDGML 87
Cdd:cd14090    1 DLYKLTgELLGEGAYASVQTCINLYTGKEYAVKIIE-----KHPGHSRSRVFREVETLHQCQgHPNILQLIEYFEDDERF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAi 167
Cdd:cd14090   76 YLVFEKMRGGPLLSHIEKRVH----FTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSPVKICDFDLG- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 qlgeSGLVAGGR-------------VGTPHFMAPEVV-----KREPYGKPVDVWGCGVILFILLSGCLPFYGT------- 222
Cdd:cd14090  151 ----SGIKLSSTsmtpvttpelltpVGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGRcgedcgw 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 223 ---------KERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd14090  227 drgeacqdcQELLFHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
8-276 2.05e-61

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: 209.83  E-value: 2.05e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftSSPGLSTEDLK-------REASICHMLK-HPHIVELLE 79
Cdd:cd14181    8 FYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEV----TAERLSPEQLEevrsstlKEIHILRQVSgHPSIITLID 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  80 TYSSDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVK 159
Cdd:cd14181   84 SYESSTFIFLVFDLMRRGELFDYLTEKV----TLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILL---DDQLHIK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 160 LGGFGVAIQLgESGLVAGGRVGTPHFMAPEVVK------REPYGKPVDVWGCGVILFILLSGCLPFYGTKERL-FEGIIK 232
Cdd:cd14181  157 LSDFGFSCHL-EPGEKLRELCGTPGYLAPEILKcsmdetHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLmLRMIME 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 548961101 233 GKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14181  236 GRYQFSSPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPFF 279
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
16-275 9.49e-61

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: 207.53  E-value: 9.49e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIV-DVAKftsspglstedLKREASIcHML--KHPHIVELLE----TYSSDGMLY 88
Cdd:cd14089    7 QVLGLGINGKVLECFHKKTGEKFALKVLrDNPK-----------ARREVEL-HWRasGCPHIVRIIDvyenTYQGRKCLL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLCFEIVKRADAGFVYSEAvaSHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQ 168
Cdd:cd14089   75 VVMECMEGGELFSRIQERADSAFTEREA--AEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTDFGFAKE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAGGRVgTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY---------GTKERlfegIIKGKYKMNP 239
Cdd:cd14089  153 TTTKKSLQTPCY-TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYsnhglaispGMKKR----IRNGQYEFPN 227
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 548961101 240 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd14089  228 PEWSNVSEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
18-276 2.46e-60

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: 205.92  E-value: 2.46e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglsTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKD-----REDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLcFEIVkrADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKeNSAPVKLGGFGVAIQLGESGLVag 177
Cdd:cd14103   76 EL-FERV--VDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSR-TGNQIKIIDFGLARKYDPDKKL-- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 178 gRV--GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISESAKDLVR 254
Cdd:cd14103  150 -KVlfGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGdNDAETLANVTRAKWDFDDEAFDDISDEAKDFIS 228
                        250       260
                 ....*....|....*....|..
gi 548961101 255 RMLMLDPAERITVYEALNHPWL 276
Cdd:cd14103  229 KLLVKDPRKRMSAAQCLQHPWL 250
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
16-276 3.53e-60

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: 205.83  E-value: 3.53e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 95
Cdd:cd06606    6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEE---ELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESGLV 175
Cdd:cd06606   83 GGSLA-SLLKKFGK---LPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGV---VKLADFGCAKRLAEIATG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 176 AGGR--VGTPHFMAPEVVKREPYGKPVDVW--GCGVILfiLLSGCLPFYGTKER---LFEgIIKGKYKmnPRQWSHISES 248
Cdd:cd06606  156 EGTKslRGTPYWMAPEVIRGEGYGRAADIWslGCTVIE--MATGKPPWSELGNPvaaLFK-IGSSGEP--PPIPEHLSEE 230
                        250       260
                 ....*....|....*....|....*...
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd06606  231 AKDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
12-275 1.28e-59

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: 204.18  E-value: 1.28e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpGLsTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14663    2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVARE-GM-VEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcFEIVKradAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIqLGE 171
Cdd:cd14663   80 ELVTGGEL-FSKIA---KNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGN---LKISDFGLSA-LSE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAG---GRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnPRqwsHIS 246
Cdd:cd14663  152 QFRQDGllhTTCGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFDDENlMALYRKIMKGEFEY-PR---WFS 227
                        250       260
                 ....*....|....*....|....*....
gi 548961101 247 ESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd14663  228 PGAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-276 1.41e-59

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: 204.11  E-value: 1.41e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGlsteDLKREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd14167    3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKET----SIENEIAVLHKIKHPNIVALDDIYESGGHLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLCFEIVKRadaGFvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAiQL 169
Cdd:cd14167   79 IMQLVSGGELFDRIVEK---GF-YTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSKIMISDFGLS-KI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQWSHISES 248
Cdd:cd14167  154 EGSGSVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDaKLFEQILKAEYEFDSPYWDDISDS 233
                        250       260
                 ....*....|....*....|....*...
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14167  234 AKDFIQHLMEKDPEKRFTCEQALQHPWI 261
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
742-908 2.70e-59

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: 200.21  E-value: 2.70e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   742 HGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLETIRKIH 821
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   822 EQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTITPGLNE-----DESLQRLQKESDVLQRTYAHY--FDLTIINNEID 894
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRlrqrgTETSERIQKRLAAAQKEAQEYhlFDYVIVNDDLE 160
                          170
                   ....*....|....
gi 548961101   895 ETIRHLEEAVELVC 908
Cdd:smart00072 161 DAYEELKEILEAEQ 174
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
12-277 4.82e-59

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: 202.32  E-value: 4.82e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpGLStEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14007    2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKS-GLE-HQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcFEIVKRADagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 171
Cdd:cd14007   80 EYAPNGEL-YKELKKQK---RFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGE---LKLADFGWSVHAPS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnprqWSHISESAK 250
Cdd:cd14007  153 NRRKT--FCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESkSHQETYKRIQNVDIKF----PSSVSPEAK 226
                        250       260
                 ....*....|....*....|....*..
gi 548961101 251 DLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd14007  227 DLISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
18-275 1.04e-57

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: 198.60  E-value: 1.04e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKK---LQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLCFEIVKRadagFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLvAG 177
Cdd:cd14009   78 DLSQYIRKR----GRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVLKIADFGFARSLQPASM-AE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 178 GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNPRQWSHISESAKDLVRRM 256
Cdd:cd14009  153 TLCGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVqLLRNIERSDAVIPFPIAAQLSPDCKDLLRRL 232
                        250
                 ....*....|....*....
gi 548961101 257 LMLDPAERITVYEALNHPW 275
Cdd:cd14009  233 LRRDPAERISFEEFFAHPF 251
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
10-276 4.74e-57

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: 197.04  E-value: 4.74e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAvkivdvAKFTSSPGLSTEDL-KREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd14114    2 DHYDILEELGTGAFGVVHRCTERATGNNFA------AKFIMTPHESDKETvRKEIQIMNQLHHPKLINLHDAFEDDNEMV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLcFEivKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnSAPVKLGGFGVAIQ 168
Cdd:cd14114   76 LILEFLSGGEL-FE--RIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKR-SNEVKLIDFGLATH 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQWSHISE 247
Cdd:cd14114  152 LDPKESVK-VTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDdETLRNVKSCDWNFDDSAFSGISE 230
                        250       260
                 ....*....|....*....|....*....
gi 548961101 248 SAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14114  231 EAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
12-275 4.78e-57

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: 197.09  E-value: 4.78e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEDL-KREASICHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd14185    2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGK-----EDMiESEILIIKSLSHPNIVKLFEVYETEKEIYLI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEN-SAPVKLGGFGVAIQL 169
Cdd:cd14185   77 LEYVRGGDLFDAIIESVK----FTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDkSTTLKLADFGLAKYV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG---TKERLFEGIIKGKYKMNPRQWSHIS 246
Cdd:cd14185  153 TGPIFTV---CGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSperDQEELFQIIQLGHYEFLPPYWDNIS 229
                        250       260
                 ....*....|....*....|....*....
gi 548961101 247 ESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd14185  230 EAAKDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
12-275 1.18e-56

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: 196.16  E-value: 1.18e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGlSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14098    2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDK-NLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIvkrADAGFVySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSAPVKLGGFGVA-IQLG 170
Cdd:cd14098   81 EYVEGGDLMDFI---MAWGAI-PEQHARELTKQILEAMAYTHSMGITHRDLKPENILI-TQDDPVIVKISDFGLAkVIHT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAggRVGTPHFMAPEVVK----REP--YGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWS 243
Cdd:cd14098  156 GTFLVT--FCGTMAYLAPEILMskeqNLQggYSNLVDMWSVGCLVYVMLTGALPFDGsSQLPVEKRIRKGRYTQPPLVDF 233
                        250       260       270
                 ....*....|....*....|....*....|..
gi 548961101 244 HISESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd14098  234 NISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
8-281 2.54e-56

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: 196.75  E-value: 2.54e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYEL---CEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstedlkREASICHMLK-HPHIVELLETYSS 83
Cdd:cd14092    1 FFQNYELdlrEEALGDGSFSVCRKCVHKKTGQEFAVKIVSRRLDTS----------REVQLLRLCQgHPNIVKLHEVFQD 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGF 163
Cdd:cd14092   71 ELHTYLVMELLRGGELLERIRKKKR----FTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAEIKIVDF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 164 GVAIQLGESGLVAggrvgTP----HFMAPEVVKREP----YGKPVDVWGCGVILFILLSGCLPFYGTKER-----LFEGI 230
Cdd:cd14092  147 GFARLKPENQPLK-----TPcftlPYAAPEVLKQALstqgYDESCDLWSLGVILYTMLSGQVPFQSPSRNesaaeIMKRI 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 548961101 231 IKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDR 281
Cdd:cd14092  222 KSGDFSFDGEEWKNVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSS 272
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
12-276 2.58e-56

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: 195.24  E-value: 2.58e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14069    3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKR---APGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcFEIVKrADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQL-- 169
Cdd:cd14069   80 EYASGGEL-FDKIE-PDVGM--PEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDN---LKISDFGLATVFry 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 -GESGLVaGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKER--LFEGIIKGKyKMNPRQWSHI 245
Cdd:cd14069  153 kGKERLL-NKMCGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELPWDQPSDScqEYSDWKENK-KTYLTPWKKI 230
                        250       260       270
                 ....*....|....*....|....*....|.
gi 548961101 246 SESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14069  231 DTAALSLLRKILTENPNKRITIEDIKKHPWY 261
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
9-276 3.60e-56

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: 194.85  E-value: 3.60e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSP-GLSTEDLKREASICHMLKHPHIVELLETYSSDGML 87
Cdd:cd14194    4 DDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRrGVSREDIEREVSILKEIQHPNVITLHEVYENKTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAP-VKLGGFGVA 166
Cdd:cd14194   84 ILILELVAGGEL-FDFLAEKES---LTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPrIKIIDFGLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHI 245
Cdd:cd14194  160 HKI-DFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGdTKQETLANVSAVNYEFEDEYFSNT 238
                        250       260       270
                 ....*....|....*....|....*....|.
gi 548961101 246 SESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14194  239 SALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
9-276 5.75e-56

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: 194.40  E-value: 5.75e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSP-GLSTEDLKREASICHMLKHPHIVELLETYSSDGML 87
Cdd:cd14196    4 EDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrGVSREEIEREVSILRQVLHPNIITLHDVYENRTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAP-VKLGGFGVA 166
Cdd:cd14196   84 VLILELVSGGEL-FDFLAQKES---LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPhIKLIDFGLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHI 245
Cdd:cd14196  160 HEI-EDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGdTKQETLANITAVSYDFDEEFFSHT 238
                        250       260       270
                 ....*....|....*....|....*....|.
gi 548961101 246 SESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14196  239 SELAKDFIRKLLVKETRKRLTIQEALRHPWI 269
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
483-563 1.35e-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: 186.15  E-value: 1.35e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 483 RLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIV 562
Cdd:cd10831    1 RLVQFQKNTDEPMGITLKMNEDGRCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREARGSITFKIV 80

                 .
gi 548961101 563 P 563
Cdd:cd10831   81 P 81
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
18-274 1.88e-55

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: 190.94  E-value: 1.88e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLL----EELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLcFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESG--LV 175
Cdd:cd00180   77 SL-KDLLKENKGPL--SEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGT---VKLADFGLAKDLDSDDslLK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 176 AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILlsgclpfygtkerlfegiikgkykmnprqwshisESAKDLVRR 255
Cdd:cd00180  151 TTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL----------------------------------EELKDLIRR 196
                        250
                 ....*....|....*....
gi 548961101 256 MLMLDPAERITVYEALNHP 274
Cdd:cd00180  197 MLQYDPKKRPSAKELLEHL 215
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
9-277 3.76e-55

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: 192.14  E-value: 3.76e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSP-GLSTEDLKREASICHMLKHPHIVELLETYSSDGML 87
Cdd:cd14195    4 EDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRrGVSREEIEREVNILREIQHPNIITLHDIFENKTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAP-VKLGGFGVA 166
Cdd:cd14195   84 VLILELVSGGEL-FDFLAEKES---LTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPrIKLIDFGIA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHI 245
Cdd:cd14195  160 HKI-EAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGeTKQETLTNISAVNYDFDEEYFSNT 238
                        250       260       270
                 ....*....|....*....|....*....|..
gi 548961101 246 SESAKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd14195  239 SELAKDFIRRLLVKDPKKRMTIAQSLEHSWIK 270
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
10-314 4.26e-55

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: 192.93  E-value: 4.26e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvaKFTSSPGLSTEDLKREAsichmlKHPHIVELLETYSSDGMLYM 89
Cdd:cd14175    1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVID--KSKRDPSEEIEILLRYG------QHPNIITLKDVYDDGKHVYL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE-NSAPVKLGGFGVAIQ 168
Cdd:cd14175   73 VTELMRGGELLDKILRQK----FFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESgNPESLRICDFGFAKQ 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 L-GESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG----TKERLFEGIIKGKYKMNPRQWS 243
Cdd:cd14175  149 LrAENGLLMT-PCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANgpsdTPEEILTRIGSGKFTLSGGNWN 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548961101 244 HISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRyaykihLPETveQLRKFNARRkLKGAVLAAVSS 314
Cdd:cd14175  228 TVSDAAKDLVSKMLHVDPHQRLTAKQVLQHPWITQKDK------LPQS--QLNHQDVQL-VKGAMAATYSA 289
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
12-271 5.40e-55

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: 191.26  E-value: 5.40e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkfTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14014    2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPE--LAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 171
Cdd:cd14014   80 EYVEGGSL-ADLLRERGP---LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGR---VKLTDFGIARALGD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGL-VAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQW-SHISESA 249
Cdd:cd14014  153 SGLtQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLnPDVPPAL 232
                        250       260
                 ....*....|....*....|..
gi 548961101 250 KDLVRRMLMLDPAERITVYEAL 271
Cdd:cd14014  233 DAIILRALAKDPEERPQSAAEL 254
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
12-276 8.35e-55

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: 190.56  E-value: 8.35e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14079    4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLD--MEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVaiqlge 171
Cdd:cd14079   82 EYVSGGELFDYIVQKGR----LSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMN---VKIADFGL------ 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGR-----VGTPHFMAPEVVKREPYGKP-VDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnPrqwSH 244
Cdd:cd14079  149 SNIMRDGEflktsCGSPNYAAPEVISGKLYAGPeVDVWSCGVILYALLCGSLPFDDEHiPNLFKKIKSGIYTI-P---SH 224
                        250       260       270
                 ....*....|....*....|....*....|..
gi 548961101 245 ISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14079  225 LSPGARDLIKRMLVVDPLKRITIPEIRQHPWF 256
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
10-275 2.50e-54

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: 189.47  E-value: 2.50e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLstedLKREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd14184    1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHL----IENEVSILRRVKHPNIIMLIEEMDTPAELYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEN-SAPVKLGGFGVAIQ 168
Cdd:cd14184   77 VMELVKGGDL-FDAITSSTK---YTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDgTKSLKLGDFGLATV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LgESGLVAggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT---KERLFEGIIKGKYKMNPRQWSHI 245
Cdd:cd14184  153 V-EGPLYT--VCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSEnnlQEDLFDQILLGKLEFPSPYWDNI 229
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 246 SESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd14184  230 TDSAKELISHMLQVNVEARYTAEQILSHPW 259
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
12-276 5.70e-54

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: 188.51  E-value: 5.70e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakfTSSPGlsTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14087    3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIE----TKCRG--REVCESELNVLRRVRHTNIIQLIEVFETKERVYMVM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQL-- 169
Cdd:cd14087   77 ELATGGELFDRIIAKGS----FTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIMITDFGLASTRkk 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISES 248
Cdd:cd14087  153 GPNCLMKT-TCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDdNRTRLYRQILRAKYSYSGEPWPSVSNL 231
                        250       260
                 ....*....|....*....|....*...
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14087  232 AKDFIDRLLTVNPGERLSATQALKHPWI 259
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
12-276 5.91e-54

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: 189.57  E-value: 5.91e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCI-NRETGQQFAVKIVDVAKFTSSPGLSTEDLK--REASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd14096    3 YRLINKIGEGAFSNVYKAVpLRNTGKPVAIKVVRKADLSSDNLKGSSRANilKEVQIMKRLSHPNIVKLLDFQESDEYYY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAS--------KENSAP--- 157
Cdd:cd14096   83 IVLELADGGEIFHQIVRLT----YFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivKLRKADdde 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 158 -------------------VKLGGFGVAIQLGESGLVAggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLP 218
Cdd:cd14096  159 tkvdegefipgvggggigiVKLADFGLSKQVWDSNTKT--PCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPP 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 219 FYG-TKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14096  237 FYDeSIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
8-276 1.80e-53

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: 187.17  E-value: 1.80e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYEL-CEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLK-HPHIVELLETYSSDG 85
Cdd:cd14106    5 INEVYTVeSTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQD---CRNEILHEIAVLELCKdCPRVVNLHEVYETRS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 MLYMVFEFMDGAdlcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGV 165
Cdd:cd14106   82 ELILILELAAGG----ELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGDIKLCDFGI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 166 AIQLGESGLVaggR--VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQW 242
Cdd:cd14106  158 SRVIGEGEEI---ReiLGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGdDKQETFLNISQCNLDFPEELF 234
                        250       260       270
                 ....*....|....*....|....*....|....
gi 548961101 243 SHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14106  235 KDVSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
8-278 2.01e-53

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: 187.43  E-value: 2.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakfTSSPGLSTEDLK--REASI--CHMLK----HPHIVELLE 79
Cdd:cd14182    1 FYEKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDI---TGGGSFSPEEVQelREATLkeIDILRkvsgHPNIIQLKD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  80 TYSSDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVK 159
Cdd:cd14182   78 TYETNTFFFLVFDLMKKGELFDYLTEKV----TLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMN---IK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 160 LGGFGVAIQLGEsGLVAGGRVGTPHFMAPEVVK------REPYGKPVDVWGCGVILFILLSGCLPFYGTKERL-FEGIIK 232
Cdd:cd14182  151 LTDFGFSCQLDP-GEKLREVCGTPGYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLmLRMIMS 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 548961101 233 GKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd14182  230 GNYQFGSPEWDDRSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQQ 275
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
12-264 4.82e-53

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 192.92  E-value: 4.82e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvAKFTSSPGLStEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLR-PELAADPEAR-ERFRREARALARLNHPNIVRVYDVGEEDGRPYLVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 171
Cdd:COG0515   87 EYVEGESLA-DLLRRRGP---LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGR---VKLIDFGIARALGG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGL-VAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISESA 249
Cdd:COG0515  160 ATLtQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGdSPAELLRAHLREPPPPPSELRPDLPPAL 239
                        250
                 ....*....|....*
gi 548961101 250 KDLVRRMLMLDPAER 264
Cdd:COG0515  240 DAIVLRALAKDPEER 254
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-276 9.56e-53

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: 185.48  E-value: 9.56e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLstedLKREASICHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd14169    4 VYELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAM----VENEIAVLRRINHENIVSLEDIYESPTHLYLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAiQLG 170
Cdd:cd14169   80 MELVTGGELFDRIIERGS----YTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFEDSKIMISDFGLS-KIE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAGGrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQWSHISESA 249
Cdd:cd14169  155 AQGMLSTA-CGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDsELFNQILKAEYEFDSPYWDDISESA 233
                        250       260
                 ....*....|....*....|....*..
gi 548961101 250 KDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14169  234 KDFIRHLLERDPEKRFTCEQALQHPWI 260
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
8-314 6.53e-52

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: 184.06  E-value: 6.53e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftSSPGLSTEDLKREAsichmlKHPHIVELLETYSSDGML 87
Cdd:cd14177    2 FTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSK--RDPSEEIEILMRYG------QHPNIITLKDVYDDGRYV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSA-PVKLGGFGVA 166
Cdd:cd14177   74 YLVTELMKGGELLDRILRQK----FFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANAdSIRICDFGFA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQL-GESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG----TKERLFEGIIKGKYKMNPRQ 241
Cdd:cd14177  150 KQLrGENGLLL-TPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANgpndTPEEILLRIGSGKFSLSGGN 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548961101 242 WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRyaykihLPEtvEQLRKFNARRKLKGAVLAAVSS 314
Cdd:cd14177  229 WDTVSDAAKDLLSHMLHVDPHQRYTAEQVLKHSWIACRDQ------LPH--YQLNRQDAPHLVKGAMAATYSA 293
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
8-318 8.02e-52

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: 185.22  E-value: 8.02e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftSSPGLSTEDLKREAsichmlKHPHIVELLETYSSDGML 87
Cdd:cd14176   17 FTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK--RDPTEEIEILLRYG------QHPNIITLKDVYDDGKYV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE-NSAPVKLGGFGVA 166
Cdd:cd14176   89 YVVTELMKGGELLDKILRQK----FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgNPESIRICDFGFA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQL-GESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG----TKERLFEGIIKGKYKMNPRQ 241
Cdd:cd14176  165 KQLrAENGLLMT-PCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANgpddTPEEILARIGSGKFSLSGGY 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548961101 242 WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRyaykihLPETveQLRKFNARRKLKGAVLAAVSSHKFN 318
Cdd:cd14176  244 WNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQ------LPQY--QLNRQDAPHLVKGAMAATYSALNRN 312
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
18-275 9.26e-52

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: 181.95  E-value: 9.26e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEV--EHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLCFEIVKRadagFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESGLVAG 177
Cdd:cd05123   79 ELFSHLSKE----GRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGH---IKLTDFGLAKELSSDGDRTY 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 178 GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnPrqwSHISESAKDLVRRM 256
Cdd:cd05123  152 TFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAeNRKEIYEKILKSPLKF-P---EYVSPEAKSLISGL 227
                        250       260
                 ....*....|....*....|..
gi 548961101 257 LMLDPAERIT---VYEALNHPW 275
Cdd:cd05123  228 LQKDPTKRLGsggAEEIKAHPF 249
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
8-280 1.12e-51

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: 183.29  E-value: 1.12e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftSSPGLSTEDLKREAsichmlKHPHIVELLETYSSDGML 87
Cdd:cd14178    1 FTDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSK--RDPSEEIEILLRYG------QHPNIITLKDVYDDGKFV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE-NSAPVKLGGFGVA 166
Cdd:cd14178   73 YLVMELMRGGELLDRILRQK----CFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESgNPESIRICDFGFA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQL-GESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG----TKERLFEGIIKGKYKMNPRQ 241
Cdd:cd14178  149 KQLrAENGLLMT-PCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANgpddTPEEILARIGSGKYALSGGN 227
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 548961101 242 WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERD 280
Cdd:cd14178  228 WDSISDAAKDIVSKMLHVDPHQRLTAPQVLRHPWIVNRE 266
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
11-277 1.14e-51

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: 181.64  E-value: 1.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspgLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd06614    1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRK------QNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLCfEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLG 170
Cdd:cd06614   75 MEYMDGGSLT-DIITQNPVRM--NESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGS---VKLADFGFAAQLT 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEGIIKGKYKM-NPRQWSHise 247
Cdd:cd06614  149 KEKSKRNSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPplRALFLITTKGIPPLkNPEKWSP--- 225
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 248 SAKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd06614  226 EFKDFLNKCLVKDPEKRPSAEELLQHPFLK 255
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
11-276 1.40e-51

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: 181.63  E-value: 1.40e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEDLKREASICHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKK-----ESILNEIAILKKCKHPNIVKYYGSYLKKDELWIV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLcFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQLg 170
Cdd:cd05122   76 MEFCSGGSL-KDLLKNTNKTL--TEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSD---GEVKLIDFGLSAQL- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY--GTKERLFEGIIKGKYKM-NPRQWshiSE 247
Cdd:cd05122  149 SDGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSelPPMKALFLIATNGPPGLrNPKKW---SK 225
                        250       260
                 ....*....|....*....|....*....
gi 548961101 248 SAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd05122  226 EFKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
9-307 8.08e-51

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: 181.01  E-value: 8.08e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglsTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd14168    9 KKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGK----ESSIENEIAVLRKIKHENIVALEDIYESPNHLY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLCFEIVKRadaGFvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQ 168
Cdd:cd14168   85 LVMQLVSGGELFDRIVEK---GF-YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMISDFGLSKM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGeSGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQWSHISE 247
Cdd:cd14168  161 EG-KGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDsKLFEQILKADYEFDSPYWDDISD 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548961101 248 SAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHlpETVE-QLRKFNARRKLKGA 307
Cdd:cd14168  240 SAKDFIRNLMEKDPNKRYTCEQALRHPWIAGDTALCKNIH--ESVSaQIRKNFAKSKWRQA 298
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
10-276 8.88e-50

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: 177.53  E-value: 8.88e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELC-EVIGKGPFSVVRRCINRETGQQFAVKIVDvakftSSPGLSTEDLKREASICHMLK-HPHIVELLETYSSDGML 87
Cdd:cd14173    1 DVYQLQeEVLGEGAYARVQTCINLITNKEYAVKIIE-----KRPGHSRSRVFREVEMLYQCQgHRNVLELIEFFEEEDKF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGF--GV 165
Cdd:cd14173   76 YLVFEKMRGGSILSHIHRRRH----FNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKICDFdlGS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 166 AIQL-GESGLVAGGRVGTP----HFMAPEVVKR-----EPYGKPVDVWGCGVILFILLSGCLPFYG-------------- 221
Cdd:cd14173  152 GIKLnSDCSPISTPELLTPcgsaEYMAPEVVEAfneeaSIYDKRCDLWSLGVILYIMLSGYPPFVGrcgsdcgwdrgeac 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 548961101 222 --TKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14173  232 paCQNMLFESIQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
12-276 1.45e-49

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: 176.06  E-value: 1.45e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTsspGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14074    5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLD---DVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLGGFGVAIQLgE 171
Cdd:cd14074   82 ELGDGGDM-YDYIMKHENGL--NEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGL--VKLTDFGFSNKF-Q 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKP-VDVWGCGVILFILLSGCLPFY--GTKERLFEgIIKGKYKMNPrqwsHISES 248
Cdd:cd14074  156 PGEKLETSCGSLAYSAPEILLGDEYDAPaVDIWSLGVILYMLVCGQPPFQeaNDSETLTM-IMDCKYTVPA----HVSPE 230
                        250       260
                 ....*....|....*....|....*...
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14074  231 CKDLIRRMLIRDPKKRASLEEIENHPWL 258
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
12-275 2.38e-49

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: 175.87  E-value: 2.38e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvAKFtsspgLSTED----LKREASICHMLKHPHIVELLETYSSDGML 87
Cdd:cd05581    3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLD-KRH-----IIKEKkvkyVTIEKEVLSRLAHPGIVKLYYTFQDESKL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAI 167
Cdd:cd05581   77 YFVLEYAPNGDLLEYIRKYGS----LDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMH---IKITDFGTAK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGESGLVAGGR-----------------VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERL-FEG 229
Cdd:cd05581  150 VLGPDSSPESTKgdadsqiaynqaraasfVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLtFQK 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 548961101 230 IIKGKYKMNPrqwsHISESAKDLVRRMLMLDPAERITV-----YEAL-NHPW 275
Cdd:cd05581  230 IVKLEYEFPE----NFPPDAKDLIQKLLVLDPSKRLGVnenggYDELkAHPF 277
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
10-276 2.61e-49

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: 175.56  E-value: 2.61e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELC-EVIGKGPFSVVRRCINRETGQQFAVKIVdvakfTSSPGLSTE-DLKREASIChmlkhPHIVELLETYS----S 83
Cdd:cd14172    3 DDYKLSkQVLGLGVNGKVLECFHRRTGQKCALKLL-----YDSPKARREvEHHWRASGG-----PHIVHILDVYEnmhhG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLYMVFEFMDGADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGF 163
Cdd:cd14172   73 KRCLLIIMECMEGGELFSRIQERGDQAF--TEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVLKLTDF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 164 GVAIQLGESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY---------GTKERlfegIIKGK 234
Cdd:cd14172  151 GFAKETTVQNALQ-TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYsntgqaispGMKRR----IRMGQ 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 548961101 235 YKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14172  226 YGFPNPEWAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
12-276 5.50e-49

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: 173.96  E-value: 5.50e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftSSPGLSTEDLKREASI----CHMLKHPHIVELLE--TYSSDG 85
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKI------KNDFRHPKAALREIKLlkhlNDVEGHPNIVKLLDvfEHRGGN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 MLYMVFEFMdGADLCfEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLasKENSAPVKLGGFGV 165
Cdd:cd05118   75 HLCLVFELM-GMNLY-ELIKDYPRGL--PLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILI--NLELGQLKLADFGL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 166 AIQLGESGLVagGRVGTPHFMAPEVVKR-EPYGKPVDVWGCGVILFILLSGclpfygtkERLFEGiikgkyKMNPRQWSH 244
Cdd:cd05118  149 ARSFTSPPYT--PYVATRWYRAPEVLLGaKPYGSSIDIWSLGCILAELLTG--------RPLFPG------DSEVDQLAK 212
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 548961101 245 I-----SESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd05118  213 IvrllgTPEALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
10-277 6.47e-49

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: 175.22  E-value: 6.47e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELC-EVIGKGPFSVVRRCINRETGQQFAVKIVDvakftSSPGLSTEDLKREASICHMLK-HPHIVELLETYSSDGML 87
Cdd:cd14174    1 DLYRLTdELLGEGAYAKVQGCVSLQNGKEYAVKIIE-----KNAGHSRSRVFREVETLYQCQgNKNILELIEFFEDDTRF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGF--GV 165
Cdd:cd14174   76 YLVFEKLRGGSILAHIQKRKH----FNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSPVKICDFdlGS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 166 AIQLGESGL-VAGGRVGTP----HFMAPEVV-----KREPYGKPVDVWGCGVILFILLSGCLPFYGT------------- 222
Cdd:cd14174  152 GVKLNSACTpITTPELTTPcgsaEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwdrgevc 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101 223 ---KERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd14174  232 rvcQNKLFESIQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
12-276 1.75e-48

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: 173.14  E-value: 1.75e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRC--INRETGQQFAVKIVDVAKftSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd14080    2 YRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKKK--APKDFLEKFLPRELEILRKLRHPNIIQVYSIFERGSKVFI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLcFEIVKRAdaGFVySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQL 169
Cdd:cd14080   80 FMEYAEHGDL-LEYIQKR--GAL-SESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNN---VKLSDFGFARLC 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GEsglvAGGRV------GTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMNPRQ 241
Cdd:cd14080  153 PD----DDGDVlsktfcGSAAYAAPEILQGIPYdPKKYDIWSLGVILYIMLCGSMPFDDSNiKKMLKDQQNRKVRFPSSV 228
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 548961101 242 WsHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14080  229 K-KLSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
10-278 6.96e-48

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: 171.72  E-value: 6.96e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLstedLKREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd14183    6 ERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHM----IQNEVSILRRVKHPNIVLLIEEMDMPTELYL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLL-ASKENSAPVKLGGFGVAIq 168
Cdd:cd14183   82 VMELVKGGDL-FDAITSTNK---YTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyEHQDGSKSLKLGDFGLAT- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 lgesglVAGGRV----GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT---KERLFEGIIKGKYKMNPRQ 241
Cdd:cd14183  157 ------VVDGPLytvcGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSgddQEVLFDQILMGQVDFPSPY 230
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 548961101 242 WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd14183  231 WDNVSDSAKELITMMLQVDVDQRYSALQVLEHPWVND 267
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
10-276 1.03e-47

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: 170.98  E-value: 1.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTEDL-KREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd14088    1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCK-----KFLKRDGRKVRKAaKNEINILKMVKHPNILQLVDVFETRKEYF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLcFEIVkrADAGFvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQ 168
Cdd:cd14088   76 IFLELATGREV-FDWI--LDQGY-YSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSKIVISDFHLAKL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 lgESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE---------RLFEGIIKGKYKMNP 239
Cdd:cd14088  152 --ENGLIKE-PCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEeddyenhdkNLFRKILAGDYEFDS 228
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 548961101 240 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14088  229 PYWDDISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
18-280 1.35e-47

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: 170.86  E-value: 1.35e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpgLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd05579    1 ISRGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRK--NQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DL--------CFEivkradagfvysEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGvaiqL 169
Cdd:cd05579   79 DLysllenvgALD------------EDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDA---NGHLKLTDFG----L 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAGGR-------------------VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEG 229
Cdd:cd05579  140 SKVGLVRRQIklsiqkksngapekedrriVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAeTPEEIFQN 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 548961101 230 IIKGKYkmNPRQWSHISESAKDLVRRMLMLDPAERI---TVYEALNHPWLKERD 280
Cdd:cd05579  220 ILNGKI--EWPEDPEVSDEAKDLISKLLTPDPEKRLgakGIEEIKNHPFFKGID 271
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
12-276 1.94e-47

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: 170.74  E-value: 1.94e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIV--DVAK--FTSSpglstedLKREASICHMLKHPHIVELLETYSSDGML 87
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIrlDNEEegIPST-------ALREISLLKELKHPNIVKLLDVIHTENKL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDgADLcFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAI 167
Cdd:cd07829   74 YLVFEYCD-QDL-KKYLDKRPGPL--PPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGV---LKLADFGLAR 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGESGLVAGGRVGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFE-----------GI 230
Cdd:cd07829  147 AFGIPLRTYTHEVVTLWYRAPEILLGSKhYSTAVDIWSVGCIFAELITGKPLFPGDSEidqlfKIFQilgtpteeswpGV 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 548961101 231 IK-GKYKMNPRQWSH---------ISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd07829  227 TKlPDYKPTFPKWPKndlekvlprLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
18-276 2.34e-47

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: 170.72  E-value: 2.34e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVdvakfTSSPGLSTEDLkreasiCHML--KHPHIVELLETYSSD----------G 85
Cdd:cd14171   14 LGTGISGPVRVCVKKSTGERFALKIL-----LDRPKARTEVR------LHMMcsGHPNIVQIYDVYANSvqfpgessprA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 MLYMVFEFMDGADLCFEIVKRAdaGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGV 165
Cdd:cd14171   83 RLLIVMELMEGGELFDRISQHR--HF--TEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAPIKLCDFGF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 166 AiqlgesgLVAGGRVGTPHF----MAPEVV------KRE-----------PYGKPVDVWGCGVILFILLSGCLPFYGT-- 222
Cdd:cd14171  159 A-------KVDQGDLMTPQFtpyyVAPQVLeaqrrhRKErsgiptsptpyTYDKSCDMWSLGVIIYIMLCGYPPFYSEhp 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101 223 ----KERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14171  232 srtiTKDMKRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
12-276 3.26e-47

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: 169.27  E-value: 3.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14099    3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTK--PKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EfmdgadLC-----FEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVA 166
Cdd:cd14099   81 E------LCsngslMELLKRRKA---LTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMN---VKIGDFGLA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQLGESGLVAGGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRqwSH 244
Cdd:cd14099  149 ARLEYDGERKKTLCGTPNYIAPEVLeKKKGHSFEVDIWSLGVILYTLLVGKPPFETsDVKETYKRIKKNEYSFPSH--LS 226
                        250       260       270
                 ....*....|....*....|....*....|..
gi 548961101 245 ISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14099  227 ISDEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
12-276 3.41e-47

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: 169.55  E-value: 3.41e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakFTSSPGLSTEDLK-------------REASICHMLKHPHIVELL 78
Cdd:cd14077    3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIP---RASNAGLKKEREKrlekeisrdirtiREAALSSLLNHPHICRLR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  79 ETYSSDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapV 158
Cdd:cd14077   80 DFLRTPNHYYMLFEYVDGGQLLDYIISHGK----LKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGN---I 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 159 KLggfgvaIQLGESGLVAGGRV-----GTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGII 231
Cdd:cd14077  153 KI------IDFGLSNLYDPRRLlrtfcGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENmPALHAKIK 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 548961101 232 KGKYKMNprqwSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14077  227 KGKVEYP----SYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
11-276 6.45e-47

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: 168.17  E-value: 6.45e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd06627    1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKS---DLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYII 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLG 170
Cdd:cd06627   78 LEYVENGSLA-SIIKKFGK---FPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGL---VKLADFGVATKLN 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVW--GCGVILfiLLSGCLPFYGTK--ERLFEgIIKGKYkmnPRQWSHIS 246
Cdd:cd06627  151 EVEKDENSVVGTPYWMAPEVIEMSGVTTASDIWsvGCTVIE--LLTGNPPYYDLQpmAALFR-IVQDDH---PPLPENIS 224
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 247 ESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd06627  225 PELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
11-276 7.12e-47

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: 168.50  E-value: 7.12e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd14097    2 IYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSS---AVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLCfEIVKRADagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASK--ENSAP--VKLGGFGVA 166
Cdd:cd14097   79 MELCEDGELK-ELLLRKG---FFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSiiDNNDKlnIKVTDFGLS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQ---LGESGLVAggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQW 242
Cdd:cd14097  155 VQkygLGEDMLQE--TCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAkSEEKLFEEIRKGDLTFTQSVW 232
                        250       260       270
                 ....*....|....*....|....*....|....
gi 548961101 243 SHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14097  233 QSVSDAAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
16-275 1.16e-46

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: 167.59  E-value: 1.16e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFtssPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 95
Cdd:cd14082    9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRF---PTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLcfEIVKRADAGFVySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLv 175
Cdd:cd14082   86 GDML--EMILSSEKGRL-PERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQVKLCDFGFARIIGEKSF- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 176 aggR---VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFyGTKERLFEGIIKGKYKMNPRQWSHISESAKDL 252
Cdd:cd14082  162 ---RrsvVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-NEDEDINDQIQNAAFMYPPNPWKEISPDAIDL 237
                        250       260
                 ....*....|....*....|...
gi 548961101 253 VRRMLMLDPAERITVYEALNHPW 275
Cdd:cd14082  238 INNLLQVKMRKRYSVDKSLSHPW 260
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
12-276 1.33e-46

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: 167.18  E-value: 1.33e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14071    2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEE---NLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAiQLGE 171
Cdd:cd14071   79 EYASNGEIFDYLAQHGR----MSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMN---IKIADFGFS-NFFK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKP-VDVWGCGVILFILLSGCLPFYGT-----KERLFEGIIKGKYKMnprqwshi 245
Cdd:cd14071  151 PGELLKTWCGSPPYAAPEVFEGKEYEGPqLDIWSLGVVLYVLVCGALPFDGStlqtlRDRVLSGRFRIPFFM-------- 222
                        250       260       270
                 ....*....|....*....|....*....|.
gi 548961101 246 SESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14071  223 STDCEHLIRRMLVLDPSKRLTIEQIKKHKWM 253
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
11-278 2.84e-46

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: 167.34  E-value: 2.84e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  11 VYELCEVIGKGPFSVVRRCINRETGQQFAvkivdvAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd14104    1 KYMIAEELGRGQFGIVHRCVETSSKKTYM------AKFVKVKGADQVLVKKEISILNIARHRNILRLHESFESHEELVMI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLcFEIVkrADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGFGVAIQLg 170
Cdd:cd14104   75 FEFISGVDI-FERI--TTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSY-IKIIEFGQSRQL- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISESA 249
Cdd:cd14104  150 KPGDKFRLQYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAeTNQQTIENIRNAEYAFDDEAFKNISIEA 229
                        250       260
                 ....*....|....*....|....*....
gi 548961101 250 KDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd14104  230 LDFVDRLLVKERKSRMTAQEALNHPWLKQ 258
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
8-277 7.33e-46

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: 167.36  E-value: 7.33e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELC---EVIGKGPFSVVRRCINRETGQQFAVKIVdvakftsSPGLSTEDLKREASICHMLKHPHIVELLETYSSD 84
Cdd:cd14180    1 FFQCYELDleePALGEGSFSVCRKCRHRQSGQEYAVKII-------SRRMEANTQREVAALRLCQSHPNIVALHEVLHDQ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  85 GMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFG 164
Cdd:cd14180   74 YHTYLVMELLRGGELLDRIKKKA----RFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGAVLKVIDFG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 165 VAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEG--------IIKGKYK 236
Cdd:cd14180  150 FARLRPQGSRPLQTPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKMFHNhaadimhkIKEGDFS 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 548961101 237 MNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd14180  230 LEGEAWKGVSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQ 270
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
12-276 8.35e-46

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: 165.25  E-value: 8.35e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTedLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVR--IRREIEIMSSLNHPHIIRIYEVFENKDKIVIVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAiQLGE 171
Cdd:cd14073   81 EYASGGELYDYISERR----RLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGN---AKIADFGLS-NLYS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYkmnpRQWSHISEsA 249
Cdd:cd14073  153 KDKLLQTFCGSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDfKRLVKQISSGDY----REPTQPSD-A 227
                        250       260
                 ....*....|....*....|....*..
gi 548961101 250 KDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14073  228 SGLIRWMLTVNPKRRATIEDIANHWWV 254
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
18-276 2.74e-45

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: 163.58  E-value: 2.74e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGlSTEDLKREASICHMLKHPHIVELLETYSSD--GMLYMVFEFMD 95
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRIPN-GEANVKREIQILRRLNHRNVIKLVDVLYNEekQKLYMVMEYCV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GAdLCFEIVKRADAGFVYSEAvaSHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLgeSGLV 175
Cdd:cd14119   80 GG-LQEMLDSAPDKRLPIWQA--HGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGT---LKISDFGVAEAL--DLFA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 176 AGGRV----GTPHFMAPEVVKREPY--GKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPrqwsHISES 248
Cdd:cd14119  152 EDDTCttsqGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIyKLFENIGKGEYTIPD----DVDPD 227
                        250       260
                 ....*....|....*....|....*...
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14119  228 LQDLLRGMLEKDPEKRFTIEQIRQHPWF 255
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
9-276 4.40e-45

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: 163.32  E-value: 4.40e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTsspglstEDL---KREASICHMLKHPHIVELLETYSSDG 85
Cdd:cd14078    2 LKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALG-------DDLprvKTEIEALKNLSHQHICRLYHVIETDN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 MLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGv 165
Cdd:cd14078   75 KIFMVLEYCPGGELFDYIVAKDR----LSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQN---LKLIDFG- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 166 aiqlgesgLVA---GGR-------VGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKG 233
Cdd:cd14078  147 --------LCAkpkGGMdhhletcCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNvMALYRKIQSG 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 548961101 234 KYKmNPRqWshISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14078  219 KYE-EPE-W--LSPSSKLLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
12-276 1.21e-44

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: 161.92  E-value: 1.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14072    2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPS---SLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRADAgfvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQlge 171
Cdd:cd14072   79 EYASGGEVFDYLVAHGRM----KEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMN---IKIADFGFSNE--- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 sgLVAGGRV----GTPHFMAPEVVKREPYGKP-VDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnPrqwSHI 245
Cdd:cd14072  149 --FTPGNKLdtfcGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGqNLKELRERVLRGKYRI-P---FYM 222
                        250       260       270
                 ....*....|....*....|....*....|.
gi 548961101 246 SESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14072  223 STDCENLLKKFLVLNPSKRGTLEQIMKDRWM 253
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
16-278 2.28e-44

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: 162.90  E-value: 2.28e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDvakftSSPGLSTE-DLKREASIChmlkhPHIVELLETY----SSDGMLYMV 90
Cdd:cd14170    8 QVLGLGINGKVLQIFNKRTQEKFALKMLQ-----DCPKARREvELHWRASQC-----PHIVRIVDVYenlyAGRKCLLIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLG 170
Cdd:cd14170   78 MECLDGGELFSRIQDRGDQAF--TEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY---------GTKERlfegIIKGKYKMNPRQ 241
Cdd:cd14170  156 SHNSLTT-PCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYsnhglaispGMKTR----IRMGQYEFPNPE 230
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 548961101 242 WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd14170  231 WSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQ 267
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
17-280 3.63e-44

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: 160.84  E-value: 3.63e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKIVdvaKFTSSPgLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDG 96
Cdd:cd06623    8 VLGQGSSGVVYKVRHKPTGKIYALKKI---HVDGDE-EFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  97 ADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCH-DNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESGLV 175
Cdd:cd06623   84 GSLA-DLLKKVGK---IPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLLINSKGE---VKIADFGISKVLENTLDQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 176 AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER----LFEGIIKG-KYKMNPRQWshiSESAK 250
Cdd:cd06623  157 CNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPsffeLMQAICDGpPPSLPAEEF---SPEFR 233
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 251 DLVRRMLMLDPAERITVYEALNHPWLKERD 280
Cdd:cd06623  234 DFISACLQKDPKKRPSAAELLQHPFIKKAD 263
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
12-276 5.56e-44

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: 160.95  E-value: 5.56e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPglSTEDLK----REASICHMLKHPHIVELLETYSSDGML 87
Cdd:cd07833    3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIK-----KFKESE--DDEDVKktalREVKVLRQLRHENIVNLKEAFRRKGRL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLcfEIVKRADAGFVYsEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLasKENSApVKLGGFGVAI 167
Cdd:cd07833   76 YLVFEYVERTLL--ELLEASPGGLPP-DAVRS-YIWQLLQAIAYCHSHNIIHRDIKPENILV--SESGV-LKLCDFGFAR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGESGLVA-GGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE--RLFEgIIKGKYKMNPRQW- 242
Cdd:cd07833  149 ALTARPASPlTDYVATRWYRAPELlVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDidQLYL-IQKCLGPLPPSHQe 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548961101 243 ----------------SHI-----------SESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd07833  228 lfssnprfagvafpepSQPeslerrypgkvSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
10-276 1.00e-43

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: 158.95  E-value: 1.00e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKivdvakFTSSPGLSTED---LKREASICHMLKHPHIVELLETYSSDGM 86
Cdd:cd14002    1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALK------FIPKRGKSEKElrnLRQEIEILRKLNHPNIIEMLDSFETKKE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 LYMVFEFMDGaDLcFEIVkrADAGfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVA 166
Cdd:cd14002   75 FVVVTEYAQG-EL-FQIL--EDDG-TLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKG---GVVKLCDFGFA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKgkykmNPRQW-SH 244
Cdd:cd14002  147 RAMSCNTLVLTSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSiYQLVQMIVK-----DPVKWpSN 221
                        250       260       270
                 ....*....|....*....|....*....|..
gi 548961101 245 ISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14002  222 MSPEFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
PDZ_MPP1-like cd10830
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 ...
483-563 1.44e-43

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: 152.33  E-value: 1.44e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 483 RLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIV 562
Cdd:cd10830    1 RLVQFEKNTEEPMGITLKLNEKQSCIVARILHGGMIHRQGSLHVGDEILEINGKSVTNHSVDQLQKMLKETKGMVSLKVI 80

                 .
gi 548961101 563 P 563
Cdd:cd10830   81 P 81
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-274 2.27e-43

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: 158.47  E-value: 2.27e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETY--SSDGMLYM 89
Cdd:cd08217    2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEK---EKQQLVSEVNILRELKHPNIVRYYDRIvdRANTTLYI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLCfEIVKRADAGFVY-SEAVASHYMRQILEALRYCHDNN-----IIHRDVKPHCVLLASKENsapVKLGGF 163
Cdd:cd08217   79 VMEYCEGGDLA-QLIKKCKKENQYiPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNN---VKLGDF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 164 GVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYkmnPRQW 242
Cdd:cd08217  155 GLARVLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANqLELAKKIKEGKF---PRIP 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 548961101 243 SHISESAKDLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd08217  232 SRYSSELNEVIKSMLNVDPDKRPSVEELLQLP 263
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
12-276 2.45e-43

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: 158.19  E-value: 2.45e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd05578    2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKD--SVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLgE 171
Cdd:cd05578   80 DLLLGGDLRYHLQQKV----KFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILL---DEQGHVHITDFNIATKL-T 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKD 251
Cdd:cd05578  152 DGTLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRAKFETASVLYPAGWSEEAID 231
                        250       260
                 ....*....|....*....|....*.
gi 548961101 252 LVRRMLMLDPAERITVYEAL-NHPWL 276
Cdd:cd05578  232 LINKLLERDPQKRLGDLSDLkNHPYF 257
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
16-278 1.56e-42

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: 157.51  E-value: 1.56e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVdvakftsSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 95
Cdd:cd14179   13 KPLGEGSFSICRKCLHKKTNQEYAVKIV-------SKRMEANTQREIAALKLCEGHPNIVKLHEVYHDQLHTFLVMELLK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLcFEIVKRADagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLV 175
Cdd:cd14179   86 GGEL-LERIKKKQ---HFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSEIKIIDFGFARLKPPDNQP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 176 AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF--------YGTKERLFEGIIKGKYKMNPRQWSHISE 247
Cdd:cd14179  162 LKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFqchdksltCTSAEEIMKKIKQGDFSFEGEAWKNVSQ 241
                        250       260       270
                 ....*....|....*....|....*....|.
gi 548961101 248 SAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd14179  242 EAKDLIQGLLTVDPNKRIKMSGLRYNEWLQD 272
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
12-276 1.84e-42

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: 155.57  E-value: 1.84e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14075    4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQK---TQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQLgE 171
Cdd:cd14075   81 EYASGGELYTKISTEGK----LSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASN---NCVKVGDFGFSTHA-K 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnPrqwSHISESA 249
Cdd:cd14075  153 RGETLNTFCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRAeTVAKLKKCILEGTYTI-P---SYVSEPC 228
                        250       260
                 ....*....|....*....|....*..
gi 548961101 250 KDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14075  229 QELIRGILQPVPSDRYSIDEIKNSEWL 255
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
12-280 3.18e-42

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: 156.20  E-value: 3.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd05580    3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQV--EHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 171
Cdd:cd05580   81 EYVPGGEL-FSLLRRSGR---FPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGH---IKITDFGFAKRVKD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 sglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnPRqwsHISESAK 250
Cdd:cd05580  154 ---RTYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDeNPMKIYEKILEGKIRF-PS---FFDPDAK 226
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 548961101 251 DLVRRMLMLDPAERI-----TVYEALNHPWLKERD 280
Cdd:cd05580  227 DLIKRLLVVDLTKRLgnlknGVEDIKNHPWFAGID 261
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
8-276 3.74e-42

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: 154.59  E-value: 3.74e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCE-VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFtsspglstedLKREASICHMLKHPHIVELLETYSSDGM 86
Cdd:cd14109    1 VRELYEIGEeDEKRAAQGAPFHVTERSTGRNFLAQLRYGDPF----------LMREVDIHNSLDHPNIVQMHDAYDDEKL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 LYMVFEFMD-GADLCFEIVKRADAgfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnsapVKLGGFGV 165
Cdd:cd14109   71 AVTVIDNLAsTIELVRDNLLPGKD--YYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDDK----LKLADFGQ 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 166 AIQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNPRQWSH 244
Cdd:cd14109  145 SRRL-LRGKLTTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDReTLTNVRSGKWSFDSSPLGN 223
                        250       260       270
                 ....*....|....*....|....*....|..
gi 548961101 245 ISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14109  224 ISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
12-298 4.16e-42

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: 155.10  E-value: 4.16e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftSSPGLstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd06609    3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEE--AEDEI--EDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADlCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQLGE 171
Cdd:cd06609   79 EYCGGGS-VLDLLKPG----PLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLS---EEGDVKLADFGVSGQLTS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGcLPFYGTKER---LFEgIIKGKYKMNPRqwSHISES 248
Cdd:cd06609  151 TMSKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKG-EPPLSDLHPmrvLFL-IPKNNPPSLEG--NKFSKP 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYkihLPETVEQLRKF 298
Cdd:cd06609  227 FKDFVELCLNKDPKERPSAKELLKHKFIKKAKKTSY---LTLLIERIKKW 273
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
9-276 4.58e-42

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: 154.78  E-value: 4.58e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIvdvakFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd14191    1 SDFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKF-----FKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLCFEIVkraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGFGVAIQ 168
Cdd:cd14191   76 MVLEMVSGGELFERII---DEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTK-IKLIDFGLARR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQWSHISE 247
Cdd:cd14191  152 LENAGSLKV-LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDnETLANVTSATWDFDDEAFDEISD 230
                        250       260
                 ....*....|....*....|....*....
gi 548961101 248 SAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14191  231 DAKDFISNLLKKDMKARLTCTQCLQHPWL 259
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
7-276 8.66e-42

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: 154.32  E-value: 8.66e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   7 LFEDVYELC--EVIGKGPFSVVRRCINRETGQQFAVKIVdvAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSD 84
Cdd:cd14197    4 PFQERYSLSpgRELGRGKFAVVRKCVEKDSGKEFAAKFM--RKRRKGQDCRMEIIHEIAVLELAQANPWVINLHEVYETA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  85 GMLYMVFEFMDGADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFG 164
Cdd:cd14197   82 SEMILVLEYAAGGEIFNQCVADREEAF--KEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGDIKIVDFG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 165 VAIQLGESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT-KERLFEGIIKGKYKMNPRQWS 243
Cdd:cd14197  160 LSRILKNSEELR-EIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDdKQETFLNISQMNVSYSEEEFE 238
                        250       260       270
                 ....*....|....*....|....*....|...
gi 548961101 244 HISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14197  239 HLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
16-276 1.33e-41

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: 153.33  E-value: 1.33e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 95
Cdd:cd06632    6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGESGLv 175
Cdd:cd06632   86 GGSI-HKLLQRYGA---FEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILV---DTNGVVKLADFGMAKHVEAFSF- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 176 AGGRVGTPHFMAPEVVKRE--PYGKPVDVW--GCGVILfiLLSGCLPFYGtkerlFEG---IIK-GKYKMNPRQWSHISE 247
Cdd:cd06632  158 AKSFKGSPYWMAPEVIMQKnsGYGLAVDIWslGCTVLE--MATGKPPWSQ-----YEGvaaIFKiGNSGELPPIPDHLSP 230
                        250       260
                 ....*....|....*....|....*....
gi 548961101 248 SAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd06632  231 DAKDFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
12-276 2.07e-41

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: 152.67  E-value: 2.07e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLstedlkREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14111    5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVL------QEYEILKSLHHERIMALHEAYITPRYLVLIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRadagFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQLGE 171
Cdd:cd14111   79 EFCSGKELLHSLIDR----FRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVT---NLNAIKIVDFGSAQSFNP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVA-GGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEG-IIKGKY---KMNPRqwshIS 246
Cdd:cd14111  152 LSLRQlGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAkILVAKFdafKLYPN----VS 227
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 247 ESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14111  228 QSASLFLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
18-275 2.30e-41

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: 153.28  E-value: 2.30e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKF------------------TSSPGLSTEDLKREASICHMLKHPHIVELLE 79
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLlkqagffrrppprrkpgaLGKPLDPLDRVYREIAILKKLDHPNVVKLVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  80 TYS--SDGMLYMVFEFMDGADlcfeiVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSap 157
Cdd:cd14118   82 VLDdpNEDNLYMVFELVDKGA-----VMEVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLL-GDDGH-- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 158 VKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVK--REPY-GKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGK 234
Cdd:cd14118  154 VKIADFGVSNEFEGDDALLSSTAGTPAFMAPEALSesRKKFsGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTD 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 548961101 235 YKMNPRQWShISESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd14118  234 PVVFPDDPV-VSEQLKDLILRMLDKNPSERITLPEIKEHPW 273
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
483-563 3.28e-41

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: 145.49  E-value: 3.28e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 483 RLVQFQKNTDEPMGITLKMNElNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIV 562
Cdd:cd06726    1 RLVEFEKARDEPLGATIKMEE-DSVIVARILHGGMAHRSGLLHVGDEILEINGIPVSGKTVDELQKLLSSLSGSVTFKLI 79

                 .
gi 548961101 563 P 563
Cdd:cd06726   80 P 80
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
18-275 4.85e-41

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: 151.61  E-value: 4.85e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVK------IVDvakfTSSPglstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKcvkkrhIVQ----TRQQ----EHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGe 171
Cdd:cd05572   73 EYCLGGELWTILRDRG----LFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLL---DSNGYVKLVDFGFAKKLG- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE---RLFEGIIKGKYKMN-PRqwsHISE 247
Cdd:cd05572  145 SGRKTWTFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEdpmKIYNIILKGIDKIEfPK---YIDK 221
                        250       260       270
                 ....*....|....*....|....*....|...
gi 548961101 248 SAKDLVRRMLMLDPAERITV----YEAL-NHPW 275
Cdd:cd05572  222 NAKNLIKQLLRRNPEERLGYlkggIRDIkKHKW 254
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
18-276 7.16e-41

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: 151.61  E-value: 7.16e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLK-HPHIVELLETYSSDGMLYMVFEFMDG 96
Cdd:cd14198   16 LGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQD---CRAEILHEIAVLELAKsNPRVVNLHEVYETTSEIILILEYAAG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  97 AD---LCFeivkrADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESG 173
Cdd:cd14198   93 GEifnLCV-----PDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFGMSRKIGHAC 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 174 LVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT-KERLFEGIIKGKYKMNPRQWSHISESAKDL 252
Cdd:cd14198  168 ELR-EIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEdNQETFLNISQVNVDYSEETFSSVSQLATDF 246
                        250       260
                 ....*....|....*....|....
gi 548961101 253 VRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14198  247 IQKLLVKNPEKRPTAEICLSHSWL 270
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
12-274 4.41e-40

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: 148.69  E-value: 4.41e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd08530    2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQK---EREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAiQLGE 171
Cdd:cd08530   79 EYAPFGDLSKLISKRKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDL---VKIGDLGIS-KVLK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLvAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYkmnPRQWSHISESAK 250
Cdd:cd08530  155 KNL-AKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEArTMQELRYKVCRGKF---PPIPPVYSQDLQ 230
                        250       260
                 ....*....|....*....|....
gi 548961101 251 DLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd08530  231 QIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
16-275 4.54e-40

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: 148.59  E-value: 4.54e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVV----RRCINRETgqqFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14121    1 EKLGSGTYATVykayRKSGAREV---VAVKCVSKSSLNKA---STENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsaPV-KLGGFGVAIQLG 170
Cdd:cd14121   75 EYCSGGDLSRFIRSRR----TLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYN--PVlKLADFGFAQHLK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAGGRvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQwSHISESA 249
Cdd:cd14121  149 PNDEAHSLR-GSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASrSFEELEEKIRSSKPIEIPTR-PELSADC 226
                        250       260
                 ....*....|....*....|....*.
gi 548961101 250 KDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd14121  227 RDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
16-276 5.86e-40

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: 148.52  E-value: 5.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 95
Cdd:cd14193   10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEK-----EEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLCFEIVkraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnSAPVKLGGFGVAIQLGESGLV 175
Cdd:cd14193   85 GGELFDRII---DENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSRE-ANQVKIIDFGLARRYKPREKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 176 aggRV--GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQWSHISESAKDL 252
Cdd:cd14193  161 ---RVnfGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDnETLNNILACQWDFEDEEFADISEEAKDF 237
                        250       260
                 ....*....|....*....|....
gi 548961101 253 VRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14193  238 ISKLLIKEKSWRMSASEALKHPWL 261
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
12-272 5.98e-40

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: 148.57  E-value: 5.98e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd08224    2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQI--FEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGE 171
Cdd:cd08224   80 ELADAGDLSRLIKHFKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITA---NGVVKLGDLGLGRFFSS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE---RLFEGIIKGKYKmnPRQWSHISES 248
Cdd:cd08224  157 KTTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMnlySLCKKIEKCEYP--PLPADLYSQE 234
                        250       260
                 ....*....|....*....|....
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALN 272
Cdd:cd08224  235 LRDLVAACIQPDPEKRPDISYVLD 258
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
12-279 6.47e-40

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: 149.64  E-value: 6.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSP-GLSTEDLkREASICHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd07841    2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKdGINFTAL-REIKLLQELKHPNIIGLLDVFGHKSNINLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGaDLcfEIVKRaDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQLG 170
Cdd:cd07841   81 FEFMET-DL--EKVIK-DKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASD---GVLKLADFGLARSFG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAGGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFE-----------GIIKG 233
Cdd:cd07841  154 SPNRKMTHQVVTRWYRAPELLfGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDidqlgKIFEalgtpteenwpGVTSL 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 548961101 234 KY-----KMNPRQWSHI----SESAKDLVRRMLMLDPAERITVYEALNHPWLKER 279
Cdd:cd07841  234 PDyvefkPFPPTPLKQIfpaaSDDALDLLQRLLTLNPNKRITARQALEHPYFSND 288
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
12-276 7.26e-40

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: 148.18  E-value: 7.26e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINReTGQQFAVKIVDVAKFTSSPGLSteDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14161    5 YEFLETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRIKDEQDLL--HIRREIEIMSSLNHPHIISVYEVFENSSKIVIVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAiQLGE 171
Cdd:cd14161   82 EYASRGDLYDYISERQR----LSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGN---IKIADFGLS-NLYN 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKP-VDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYkmnpRQWSHISEsA 249
Cdd:cd14161  154 QDKFLQTYCGSPLYASPEIVNGRPYIGPeVDSWSLGVLLYILVHGTMPFDGHDYKiLVKQISSGAY----REPTKPSD-A 228
                        250       260
                 ....*....|....*....|....*..
gi 548961101 250 KDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14161  229 CGLIRWLLMVNPERRATLEDVASHWWV 255
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
12-276 1.64e-39

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: 147.17  E-value: 1.64e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspgLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd08529    2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSR---KMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcFEIVKRaDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 171
Cdd:cd08529   79 EYAENGDL-HSLIKS-QRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDN---VKIGDLGVAKILSD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQWshiSESAK 250
Cdd:cd08529  154 TTNFAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQgALILKIVRGKYPPISASY---SQDLS 230
                        250       260
                 ....*....|....*....|....*.
gi 548961101 251 DLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd08529  231 QLIDSCLTKDYRQRPDTTELLRNPSL 256
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
17-275 3.52e-39

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: 146.35  E-value: 3.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDG 96
Cdd:cd06625    7 LLGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEASKEVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  97 ADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESGLVA 176
Cdd:cd06625   87 GSVKDEIKAYG----ALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGN---VKLGDFGASKRLQTICSST 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 177 GGR--VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGtkerlFE---GIIK-GKYKMNPRQWSHISESAK 250
Cdd:cd06625  160 GMKsvTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAE-----FEpmaAIFKiATQPTNPQLPPHVSEDAR 234
                        250       260
                 ....*....|....*....|....*
gi 548961101 251 DLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd06625  235 DFLSLIFVRNKKQRPSAEELLSHSF 259
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
9-276 6.86e-39

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: 145.49  E-value: 6.86e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglSTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd06612    2 EEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEE-------DLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLW 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLCfEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQ 168
Cdd:cd06612   75 IVMEYCGAGSVS-DIMKITNKTL--TEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQ---AKLADFGVSGQ 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEgiIKGK----YKmNPRQW 242
Cdd:cd06612  149 LTDTMAKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHpmRAIFM--IPNKppptLS-DPEKW 225
                        250       260       270
                 ....*....|....*....|....*....|....
gi 548961101 243 shiSESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd06612  226 ---SPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
5-276 7.89e-39

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: 145.50  E-value: 7.89e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   5 DVLFEDVYELceviGKGPFSVVRRCINRETGQQFAVKivdvakFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSD 84
Cdd:cd14113    6 DSFYSEVAEL----GRGRFSVVKKCDQRGTKRAVATK------FVNKKLMKRDQVTHELGVLQSLQHPQLVGLLDTFETP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  85 GMLYMVFEFMDGADLCFEIVKradAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFG 164
Cdd:cd14113   76 TSYILVLEMADQGRLLDYVVR---WGNLTEEKIRF-YLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTIKLADFG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 165 VAIQLGESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWS 243
Cdd:cd14113  152 DAVQLNTTYYIH-QLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDeSVEETCLNICRLDFSFPDDYFK 230
                        250       260       270
                 ....*....|....*....|....*....|...
gi 548961101 244 HISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14113  231 GVSQKAKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
11-276 8.08e-39

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: 145.03  E-value: 8.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLstedlkREASICHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd14107    3 VYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAF------QERDILARLSHRRLTCLLDQFETRKTLILI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSaPVKLGGFGVAIQLG 170
Cdd:cd14107   77 LELCSSEELLDRLFLKG----VVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRE-DIKICDFGFAQEIT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLvAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNPRQWSHISESA 249
Cdd:cd14107  152 PSEH-QFSKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRaTLLNVAEGVVSWDTPEITHLSEDA 230
                        250       260
                 ....*....|....*....|....*..
gi 548961101 250 KDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14107  231 KDFIKRVLQPDPEKRPSASECLSHEWF 257
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
9-276 9.73e-39

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: 145.00  E-value: 9.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDvYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvAKFTSSPGLsTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd14186    1 ED-FKVLNLLGKGSFACVYRARSLHTGLEVAIKMID-KKAMQKAGM-VQRVRNEVEIHCQLKHPSILELYNYFEDSNYVY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQ 168
Cdd:cd14186   78 LVLEMCHNGEMSRYLKNRKKP---FTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMN---IKIADFGLATQ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF-YGTKERLFEGIIKGKYKMNprqwSHISE 247
Cdd:cd14186  152 LKMPHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFdTDTVKNTLNKVVLADYEMP----AFLSR 227
                        250       260
                 ....*....|....*....|....*....
gi 548961101 248 SAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14186  228 EAQDLIHQLLRKNPADRLSLSSVLDHPFM 256
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
18-275 1.39e-38

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: 144.33  E-value: 1.39e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKivdvakFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVK------FVSKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLcFEIVKRADAgfVYSEAVAsHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLgesglvAG 177
Cdd:cd14115   75 RL-LDYLMNHDE--LMEEKVA-FYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQI------SG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 178 GR-----VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISESAKD 251
Cdd:cd14115  145 HRhvhhlLGNPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDeSKEETCINVCRVDFSFPDEYFGDVSQAARD 224
                        250       260
                 ....*....|....*....|....
gi 548961101 252 LVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd14115  225 FINVILQEDPRRRPTAATCLQHPW 248
SH3_CASK cd12081
Src Homology 3 domain of Calcium/calmodulin-dependent Serine protein Kinase; CASK is a ...
610-671 1.50e-38

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: 137.34  E-value: 1.50e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 610 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPEL 671
Cdd:cd12081    1 YVRAQFEYDPLKDDLIPCKQAGIRFRVGDILQIISKDDHNWWQAKLENSKNGTAGLIPSPEL 62
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
18-276 1.71e-38

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: 144.37  E-value: 1.71e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRC--INRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLE-TYSSDGMLYMVFEFM 94
Cdd:cd13994    1 IGKGATSVVRIVtkKNPRSGVLYAVKEYRRRDDESKRKDYVKRLTSEYIISSKLHHPNIVKVLDlCQDLHGKWCLVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  95 DGADLCFEIVKRADAGFvysEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESG- 173
Cdd:cd13994   81 PGGDLFTLIEKADSLSL---EEKDC-FFKQILRGVAYLHSHGIAHRDLKPENILLDEDGV---LKLTDFGTAEVFGMPAe 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 174 ---LVAGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFEGIIKGKYKMNPRQWSH 244
Cdd:cd13994  154 kesPMSAGLCGSEPYMAPEVFTSGSYdGRAVDVWSCGIVLFALFTGRFPWRSAKKsdsayKAYEKSGDFTNGPYEPIENL 233
                        250       260       270
                 ....*....|....*....|....*....|..
gi 548961101 245 ISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd13994  234 LPSECRRLIYRMLHPDPEKRITIDEALNDPWV 265
SH3_MPP1-like cd12035
Src Homology 3 domain of Membrane Protein, Palmitoylated 1 (or MAGUK p55 subfamily member 1) ...
610-671 1.74e-38

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: 137.18  E-value: 1.74e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 610 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPEL 671
Cdd:cd12035    1 YVRAQFDYDPSKDDLIPCQQAGIAFKTGDILQIISKDDHNWWQARKPGASKEPAGLIPSPEL 62
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
12-276 2.05e-38

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: 144.33  E-value: 2.05e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELC--EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEDLKREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd14192    4 YAVCphEVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKER-----EEVKNEINIMNQLNHVNLIQLYDAFESKTNLTL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLCFEIVkraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGFGVAIQL 169
Cdd:cd14192   79 IMEYVDGGELFDRIT---DESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQ-IKIIDFGLARRY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 G--ESGLVaggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHIS 246
Cdd:cd14192  155 KprEKLKV---NFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGeTDAETMNNIVNCKWDFDAEAFENLS 231
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 247 ESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14192  232 EEAKDFISRLLVKEKSCRMSATQCLKHEWL 261
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
18-264 2.26e-38

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: 143.45  E-value: 2.26e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRetGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd13999    1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDE---LLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLcFEIVKraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESGLVAG 177
Cdd:cd13999   76 SL-YDLLH--KKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFT---VKIADFGLSRIKNSTTEKMT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 178 GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF--YGTKERLFEGIIKGKYKMNPrqwSHISESAKDLVRR 255
Cdd:cd13999  150 GVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFkeLSPIQIAAAVVQKGLRPPIP---PDCPPELSKLIKR 226

                 ....*....
gi 548961101 256 MLMLDPAER 264
Cdd:cd13999  227 CWNEDPEKR 235
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
12-276 2.97e-38

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: 143.77  E-value: 2.97e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftSSPGLSTEDLKREASICHMLKHPHIVELLETY-SSDGMLYMV 90
Cdd:cd14165    3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKK--APDDFVEKFLPRELEILARLNHKSIIKTYEIFeTSDGKVYIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQL- 169
Cdd:cd14165   81 MELGVQGDL-LEFIKLRGA---LPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLL---DKDFNIKLTDFGFSKRCl 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 -GESGLVAGGRV--GTPHFMAPEVVKREPYGKPV-DVWGCGVILFILLSGCLPFYGTKERLFEGIIKgKYKMNPRQWSHI 245
Cdd:cd14165  154 rDENGRIVLSKTfcGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQK-EHRVRFPRSKNL 232
                        250       260       270
                 ....*....|....*....|....*....|.
gi 548961101 246 SESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14165  233 TSECKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
12-276 4.79e-38

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: 143.03  E-value: 4.79e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14070    4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVID-KKKAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 171
Cdd:cd14070   83 ELCPGGNLMHRIYDKKR----LEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDN---IKLIDFGLSNCAGI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAG--GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFygTKE-----RLFEGIIKGkyKMNPRQwSH 244
Cdd:cd14070  156 LGYSDPfsTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPF--TVEpfslrALHQKMVDK--EMNPLP-TD 230
                        250       260       270
                 ....*....|....*....|....*....|..
gi 548961101 245 ISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14070  231 LSPGAISFLRSLLEPDPLKRPNIKQALANRWL 262
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
17-265 7.55e-38

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: 144.47  E-value: 7.55e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFS---VVRRCINRETGQQFAVKIVDVAKFTSSPGlSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEF 93
Cdd:cd05584    3 VLGKGGYGkvfQVRKTTGSDKGKIFAMKVLKKASIVRNQK-DTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLILEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  94 MDGADLcFEIVKRADagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESG 173
Cdd:cd05584   82 LSGGEL-FMHLEREG---IFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGH---VKLTDFGLCKESIHDG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 174 LVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPrqwsHISESAKDL 252
Cdd:cd05584  155 TVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAeNRKKTIDKILKGKLNLPP----YLTNEARDL 230
                        250
                 ....*....|...
gi 548961101 253 VRRMLMLDPAERI 265
Cdd:cd05584  231 LKKLLKRNVSSRL 243
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
9-290 8.55e-38

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: 142.96  E-value: 8.55e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakFTSSPGLstEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd06611    4 NDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQ---IESEEEL--EDFMVEIDILSECKHPNIVGLYEAYFYENKLW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLCfEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQ 168
Cdd:cd06611   79 ILIEFCDGGALD-SIMLELERGL--TEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGD---VKLADFGVSAK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAGGRVGTPHFMAPEVV-----KREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYK--MNPR 240
Cdd:cd06611  153 NKSTLQKRDTFIGTPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHHELNPmRVLLKILKSEPPtlDQPS 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 548961101 241 QWshiSESAKDLVRRMLMLDPAERITVYEALNHPWLKER-DRYAYKIHLPE 290
Cdd:cd06611  233 KW---SSSFNDFLKSCLVKDPDDRPTAAELLKHPFVSDQsDNKAIKDLLAE 280
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
12-294 1.57e-37

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 143.80  E-value: 1.57e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIV---DVAKFTSspglsTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLkkrEILKMKQ-----VQHVAQEKSILMELSHPFIVNMMCSFQDENRVY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQ 168
Cdd:PTZ00263  95 FLLEFVVGGEL-FTHLRKAGR---FPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGH---VKVTDFGFAKK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnPRqWshISE 247
Cdd:PTZ00263 168 VPDRTFTL---CGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDdTPFRIYEKILAGRLKF-PN-W--FDG 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 548961101 248 SAKDLVRRMLMLDPAERI-----TVYEALNHPWLKERD---RYAYKIHLPETVEQ 294
Cdd:PTZ00263 241 RARDLVKGLLQTDHTKRLgtlkgGVADVKNHPYFHGANwdkLYARYYPAPIPVRV 295
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
18-277 1.71e-37

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: 141.43  E-value: 1.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd06648   15 IGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRR-----ELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLCfEIVKradAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGESGLVAG 177
Cdd:cd06648   90 ALT-DIVT---HTRMNEEQIAT-VCRAVLKALSFLHSQGVIHRDIKSDSILLTS---DGRVKLSDFGFCAQVSKEVPRRK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 178 GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYgtKERLFEGiIKGKYKMNPRQWSH---ISESAKDLVR 254
Cdd:cd06648  162 SLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYF--NEPPLQA-MKRIRDNEPPKLKNlhkVSPRLRSFLD 238
                        250       260
                 ....*....|....*....|...
gi 548961101 255 RMLMLDPAERITVYEALNHPWLK 277
Cdd:cd06648  239 RMLVRDPAQRATAAELLNHPFLA 261
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
10-274 2.22e-37

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: 141.34  E-value: 2.22e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglsTEDLKREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd06610    1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTS----MDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADlCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQL 169
Cdd:cd06610   77 VMPLLSGGS-LLDIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGE---DGSVKIADFGVSASL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAGGR----VGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPFY-------------GTKERLFEGII 231
Cdd:cd06610  153 ATGGDRTRKVrktfVGTPCWMAPEVMEQVRgYDFKADIWSFGITAIELATGAAPYSkyppmkvlmltlqNDPPSLETGAD 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 548961101 232 KGKYkmnprqwshiSESAKDLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd06610  233 YKKY----------SKSFRKMISLCLQKDPSKRPTAEELLKHK 265
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
12-275 3.93e-37

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: 140.51  E-value: 3.93e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14665    2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKID------ENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcFEIVkrADAGfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkeNSAP-VKLGGFGVAiqlg 170
Cdd:cd14665   76 EYAAGGEL-FERI--CNAG-RFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDG--SPAPrLKICDFGYS---- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAG---GRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFEGIIKGKYKMNprQ 241
Cdd:cd14665  146 KSSVLHSqpkSTVGTPAYIAPEVLLKKEYdGKIADVWSCGVTLYVMLVGAYPFEDPEEprnfrKTIQRILSVQYSIP--D 223
                        250       260       270
                 ....*....|....*....|....*....|....
gi 548961101 242 WSHISESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd14665  224 YVHISPECRHLISRIFVADPATRITIPEIRNHEW 257
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
12-275 4.82e-37

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: 141.16  E-value: 4.82e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspgLSTED------LKREASICHMLKHPHIVELLETYSSD- 84
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIR---------MENEKegfpitAIREIKLLQKLDHPNVVRLKEIVTSKg 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  85 -----GMLYMVFEFMDgADLcfeivkradAGFVYSEAVAS------HYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE 153
Cdd:cd07840   72 sakykGSIYMVFEYMD-HDL---------TGLLDNPEVKFtesqikCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 154 NsapVKLGGFGVAIQL-GESGLVAGGRVGTPHFMAPEVV---KRepYGKPVDVWGCGVILFILLSGCLPFYGTKE----- 224
Cdd:cd07840  142 V---LKLADFGLARPYtKENNADYTNRVITLWYRPPELLlgaTR--YGPEVDMWSVGCILAELFTGKPIFQGKTEleqle 216
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548961101 225 RLFE-----------GIIKGKYKMNPRQ-----------WSH-ISESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd07840  217 KIFElcgspteenwpGVSDLPWFENLKPkkpykrrlrevFKNvIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
12-276 2.15e-36

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: 138.82  E-value: 2.15e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvAKFTSspglsTED---LKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMK-KKFYS-----WEEcmnLREVKSLRKLNEHPNIVKLKEVFRENDELY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGaDLcFEIVKRADaGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQ 168
Cdd:cd07830   75 FVFEYMEG-NL-YQLMKDRK-GKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEV---VKIADFGLARE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LgESGLVAGGRVGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPFYGTKErlfegiIKGKYKM-------NPR 240
Cdd:cd07830  149 I-RSRPPYTDYVSTRWYRAPEILLRSTsYSSPVDIWALGCIMAELYTLRPLFPGSSE------IDQLYKIcsvlgtpTKQ 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 241 QWS--------------------------HISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd07830  222 DWPegyklasklgfrfpqfaptslhqlipNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
12-276 4.32e-36

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: 137.37  E-value: 4.32e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVD---VAKFTSSPGLstEDLKREasICHMLK-----HPHIVELLETYS- 82
Cdd:cd14005    2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPksrVTEWAMINGP--VPVPLE--IALLLKaskpgVPGVIRLLDWYEr 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  83 SDGMLyMVFEFMDGA-DLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLG 161
Cdd:cd14005   78 PDGFL-LIMERPEPCqDL-FDFITERGA---LSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGE--VKLI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 162 GFGVAIQLGESglVAGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKgkykmnpr 240
Cdd:cd14005  151 DFGCGALLKDS--VYTDFDGTRVYSPPEWIRHGRYhGRPATVWSLGILLYDMLCGDIPFENDEQILRGNVLF-------- 220
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 548961101 241 qWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14005  221 -RPRLSKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
12-275 5.71e-36

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: 136.82  E-value: 5.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14662    2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKID------ENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcFEivKRADAGfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkeNSAP-VKLGGFGVAiqlg 170
Cdd:cd14662   76 EYAAGGEL-FE--RICNAG-RFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDG--SPAPrLKICDFGYS---- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAG---GRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFEGIIKGKYKMNprQ 241
Cdd:cd14662  146 KSSVLHSqpkSTVGTPAYIAPEVLSRKEYdGKVADVWSCGVTLYVMLVGAYPFEDPDDpknfrKTIQRIMSVQYKIP--D 223
                        250       260       270
                 ....*....|....*....|....*....|....
gi 548961101 242 WSHISESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd14662  224 YVRVSQDCRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
12-276 2.44e-35

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: 135.12  E-value: 2.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvaKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14162    2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVS--KKKAPEDYLQKFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcFEIVKRADAGfvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAiqLGE 171
Cdd:cd14162   80 ELAENGDL-LDYIRKNGAL---PEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNN---LKITDFGFA--RGV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRV------GTPHFMAPEVVKREPYgKPV--DVWGCGVILFILLSGCLPFYGTKER-LFEGIIKG-KYKMNPrq 241
Cdd:cd14162  151 MKTKDGKPKlsetycGSYAYASPEILRGIPY-DPFlsDIWSMGVVLYTMVYGRLPFDDSNLKvLLKQVQRRvVFPKNP-- 227
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 548961101 242 wsHISESAKDLVRRMLMLDPaERITVYEALNHPWL 276
Cdd:cd14162  228 --TVSEECKDLILRMLSPVK-KRITIEEIKRDPWF 259
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
12-276 4.00e-35

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: 135.53  E-value: 4.00e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd07832    2 YKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEG--GIPNQALREIKALQACQGHPYVVKLRDVFPHGTGFVLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGaDLcFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVA-IQLG 170
Cdd:cd07832   80 EYMLS-SL-SEVLRDEERPL--TEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGV---LKIADFGLArLFSE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAGGRVGTPHFMAPEVV--KREpYGKPVDVWGCGVILFILLSGCLPFYGT----------------KERLFEGII- 231
Cdd:cd07832  153 EDPRLYSHQVATRWYRAPELLygSRK-YDEGVDLWAVGCIFAELLNGSPLFPGEndieqlaivlrtlgtpNEKTWPELTs 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 548961101 232 -----KGKYKMNPRQ-WSHI----SESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd07832  232 lpdynKITFPESKGIrLEEIfpdcSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
12-277 4.79e-35

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: 137.03  E-value: 4.79e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIV---DVAKFTSSPGLSTE-DLKREASichmlkHPHIVELLETYSSDGML 87
Cdd:cd05573    3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILrksDMLKREQIAHVRAErDILADAD------SPWIVRLHYAFQDEDHL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAI 167
Cdd:cd05573   77 YLVMEYMPGGDLMNLLIKYD----VFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGH---IKLADFGLCT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGESGLV-----------------------------AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLP 218
Cdd:cd05573  150 KMNKSGDResylndsvntlfqdnvlarrrphkqrrvrAYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPP 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 219 FYG-TKERLFEGIIKGKYKMN-PRQwSHISESAKDLVRRmLMLDPAERITVYEAL-NHPWLK 277
Cdd:cd05573  230 FYSdSLVETYSKIMNWKESLVfPDD-PDVSPEAIDLIRR-LLCDPEDRLGSAEEIkAHPFFK 289
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-264 5.99e-35

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: 133.95  E-value: 5.99e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglsTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd08219    2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSA----VEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIvkRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 171
Cdd:cd08219   78 EYCDGGDLMQKI--KLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGK---VKLGDFGSARLLTS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY-GTKERLFEGIIKGKYKMNPrqwSHISESAK 250
Cdd:cd08219  153 PGAYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQaNSWKNLILKVCQGSYKPLP---SHYSYELR 229
                        250
                 ....*....|....
gi 548961101 251 DLVRRMLMLDPAER 264
Cdd:cd08219  230 SLIKQMFKRNPRSR 243
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-276 6.89e-35

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: 133.93  E-value: 6.89e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd08225    2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEID---LTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRAdaGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkeNSAPVKLGGFGVAIQLGE 171
Cdd:cd08225   79 EYCDGGDLMKRINRQR--GVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSK--NGMVAKLGDFGIARQLND 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYK-MNPrqwsHISESA 249
Cdd:cd08225  155 SMELAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNlHQLVLKICQGYFApISP----NFSRDL 230
                        250       260
                 ....*....|....*....|....*..
gi 548961101 250 KDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd08225  231 RSLISQLFKVSPRDRPSITSILKRPFL 257
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
10-280 6.90e-35

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: 134.87  E-value: 6.90e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd05612    1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLK--QEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSapVKLGGFGVAIQL 169
Cdd:cd05612   79 LMEYVPGGEL-FSYLRNSGR---FSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILL-DKEGH--IKLTDFGFAKKL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnPRqwsHISES 248
Cdd:cd05612  152 RDRTWTL---CGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDdNPFGIYEKILAGKLEF-PR---HLDLY 224
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 548961101 249 AKDLVRRMLMLDPAERI-----TVYEALNHPWLKERD 280
Cdd:cd05612  225 AKDLIKKLLVVDRTRRLgnmknGADDVKNHRWFKSVD 261
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-276 7.65e-35

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: 133.78  E-value: 7.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd08218    2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPK---EREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIvkRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQLGE 171
Cdd:cd08218   79 DYCDGGDLYKRI--NAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLT---KDGIIKLGDFGIARVLNS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF-YGTKERLFEGIIKGKYKMNPrqwSHISESAK 250
Cdd:cd08218  154 TVELARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFeAGNMKNLVLKIIRGSYPPVP---SRYSYDLR 230
                        250       260
                 ....*....|....*....|....*.
gi 548961101 251 DLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd08218  231 SLVSQLFKRNPRDRPSINSILEKPFI 256
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
12-278 1.37e-34

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: 134.96  E-value: 1.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKivDVAKFTSSPglstEDLK---REASICHMLKHPHIVELL-----ETYSS 83
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIK--KISNVFDDL----IDAKrilREIKILRHLKHENIIGLLdilrpPSPEE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLYMVFEFMDgADLCfEIVKradAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGF 163
Cdd:cd07834   76 FNDVYIVTELME-TDLH-KVIK---SPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCD---LKICDF 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 164 GVA--IQLGESGLVAGGRVGTPHFMAPEVV---KRepYGKPVDVWGCGVILFILLSGCLPFYGT---------------- 222
Cdd:cd07834  148 GLArgVDPDEDKGFLTEYVVTRWYRAPELLlssKK--YTKAIDIWSVGCIFAELLTRKPLFPGRdyidqlnlivevlgtp 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101 223 KERLFEGI--------IKGKYKMNPRQWSHI----SESAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd07834  226 SEEDLKFIssekarnyLKSLPKKPKKPLSEVfpgaSPEAIDLLEKMLVFNPKKRITADEALAHPYLAQ 293
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
18-277 1.93e-34

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: 132.60  E-value: 1.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSteDLKREASICHMLKH-PHIVELLETYSSDGMLYMVFEFMDG 96
Cdd:cd05611    4 ISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVT--NVKAERAIMMIQGEsPYVAKLYYSFQSKDYLYLVMEYLNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  97 ADlCFEIVKRADagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGvaiqLGESGLVa 176
Cdd:cd05611   82 GD-CASLIKTLG---GLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLI---DQTGHLKLTDFG----LSRNGLE- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 177 gGR-----VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY-GTKERLFEGIIKGKYKMNPRQWSHISESAK 250
Cdd:cd05611  150 -KRhnkkfVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHaETPDAVFDNILSRRINWPEEVKEFCSPEAV 228
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 251 DLVRRMLMLDPAERI---TVYEALNHPWLK 277
Cdd:cd05611  229 DLINRLLCMDPAKRLganGYQEIKSHPFFK 258
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
16-276 2.53e-34

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: 132.35  E-value: 2.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDvakfTSSPGlSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 95
Cdd:cd14190   10 EVLGGGKFGKVHTCTEKRTGLKLAAKVIN----KQNSK-DKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLCFEIVkraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKeNSAPVKLGGFGVAIQLG-ESGL 174
Cdd:cd14190   85 GGELFERIV---DEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNR-TGHQVKIIDFGLARRYNpREKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 175 VAGgrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQWSHISESAKDLV 253
Cdd:cd14190  161 KVN--FGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDtETLNNVLMGNWYFDEETFEHVSDEAKDFV 238
                        250       260
                 ....*....|....*....|...
gi 548961101 254 RRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14190  239 SNLIIKERSARMSATQCLKHPWL 261
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
12-275 2.80e-34

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: 132.93  E-value: 2.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQqfavkIVDVAKFtsspgLSTEDLK-------REASICHMLKHPHIVELLETYSSD 84
Cdd:cd07846    3 YENLGLVGEGSYGMVMKCRHKETGQ-----IVAIKKF-----LESEDDKmvkkiamREIKMLKQLRHENLVNLIEVFRRK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  85 GMLYMVFEFMDGADLcfEIVKRADAGFVYSeaVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFG 164
Cdd:cd07846   73 KRWYLVFEFVDHTVL--DDLEKYPNGLDES--RVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQ---SGVVKLCDFG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 165 VAIQLGESGLVAGGRVGTPHFMAPE-VVKREPYGKPVDVWGCGVILFILLSGCLPFYG---------------------- 221
Cdd:cd07846  146 FARTLAAPGEVYTDYVATRWYRAPElLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGdsdidqlyhiikclgnliprhq 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548961101 222 ---TKERLFEGI----IKGKYKMNpRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd07846  226 elfQKNPLFAGVrlpeVKEVEPLE-RRYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
12-276 3.13e-34

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: 132.15  E-value: 3.13e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCE-----VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEDLKREASICHMLKHPHIVELLETYSSDGM 86
Cdd:cd06624    5 YEYDEsgervVLGKGTFGVVYAARDLSTQVRIAIKEIPERDSREV-----QPLHEEIALHSRLSHKNIVQYLGSVSEDGF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 LYMVFEFMDGADLCfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKenSAPVKLGGFGVA 166
Cdd:cd06624   80 FKIFMEQVPGGSLS-ALLRSKWGPLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTY--SGVVKISDFGTS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQLGESGLVAGGRVGTPHFMAPEVVKREP--YGKPVDVW--GCGVILfiLLSGCLPFY--GTKErlfEGIIK-GKYKMNP 239
Cdd:cd06624  157 KRLAGINPCTETFTGTLQYMAPEVIDKGQrgYGPPADIWslGCTIIE--MATGKPPFIelGEPQ---AAMFKvGMFKIHP 231
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 548961101 240 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd06624  232 EIPESLSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
17-280 3.29e-34

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: 133.88  E-value: 3.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKIVdvakftsSPGLSTEDLKREASIC--HML----KHPHIVELLETYSSDGMLYMV 90
Cdd:cd05570    2 VLGKGSFGKVMLAERKKTDELYAIKVL-------KKEVIIEDDDVECTMTekRVLalanRHPFLTGLHACFQTEDRLYFV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLCFEIVKradaGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGvaiqLG 170
Cdd:cd05570   75 MEYVNGGDLMFHIQR----ARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGH---IKIADFG----MC 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAGGRV----GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnPRqwsHI 245
Cdd:cd05570  144 KEGIWGGNTTstfcGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGdDEDELFEAILNDEVLY-PR---WL 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 548961101 246 SESAKDLVRRMLMLDPAERITVY-----EALNHPWLKERD 280
Cdd:cd05570  220 SREAVSILKGLLTKDPARRLGCGpkgeaDIKAHPFFRNID 259
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
12-276 5.63e-34

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: 132.00  E-value: 5.63e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKF---------------------TSSPGLSTEDLKREASICHMLK 70
Cdd:cd14200    2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLlkqygfprrppprgskaaqgeQAKPLAPLERVYQEIAILKKLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  71 HPHIVELLETYS--SDGMLYMVFEFMDGADlcfeiVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVL 148
Cdd:cd14200   82 HVNIVKLIEVLDdpAEDNLYMVFDLLRKGP-----VMEVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 149 LAskeNSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVV--KREPY-GKPVDVWGCGVILFILLSGCLPFYGTKER 225
Cdd:cd14200  157 LG---DDGHVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLsdSGQSFsGKALDVWAMGVTLYCFVYGKCPFIDEFIL 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 548961101 226 LFEGIIKGKYKMNPRQwSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14200  234 ALHNKIKNKPVEFPEE-PEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
16-275 8.06e-34

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: 132.86  E-value: 8.06e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKI----VDVAKFTSSPGLStedlkrEASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd05571    1 KVLGKGTFGKVILCREKATGELYAIKIlkkeVIIAKDEVAHTLT------ENRVLQNTRHPFLTSLKYSFQTNDRLCFVM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSapVKLGGFGVAIQLGE 171
Cdd:cd05571   75 EYVNGGELFFHLSRER----VFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLL-DKDGH--IKITDFGLCKEEIS 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnPRqwsHISESAK 250
Cdd:cd05571  148 YGATTKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDhEVLFELILMEEVRF-PS---TLSPEAK 223
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 251 DLVRRMLMLDPAERI-----TVYEALNHPW 275
Cdd:cd05571  224 SLLAGLLKKDPKKRLgggprDAKEIMEHPF 253
SH3_MPP1 cd12080
Src Homology 3 domain of Membrane Protein, Palmitoylated 1 (or MAGUK p55 subfamily member 1); ...
610-671 8.23e-34

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: 123.91  E-value: 8.23e-34
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 610 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPEL 671
Cdd:cd12080    1 YMRAQFDYDPKKDNLIPCKEAGLKFQTGDIIQIINKDDSNWWQGRVEGSGEESAGLIPSPEL 62
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
16-276 9.56e-34

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: 131.02  E-value: 9.56e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRrCINRETGQQFAVKIVDVAkfTSSPGLST---EDLKREASICHMLKHPHIVELLETYSSDGMLYMVFE 92
Cdd:cd06631    7 NVLGKGAYGTVY-CGLTSTGQLIAVKQVELD--TSDKEKAEkeyEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFME 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  93 FMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGES 172
Cdd:cd06631   84 FVPGGSIA-SILARFGA---LEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMP---NGVIKLIDFGCAKRLCIN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 173 GLVAG-GRV-----GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLP----------FYgtkerlfegiIKGKYK 236
Cdd:cd06631  157 LSSGSqSQLlksmrGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPwadmnpmaaiFA----------IGSGRK 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 548961101 237 MNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd06631  227 PVPRLPDKFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
18-277 1.05e-33

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: 131.39  E-value: 1.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVakfTSSPGLSTEDLkREASICHMLKHPHIVELLETY--SSDGMLYMVFEFMD 95
Cdd:cd06621    9 LGEGAGGSVTKCRLRNTKTIFALKTITT---DPNPDVQKQIL-RELEINKSCASPYIVKYYGAFldEQDSSIGIAMEYCE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLcFEIVKRADA-GFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESgl 174
Cdd:cd06621   85 GGSL-DSIYKKVKKkGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQ---VKLCDFGVSGELVNS-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 175 VAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER------LFEGIIKGK-YKM-----NPRQW 242
Cdd:cd06621  159 LAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPplgpieLLSYIVNMPnPELkdepeNGIKW 238
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 548961101 243 shiSESAKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd06621  239 ---SESFKDFIEKCLEKDGTRRPGPWQMLAHPWIK 270
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
10-276 1.45e-33

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: 130.02  E-value: 1.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAvkivdvAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd14108    2 DYYDIHKEIGRGAFSYLRRVKEKSSDLSFA------AKFIPVRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVII 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEfmdgadLCFE-IVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkENSAPVKLGGFGVAIQ 168
Cdd:cd14108   76 VTE------LCHEeLLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMAD-QKTDQVRICDFGNAQE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 L--GESGLVaggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNPRQWSHI 245
Cdd:cd14108  149 LtpNEPQYC---KYGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRtTLMNIRNYNVAFEESMFKDL 225
                        250       260       270
                 ....*....|....*....|....*....|.
gi 548961101 246 SESAKDLVRRMLMLDPAeRITVYEALNHPWL 276
Cdd:cd14108  226 CREAKGFIIKVLVSDRL-RPDAEETLEHPWF 255
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
12-276 1.53e-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: 1.53e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLS---------------------TEDLKREASICHMLK 70
Cdd:cd14199    4 YKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRQAGFPrrppprgaraapegctqprgpIERVYQEIAILKKLD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  71 HPHIVELLETYS--SDGMLYMVFEFMD-GADLCFEIVKRadagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCV 147
Cdd:cd14199   84 HPNVVKLVEVLDdpSEDHLYMVFELVKqGPVMEVPTLKP------LSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 148 LLASKENsapVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVK--REPY-GKPVDVWGCGVILFILLSGCLPFYGTKE 224
Cdd:cd14199  158 LVGEDGH---IKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSetRKIFsGKALDVWAMGVTLYCFVFGQCPFMDERI 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 548961101 225 RLFEGIIKGKYKMNPRQwSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14199  235 LSLHSKIKTQPLEFPDQ-PDISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
16-274 3.90e-33

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: 129.09  E-value: 3.90e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLST-EDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFM 94
Cdd:cd06630    6 PLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQEEVvEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  95 DGADLCFeIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkeNSAPVKLGGFGVAIQLGE--- 171
Cdd:cd06630   86 AGGSVAS-LLSKYGA---FSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDS--TGQRLRIADFGAAARLASkgt 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 -SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIkgkYKMN-----PRQWSHI 245
Cdd:cd06630  160 gAGEFQGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALI---FKIAsattpPPIPEHL 236
                        250       260
                 ....*....|....*....|....*....
gi 548961101 246 SESAKDLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd06630  237 SPGLRDVTLRCLELQPEDRPPARELLKHP 265
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
10-280 4.44e-33

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: 129.45  E-value: 4.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLstEDLKREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd14209    1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQV--EHTLNEKRILQAINFPFLVKLEYSFKDNSNLYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQL 169
Cdd:cd14209   79 VMEYVPGGEM-FSHLRRIGR---FSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQ---GYIKVTDFGFAKRV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GesglvagGRV----GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMnPrqwSH 244
Cdd:cd14209  152 K-------GRTwtlcGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPiQIYEKIVSGKVRF-P---SH 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 548961101 245 ISESAKDLVRRMLMLDPAERI-----TVYEALNHPWLKERD 280
Cdd:cd14209  221 FSSDLKDLLRNLLQVDLTKRFgnlknGVNDIKNHKWFATTD 261
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
12-276 4.83e-33

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: 129.32  E-value: 4.83e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkfTSSPGLSTEDLkREASICHMLK---HPHIVELLE-----TYSS 83
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVP--LSEEGIPLSTI-REIALLKQLEsfeHPNVVRLLDvchgpRTDR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLYMVFEFMDgADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGF 163
Cdd:cd07838   78 ELKLTLVFEHVD-QDLATYLDKCPKPGL--PPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTS---DGQVKLADF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 164 GVAIQLG-ESGLVAggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFEGIIKGKYKM 237
Cdd:cd07838  152 GLARIYSfEMALTS--VVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEadqlgKIFDVIGLPSEEE 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101 238 NPRQ----WS---------------HISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd07838  230 WPRNsalpRSsfpsytprpfksfvpEIDEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
12-276 5.38e-33

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: 128.44  E-value: 5.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvaKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYS-SDGMLYMV 90
Cdd:cd14164    2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVD--RRRASPDFVQKFLPRELSILRRVNHPNIVQMFECIEvANGRLYIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEfMDGADLCFEIVKRADAGFVYSEAVashyMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLGGFGVAIQLG 170
Cdd:cd14164   80 ME-AAATDLLQKIQEVHHIPKDLARDM----FAQMVGAVNYLHDMNIVHRDLKCENILLSADDRK--IKIADFGFARFVE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGkyKMNPRQWShISESA 249
Cdd:cd14164  153 DYPELSTTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPFDETNVRRLRLQQRG--VLYPSGVA-LEEPC 229
                        250       260
                 ....*....|....*....|....*..
gi 548961101 250 KDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14164  230 RALIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
18-276 5.52e-33

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: 128.57  E-value: 5.52e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVEL--LETYSSDGMLYMvfEFMD 95
Cdd:cd06626    8 IGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPK---TIKEIADEMKVLEGLDHPNLVRYygVEVHREEVYIFM--EYCQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLcFEIVKRadaGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGESG-L 174
Cdd:cd06626   83 EGTL-EELLRH---GRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDS---NGLIKLGDFGSAVKLKNNTtT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 175 VAGGR----VGTPHFMAPEVVKREP---YGKPVDVWGCGVILFILLSGCLPFYgTKERLFEGIIKGKYKMNPR--QWSHI 245
Cdd:cd06626  156 MAPGEvnslVGTPAYMAPEVITGNKgegHGRAADIWSLGCVVLEMATGKRPWS-ELDNEWAIMYHVGMGHKPPipDSLQL 234
                        250       260       270
                 ....*....|....*....|....*....|.
gi 548961101 246 SESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd06626  235 SPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
17-278 7.08e-33

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: 128.99  E-value: 7.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEdlKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDG 96
Cdd:cd05630    7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMA--LNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  97 ADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGEsGLVA 176
Cdd:cd05630   85 GDLKFHIYHMGQAGF--PEARAVFYAAEICCGLEDLHRERIVYRDLKPENILL---DDHGHIRISDLGLAVHVPE-GQTI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 177 GGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWS-HISESAKDLVRR 255
Cdd:cd05630  159 KGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSeKFSPQARSLCSM 238
                        250       260
                 ....*....|....*....|....*...
gi 548961101 256 MLMLDPAERI-----TVYEALNHPWLKE 278
Cdd:cd05630  239 LLCKDPAERLgcrggGAREVKEHPLFKK 266
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
17-276 8.94e-33

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: 128.04  E-value: 8.94e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKIVDvakfTSSPGLSTED--------LKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd06628    7 LIGSGSFGSVYLGMNASSGELMAVKQVE----LPSVSAENKDrkksmldaLQREIALLRELQHENIVQYLGSSSDANHLN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGAdlcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQ 168
Cdd:cd06628   83 IFLEYVPGG----SVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILV---DNKGGIKISDFGISKK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAGGRVGTPHF------MAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKErlFEGIIKGKYKMNPRQW 242
Cdd:cd06628  156 LEANSLSTKNNGARPSLqgsvfwMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQ--MQAIFKIGENASPTIP 233
                        250       260       270
                 ....*....|....*....|....*....|....
gi 548961101 243 SHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd06628  234 SNISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
8-272 1.19e-32

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: 127.79  E-value: 1.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVyelcEVIGKGPFSVVRRCINRETGQQFAVKIVdvaKFTSSPgLSTEDLKREASICHMLKHPHIVELLETYSSDGML 87
Cdd:cd13996    8 FEEI----ELLGSGGFGSVYKVRNKVDGVTYAIKKI---RLTEKS-SASEKVLREVKALAKLNHPNIVRYYTAWVEEPPL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRaDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLGGFGVA- 166
Cdd:cd13996   80 YIQMELCEGGTLRDWIDRR-NSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQ--VKIGDFGLAt 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 ---IQLGESGLVAG----------GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSgclPFYGTKERL--FEGII 231
Cdd:cd13996  157 sigNQKRELNNLNNnnngntsnnsVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLH---PFKTAMERStiLTDLR 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 548961101 232 KGKYKMNPRQWsHISEsaKDLVRRMLMLDPAERITVYEALN 272
Cdd:cd13996  234 NGILPESFKAK-HPKE--ADLIQSLLSKNPEERPSAEQLLR 271
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
12-276 1.41e-32

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: 127.12  E-value: 1.41e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKR---EASICHMLK---HPHIVELLETYSSDG 85
Cdd:cd14004    2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDTWVRDRKLGTvplEIHILDTLNkrsHPNIVKLLDFFEDDE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 MLYMVFE-FMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensapvklgGFG 164
Cdd:cd14004   82 FYYLVMEkHGSGMDL-FDFIERKPN---MDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGN---------GTI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 165 VAIQLGESGLVAGGR----VGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKErlfegIIKGKYKMNp 239
Cdd:cd14004  149 KLIDFGSAAYIKSGPfdtfVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPFYNIEE-----ILEADLRIP- 222
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 548961101 240 rqwSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14004  223 ---YAVSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
18-301 1.58e-32

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: 128.18  E-value: 1.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVrrCINRE--TGQQFAVKIVDVAKFTSSpglstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 95
Cdd:cd06659   29 IGEGSTGVV--CIAREkhSGRQVAVKMMDLRKQQRR-----ELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQ 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLCfEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGESGLV 175
Cdd:cd06659  102 GGALT-DIVSQTR----LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTL---DGRVKLSDFGFCAQISKDVPK 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 176 AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRR 255
Cdd:cd06659  174 RKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNSHKASPVLRDFLER 253
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 548961101 256 MLMLDPAERITVYEALNHPWLkerdryaYKIHLPET----VEQLRKFNAR 301
Cdd:cd06659  254 MLVRDPQERATAQELLDHPFL-------LQTGLPEClvplIQQYRKRTST 296
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
17-265 2.41e-32

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: 127.42  E-value: 2.41e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEdlKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDG 96
Cdd:cd05631    7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMA--LNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  97 ADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGEsGLVA 176
Cdd:cd05631   85 GDLKFHIYNMGNPGF--DEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILL---DDRGHIRISDLGLAVQIPE-GETV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 177 GGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSH-ISESAKDLVRR 255
Cdd:cd05631  159 RGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRRVKEDQEEYSEkFSEDAKSICRM 238
                        250
                 ....*....|
gi 548961101 256 MLMLDPAERI 265
Cdd:cd05631  239 LLTKNPKERL 248
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
11-277 4.71e-32

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: 126.44  E-value: 4.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftSSPGLSTEDLKREASICHMLKH---PHIVELLETYSSDGML 87
Cdd:cd06917    2 LYRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNL----DTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLcfEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAI 167
Cdd:cd06917   78 WIIMDYCEGGSI--RTLMRAGP---IAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGN---VKLCDFGVAA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGESGLVAGGRVGTPHFMAPEVVKR-EPYGKPVDVWGCGVILFILLSGCLPFygTKERLFEGIIKGKYKMNPR-QWSHI 245
Cdd:cd06917  150 SLNQNSSKRSTFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPY--SDVDALRAVMLIPKSKPPRlEGNGY 227
                        250       260       270
                 ....*....|....*....|....*....|..
gi 548961101 246 SESAKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd06917  228 SPLLKEFVAACLDEEPKDRLSADELLKSKWIK 259
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
12-280 5.11e-32

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: 126.37  E-value: 5.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTEDLKR---EASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd05609    2 FETIKLISNGAYGAVYLVRHRETRQRFAMK-----KINKQNLILRNQIQQvfvERDILTFAENPFVVSMYCSFETKRHLC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADlCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV--- 165
Cdd:cd05609   77 MVMEYVEGGD-CATLLKNIGP---LPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGH---IKLTDFGLski 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 166 -----AIQLGESGLVAGGR-------VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIK 232
Cdd:cd05609  150 glmslTTNLYEGHIEKDTRefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGdTPEELFGQVIS 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 548961101 233 GKYkMNPRQWSHISESAKDLVRRMLMLDPAERI---TVYEALNHPWLKERD 280
Cdd:cd05609  230 DEI-EWPEGDDALPDDAQDLITRLLQQNPLERLgtgGAEEVKQHPFFQDLD 279
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-276 5.26e-32

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: 125.63  E-value: 5.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEdlkREASICHMLKHPHIVELLETYSS-DGMLYMV 90
Cdd:cd08223    2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAE---QEAKLLSKLKHPNIVSYKESFEGeDGFLYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLCFEIvkRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQLG 170
Cdd:cd08223   79 MGFCEGGDLYTRL--KEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLT---KSNIIKVGDLGIARVLE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMNPRQWshiSESA 249
Cdd:cd08223  154 SSSDMATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDmNSLVYKILEGKLPPMPKQY---SPEL 230
                        250       260
                 ....*....|....*....|....*..
gi 548961101 250 KDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd08223  231 GELIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
10-275 6.26e-32

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: 126.33  E-value: 6.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQqfavkIVDVAKFTSSpglstED---LK----REASICHMLKHPHIVELLETYS 82
Cdd:cd07847    1 EKYEKLSKIGEGSYGVVFKCRNRETGQ-----IVAIKKFVES-----EDdpvIKkialREIRMLKQLKHPNLVNLIEVFR 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  83 SDGMLYMVFEFMDGADLcFEIVKradagfvYSEAVASHYMR----QILEALRYCHDNNIIHRDVKPHCVLLaSKENSapV 158
Cdd:cd07847   71 RKRKLHLVFEYCDHTVL-NELEK-------NPRGVPEHLIKkiiwQTLQAVNFCHKHNCIHRDVKPENILI-TKQGQ--I 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 159 KLGGFGVAIQLGESGLVAGGRVGTPHFMAPE-VVKREPYGKPVDVWGCGVILFILLSGClPFYGTK---ERLFEgIIKGK 234
Cdd:cd07847  140 KLCDFGFARILTGPGDDYTDYVATRWYRAPElLVGDTQYGPPVDVWAIGCVFAELLTGQ-PLWPGKsdvDQLYL-IRKTL 217
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101 235 YKMNPR---------------------------QWSHISESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd07847  218 GDLIPRhqqifstnqffkglsipepetreplesKFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
12-278 6.66e-32

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: 127.67  E-value: 6.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAV-KIVDVakFTSSpglstEDLK---REASICHMLK-HPHIVELLETYSSDGM 86
Cdd:cd07852    9 YEILKKLGKGAYGIVWKAIDKKTGEVVALkKIFDA--FRNA-----TDAQrtfREIMFLQELNdHPNIIKLLNVIRAEND 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 --LYMVFEFMDgADLcfEIVKRADagfvYSEAVASHY-MRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGF 163
Cdd:cd07852   82 kdIYLVFEYME-TDL--HAVIRAN----ILEDIHKQYiMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCR---VKLADF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 164 GVA-----IQLGESGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-----ERLFEGI-- 230
Cdd:cd07852  152 GLArslsqLEEDDENPVLTDYVATRWYRAPEIlLGSTRYTKGVDMWSVGCILGEMLLGKPLFPGTStlnqlEKIIEVIgr 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 231 --------IKGKY------KMNPRQ-------WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd07852  232 psaediesIQSPFaatmleSLPPSRpksldelFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQ 300
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
12-276 7.95e-32

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: 125.40  E-value: 7.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINrETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKH-PHIVELL--ETYSSDGMLY 88
Cdd:cd14131    3 YEILKQLGKGGSSKVYKVLN-PKKKIYALKRVDLEGADEQ---TLQSYKNEIELLKKLKGsDRIIQLYdyEVTDEDDYLY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGaDLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnsapVKLGGFGVA-- 166
Cdd:cd14131   79 MVMECGEI-DLATILKKKRPKPI--DPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKGR----LKLIDFGIAka 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQLGESGLVAGGRVGTPHFMAPEVVK--------REPY--GKPVDVWGCGVILFILLSGCLPFYgtkeRLFEGIIKGKYK 236
Cdd:cd14131  152 IQNDTTSIVRDSQVGTLNYMSPEAIKdtsasgegKPKSkiGRPSDVWSLGCILYQMVYGKTPFQ----HITNPIAKLQAI 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 548961101 237 MNPR---QWSHISE-SAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14131  228 IDPNheiEFPDIPNpDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
10-276 8.66e-32

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: 125.07  E-value: 8.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpGLSTEdLKREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd14116    5 EDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKA-GVEHQ-LRREVEIQSHLRHPNILRLYGYFHDATRVYL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQL 169
Cdd:cd14116   83 ILEYAPLGTVYRELQKLSK----FDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGS---AGELKIADFGWSVHA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPrqwsHISES 248
Cdd:cd14116  156 PSSRRTT--LCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEAnTYQETYKRISRVEFTFPD----FVTEG 229
                        250       260
                 ....*....|....*....|....*...
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14116  230 ARDLISRLLKHNPSQRPMLREVLEHPWI 257
PDZ_MPP6-MPP2-like cd10832
PDZ domain of membrane palmitoylated protein 6 (MPP6), MPP2, and related domains; PDZ (PSD-95 ...
483-563 8.94e-32

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: 118.48  E-value: 8.94e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 483 RLVQFQKNTDEPMGITLKMNElNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQtvEQLQKMLREMRGSITFKIV 562
Cdd:cd10832    1 RMVGIRKNPGEPLGVTVRLEE-GELVIARILHGGMIDRQGLLHVGDIIKEVNGVPVGSP--EQLQEMLKNASGSVTLKIL 77

                 .
gi 548961101 563 P 563
Cdd:cd10832   78 P 78
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
18-265 9.43e-32

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: 125.33  E-value: 9.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREasICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKI--ILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGEsGLVAG 177
Cdd:cd05577   79 DLKYHIYNVGTRGF--SEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGH---VRISDLGLAVEFKG-GKKIK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 178 GRVGTPHFMAPEVVKRE-PYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSH-ISESAKDLVRR 255
Cdd:cd05577  153 GRVGTHGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMAVEYPDsFSPEARSLCEG 232
                        250
                 ....*....|
gi 548961101 256 MLMLDPAERI 265
Cdd:cd05577  233 LLQKDPERRL 242
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
12-276 9.99e-32

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: 125.29  E-value: 9.99e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVR-----RCINRETGQQFAVKIVdvAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGM 86
Cdd:cd14076    3 YILGRTLGEGEFGKVKlgwplPKANHRSGVQVAIKLI--RRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 LYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVA 166
Cdd:cd14076   81 IGIVLEFVSGGEL-FDYILARRR---LKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRN---LVITDFGFA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQLGES-GLVAGGRVGTPHFMAPE-VVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKE--------RLFegiikgKY 235
Cdd:cd14076  154 NTFDHFnGDLMSTSCGSPCYAAPElVVSDSMYaGRKADIWSCGVILYAMLAGYLPFDDDPHnpngdnvpRLY------RY 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 548961101 236 KMN-PRQW-SHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14076  228 ICNtPLIFpEYVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
9-277 1.11e-31

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: 126.24  E-value: 1.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEdlKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd05632    1 KNTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMA--LNEKQILEKVNSQFVVNLAYAYETKDALC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQ 168
Cdd:cd05632   79 LVLTIMNGGDLKFHIYNMGNPGF--EEERALFYAAEILCGLEDLHRENTVYRDLKPENILL---DDYGHIRISDLGLAVK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWS-HISE 247
Cdd:cd05632  154 IPEGESIRG-RVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSaKFSE 232
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 548961101 248 SAKDLVRRMLMLDPAERITVY-----EALNHPWLK 277
Cdd:cd05632  233 EAKSICKMLLTKDPKQRLGCQeegagEVKRHPFFR 267
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
16-265 2.93e-31

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: 125.12  E-value: 2.93e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKI----VDVAKFTSSPGLStedlkrEASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd05595    1 KLLGKGTFGKVILVREKATGRYYAMKIlrkeVIIAKDEVAHTVT------ESRVLQNTRHPFLTALKYAFQTHDRLCFVM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGE 171
Cdd:cd05595   75 EYANGGELFFHLSRER----VFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLML---DKDGHIKITDFGLCKEGIT 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnPRQwshISESAK 250
Cdd:cd05595  148 DGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDhERLFELILMEEIRF-PRT---LSPEAK 223
                        250
                 ....*....|....*
gi 548961101 251 DLVRRMLMLDPAERI 265
Cdd:cd05595  224 SLLAGLLKKDPKQRL 238
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
17-277 3.54e-31

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: 124.00  E-value: 3.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGlstEDLK-REASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 95
Cdd:cd05605    7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKG---EAMAlNEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGESGLV 175
Cdd:cd05605   84 GGDLKFHIYNMGNPGF--EEERAVFYAAEITCGLEHLHSERIVYRDLKPENILL---DDHGHVRISDLGLAVEIPEGETI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 176 AGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSH-ISESAKDLVR 254
Cdd:cd05605  159 RG-RVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRRVKEDQEEYSEkFSEEAKSICS 237
                        250       260
                 ....*....|....*....|....*...
gi 548961101 255 RMLMLDPAERI-----TVYEALNHPWLK 277
Cdd:cd05605  238 QLLQKDPKTRLgcrgeGAEDVKSHPFFK 265
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
12-276 3.82e-31

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: 123.94  E-value: 3.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspgLSTED------LKREASICHMLKHPHIVELLETYSSDG 85
Cdd:cd07835    1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIR---------LETEDegvpstAIREISLLKELNHPNIVRLLDVVHSEN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 MLYMVFEFMDgADLcfeiVKRADA--GFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGF 163
Cdd:cd07835   72 KLYLVFEFLD-LDL----KKYMDSspLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGA---LKLADF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 164 GVAIQLGESGLVAGGRVGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLF-------EGI 230
Cdd:cd07835  144 GLARAFGVPVRTYTHEVVTLWYRAPEILLGSKhYSTPVDIWSVGCIFAEMVTRRPLFPGDSEidqlfRIFrtlgtpdEDV 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 231 IKG-----KYKMN-----PRQWSHI----SESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd07835  224 WPGvtslpDYKPTfpkwaRQDLSKVvpslDEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
18-272 4.57e-31

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: 123.12  E-value: 4.57e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVdvAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd14187   15 LGKGGFAKCYEITDADTKEVFAGKIV--PKSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGESGLVAG 177
Cdd:cd14187   93 SL-LELHKRRKA---LTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFL---NDDMEVKIGDFGLATKVEYDGERKK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 178 GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT--KERLFEgIIKGKYKMnPRqwsHISESAKDLVRR 255
Cdd:cd14187  166 TLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSclKETYLR-IKKNEYSI-PK---HINPVAASLIQK 240
                        250
                 ....*....|....*..
gi 548961101 256 MLMLDPAERITVYEALN 272
Cdd:cd14187  241 MLQTDPTARPTINELLN 257
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
11-274 5.07e-31

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: 122.80  E-value: 5.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd06613    1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKL-----EPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLG 170
Cdd:cd06613   76 MEYCGGGSLQ-DIYQVTGP---LSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTE---DGDVKLADFGVSAQLT 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAGGRVGTPHFMAPEVV---KREPYGKPVDVWGCGVILFILLSGCLPFYGTKER--LFegiIKGKYKMNP------ 239
Cdd:cd06613  149 ATIAKRKSFIGTPYWMAPEVAaveRKGGYDGKCDIWALGITAIELAELQPPMFDLHPMraLF---LIPKSNFDPpklkdk 225
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 548961101 240 RQWS---HisesakDLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd06613  226 EKWSpdfH------DFIKKCLTKNPKKRPTATKLLQHP 257
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
12-276 5.29e-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: 122.79  E-value: 5.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvaKFTSSPGLSTEDLKREASICHMLKHPHIVELLETY-SSDGMLYMV 90
Cdd:cd14163    2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIID--KSGGPEEFIQRFLPRELQIVERLDHKNIIHVYEMLeSADGKIYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLcFEIVKRadaGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnsapVKLGGFGVAIQLG 170
Cdd:cd14163   80 MELAEDGDV-FDCVLH---GGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFT----LKLTDFGFAKQLP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGL-VAGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEgiiKGKYKMNPRQWShIS 246
Cdd:cd14163  152 KGGReLSQTFCGSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPFDDTDipKMLCQ---QQKGVSLPGHLG-VS 227
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 247 ESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14163  228 RTCQDLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
10-276 7.13e-31

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: 123.76  E-value: 7.13e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftSSPGLSTEDLkREASICHMLKHPHIVELLETYSSD----- 84
Cdd:cd07864    7 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDN--EKEGFPITAI-REIKILRQLNHRSVVNLKEIVTDKqdald 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  85 -----GMLYMVFEFMDgadlcFEIVKRADAGFV-YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPV 158
Cdd:cd07864   84 fkkdkGAFYLVFEYMD-----HDLMGLLESGLVhFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILL---NNKGQI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 159 KLGGFGVA-IQLGESGLVAGGRVGTPHFMAPE-VVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERL-FEGIIKGKY 235
Cdd:cd07864  156 KLADFGLArLYNSEESRPYTNKVITLWYRPPElLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAqLELISRLCG 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548961101 236 KMNPRQW--------------------------SHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd07864  236 SPCPAVWpdviklpyfntmkpkkqyrrrlreefSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-274 8.14e-31

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: 122.15  E-value: 8.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDlkrEASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd08220    2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALN---EVKVLSMLHHPNIIEYYESFLEDKALMIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRADAgfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLGGFGVAIQLGE 171
Cdd:cd08220   79 EYAPGGTLFEYIQQRKGS--LLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTV--VKIGDFGISKILSS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLvAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSgclpfygtKERLFEG---------IIKGKYKMNPRQW 242
Cdd:cd08220  155 KSK-AYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELAS--------LKRAFEAanlpalvlkIMRGTFAPISDRY 225
                        250       260       270
                 ....*....|....*....|....*....|..
gi 548961101 243 shiSESAKDLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd08220  226 ---SEELRHLILSMLHLDPNKRPTLSEIMAQP 254
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
58-276 9.65e-31

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: 121.77  E-value: 9.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  58 DLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNI 137
Cdd:cd08221   45 DALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQKNQLF--PEEVVLWYLYQIVSAVSHIHKAGI 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 138 IHRDVKPHCVLLAskeNSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCL 217
Cdd:cd08221  123 LHRDIKTLNIFLT---KADLVKLGDFGISKVLDSESSMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKR 199
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 218 PFYGTKE-RLFEGIIKGKYKMNPRQWshiSESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd08221  200 TFDATNPlRLAVKIVQGEYEDIDEQY---SEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
12-274 9.89e-31

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: 122.80  E-value: 9.89e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPglSTEDLK----REASICHMLKHPHIVELLETYSSDGML 87
Cdd:cd07848    3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIK-----KFKDSE--ENEEVKettlRELKMLRTLKQENIVELKEAFRRRGKL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLcfEIVKRADAGfVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnsaPVKLGGFGVAI 167
Cdd:cd07848   76 YLVFEYVEKNML--ELLEEMPNG-VPPEKVRS-YIYQLIKAIHWCHKNDIVHRDIKPENLLISHND---VLKLCDFGFAR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGE-SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE--RLFE-----GIIKGK----Y 235
Cdd:cd07848  149 NLSEgSNANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEidQLFTiqkvlGPLPAEqmklF 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 548961101 236 KMNPR-------QWSH-----------ISESAKDLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd07848  229 YSNPRfhglrfpAVNHpqslerrylgiLSGVLLDLMKNLLKLNPTDRYLTEQCLNHP 285
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
17-265 1.17e-30

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: 123.58  E-value: 1.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKIvdvakftsspgLSTEDLKREASICHM----------LKHPHIVELLETYSSDGM 86
Cdd:cd05575    2 VIGKGSFGKVLLARHKAEGKLYAVKV-----------LQKKAILKRNEVKHImaernvllknVKHPFLVGLHYSFQTKDK 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 LYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGva 166
Cdd:cd05575   71 LYFVLDYVNGGELFFHLQRER----HFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGH---VVLTDFG-- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 iqLGESGLVAGGRV----GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG--TKErLFEGIIKGKYKMNPr 240
Cdd:cd05575  142 --LCKEGIEPSDTTstfcGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSrdTAE-MYDNILHKPLRLRT- 217
                        250       260
                 ....*....|....*....|....*
gi 548961101 241 qwsHISESAKDLVRRMLMLDPAERI 265
Cdd:cd05575  218 ---NVSPSARDLLEGLLQKDRTKRL 239
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
12-276 1.31e-30

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: 122.14  E-value: 1.31e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspgLSTED------LKREASICHMLKHPHIVELLETYSSDG 85
Cdd:cd07861    2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIR---------LESEEegvpstAIREISLLKELQHPNIVCLEDVLMQEN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 MLYMVFEFmdgadLCFEIVKRADA----GFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLG 161
Cdd:cd07861   73 RLYLVFEF-----LSMDLKKYLDSlpkgKYMDAELVKS-YLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGV---IKLA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 162 GFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLF-------E 228
Cdd:cd07861  144 DFGLARAFGIPVRVYTHEVVTLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHGDSEidqlfRIFrilgtptE 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 229 GIIKG-----KYKMNPRQWS---------HISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd07861  224 DIWPGvtslpDYKNTFPKWKkgslrtavkNLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
16-280 1.32e-30

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: 123.48  E-value: 1.32e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIV--DVAkftsspgLSTEDL------KREASICHmlKHPHIVELLETYSSDGML 87
Cdd:cd05590    1 RVLGKGSFGKVMLARLKESGRLYAVKVLkkDVI-------LQDDDVectmteKRILSLAR--NHPFLTQLYCCFQTPDRL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAI 167
Cdd:cd05590   72 FFVMEFVNGGDLMFHIQKSRR----FDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLL---DHEGHCKLADFGMCK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNprQWshIS 246
Cdd:cd05590  145 EGIFNGKTTSTFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAeNEDDLFEAILNDEVVYP--TW--LS 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 548961101 247 ESAKDLVRRMLMLDPAERITVYE------ALNHPWLKERD 280
Cdd:cd05590  221 QDAVDILKAFMTKNPTMRLGSLTlggeeaILRHPFFKELD 260
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
12-275 1.50e-30

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: 121.63  E-value: 1.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVV---RRcinRETGQQFAVKIVDVAKftsspglsTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd14010    2 YVLYDEIGRGKHSVVykgRR---KGTIEFVAIKCVDKSK--------RPEVLNEVRLTHELKHPNVLKFYEWYETSNHLW 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLcfEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQ 168
Cdd:cd14010   71 LVVEYCTGGDL--ETLLRQDGNL--PESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILL---DGNGTLKLSDFGLARR 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGES-----GLVAG-----------GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGII 231
Cdd:cd14010  144 EGEIlkelfGQFSDegnvnkvskkqAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESfTELVEKIL 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 548961101 232 KGKYK-MNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHP-W 275
Cdd:cd14010  224 NEDPPpPPPKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
12-275 1.91e-30

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: 121.82  E-value: 1.91e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTedlkREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd07836    2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEEGTPSTAI----REISLMKELKHENIVRLHDVIHTENKLMLVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGaDLCFEIVKRADAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQLGE 171
Cdd:cd07836   78 EYMDK-DLKKYMDTHGVRGALDPNTVKS-FTYQLLKGIAFCHENRVLHRDLKPQNLLINKR---GELKLADFGLARAFGI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGT----------------KERLFEGI---- 230
Cdd:cd07836  153 PVNTFSNEVVTLWYRAPDVlLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTnnedqllkifrimgtpTESTWPGIsqlp 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 548961101 231 -IKGKYKMNPRQ-----WSHISESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd07836  233 eYKPTFPRYPPQdlqqlFPHADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
12-280 4.14e-30

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: 121.95  E-value: 4.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftsspgLSTEDLKREaSICHM---------LKHPHIVELLETYS 82
Cdd:cd05599    3 FEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKL----------RKSEMLEKE-QVAHVraerdilaeADNPWVVKLYYSFQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  83 SDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGG 162
Cdd:cd05599   72 DEENLYLIMEFLPGGDMMTLLMKKD----TLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGH---IKLSD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 163 FGVAIQLGESGLvAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGtkerlfEGIIKGKYK-MNPRQ 241
Cdd:cd05599  145 FGLCTGLKKSHL-AYSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCS------DDPQETCRKiMNWRE 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 548961101 242 W------SHISESAKDLVRRmLMLDPAERI---TVYEALNHPWLKERD 280
Cdd:cd05599  218 TlvfppeVPISPEAKDLIER-LLCDAEHRLganGVEEIKSHPFFKGVD 264
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
12-275 4.79e-30

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: 120.50  E-value: 4.79e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstEDLK--------REASICHMLKHPHIVELLETYSS 83
Cdd:cd13990    2 YLLLNLLGKGGFSEVYKAFDLVEQRYVACKIHQLNKDWS------EEKKqnyikhalREYEIHKSLDHPRIVKLYDVFEI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 D-GMLYMVFEFMDGADLCFeIVKRADagfVYSEAVASHYMRQILEALRYC--HDNNIIHRDVKPHCVLLASKENSAPVKL 160
Cdd:cd13990   76 DtDSFCTVLEYCDGNDLDF-YLKQHK---SIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNVSGEIKI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 161 GGFGVAIQLGESGLVAGGR------VGTPHFMAPE--VVKREP--YGKPVDVWGCGVILFILLSGCLPFyG---TKER-L 226
Cdd:cd13990  152 TDFGLSKIMDDESYNSDGMeltsqgAGTYWYLPPEcfVVGKTPpkISSKVDVWSVGVIFYQMLYGRKPF-GhnqSQEAiL 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 548961101 227 FEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd13990  231 EENTILKATEVEFPSKPVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
SH3_MPP cd11862
Src Homology 3 domain of Membrane Protein, Palmitoylated (or MAGUK p55 subfamily member) ...
610-670 6.89e-30

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: 112.29  E-value: 6.89e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548961101 610 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPE 670
Cdd:cd11862    1 FVRALFDYDPEEDPLIPCKEAGLSFKKGDILQIVNQDDPNWWQARKVGDPNGRAGLIPSQD 61
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
12-275 6.98e-30

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: 120.30  E-value: 6.98e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkfTSSPGLSTEDLkREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd07860    2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLD--TETEGVPSTAI-REISLLKELNHPNIVKLLDVIHTENKLYLVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDgADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGE 171
Cdd:cd07860   79 EFLH-QDLKKFMDASALTGI--PLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLI---NTEGAIKLADFGLARAFGV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFEGI--------------- 230
Cdd:cd07860  153 PVRTYTHEVVTLWYRAPEIlLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEidqlfRIFRTLgtpdevvwpgvtsmp 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 548961101 231 -IKGKYKMNPRQ-WSHI----SESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd07860  233 dYKPSFPKWARQdFSKVvpplDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
736-904 8.22e-30

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: 116.44  E-value: 8.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  736 LVLLGAHGVGRRHIKNTLITKHPDrFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLE 815
Cdd:TIGR03263   3 IVISGPSGAGKSTLVKALLEEDPN-LKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTPKS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  816 TIRKIHEQGLIAILDVEPQ-ALKVLRTAEFAPFvVFIAAPTItpglneDESLQRLQK-----ESDVLQR--------TYA 881
Cdd:TIGR03263  82 PVEEALAAGKDVLLEIDVQgARQVKKKFPDAVS-IFILPPSL------EELERRLRKrgtdsEEVIERRlakakkeiAHA 154
                         170       180
                  ....*....|....*....|...
gi 548961101  882 HYFDLTIINNEIDETIRHLEEAV 904
Cdd:TIGR03263 155 DEFDYVIVNDDLEKAVEELKSII 177
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
18-274 8.34e-30

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: 119.01  E-value: 8.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRE-TGQQFAVKIVDVAKFTSSPGLstedLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDG 96
Cdd:cd14120    1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKSQNL----LGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  97 ADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLL--ASKENSAP----VKLGGFGVAIQLg 170
Cdd:cd14120   77 GDLADYLQAKG----TLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLshNSGRKPSPndirLKIADFGFARFL- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLfegiiKGKYKMN----PRQWSHI 245
Cdd:cd14120  152 QDGMMAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAqTPQEL-----KAFYEKNanlrPNIPSGT 226
                        250       260
                 ....*....|....*....|....*....
gi 548961101 246 SESAKDLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd14120  227 SPALKDLLLGLLKRNPKDRIDFEDFFSHP 255
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
16-276 1.14e-29

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: 118.96  E-value: 1.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQ-QFAVKIVDVAKFTSSPGLstedLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFM 94
Cdd:cd14202    8 DLIGHGAFAVVFKGRHKEKHDlEVAVKCINKKNLAKSQTL----LGKEIKILKELKHENIVALYDFQEIANSVYLVMEYC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  95 DGADLcfeivkradAGFVYSEAVASH-----YMRQILEALRYCHDNNIIHRDVKPHCVLLA------SKENSAPVKLGGF 163
Cdd:cd14202   84 NGGDL---------ADYLHTMRTLSEdtirlFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrkSNPNNIRIKIADF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 164 GVAIQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWS 243
Cdd:cd14202  155 GFARYL-QNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPNIPR 233
                        250       260       270
                 ....*....|....*....|....*....|...
gi 548961101 244 HISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14202  234 ETSSHLRQLLLGLLQRNQKDRMDFDEFFHHPFL 266
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
17-281 1.15e-29

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: 118.99  E-value: 1.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVakfTSSPGLSTEDLkREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDG 96
Cdd:cd06605    8 ELGEGNGGVVSKVRHRPSGQIMAVKVIRL---EIDEALQKQIL-RELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  97 ADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHDN-NIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESglV 175
Cdd:cd06605   84 GSLD-KILKEVGR---IPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQ---VKLCDFGVSGQLVDS--L 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 176 AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF-------YGTKERLFEGIIKGKykmNPRQWSHI-SE 247
Cdd:cd06605  155 AKTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYpppnakpSMMIFELLSYIVDEP---PPLLPSGKfSP 231
                        250       260       270
                 ....*....|....*....|....*....|....
gi 548961101 248 SAKDLVRRMLMLDPAERITVYEALNHPWLKERDR 281
Cdd:cd06605  232 DFQDFVSQCLQKDPTERPSYKELMEHPFIKRYEY 265
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
18-275 1.37e-29

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: 118.58  E-value: 1.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKivdvakFTSSPGLSTEDLKREASI-CHMLKHPHIVELLETY-SSDGMLYMVFEFMD 95
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALK------FVPKPSTKLKDFLREYNIsLELSVHPHIIKTYDVAfETEDYYVFAQEYAP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLcFEIVKrADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGFGVAIQlgesglv 175
Cdd:cd13987   75 YGDL-FSIIP-PQVGL--PEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRR-VKLCDFGLTRR------- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 176 AGGRV----GTPHFMAPEV---VKREPY--GKPVDVWGCGVILFILLSGCLP---------FYgtkeRLFEGIIKGKYKM 237
Cdd:cd13987  143 VGSTVkrvsGTIPYTAPEVceaKKNEGFvvDPSIDVWAFGVLLFCCLTGNFPwekadsddqFY----EEFVRWQKRKNTA 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 548961101 238 NPRQWSHISESAKDLVRRMLMLDPAERIT---VYEALNHPW 275
Cdd:cd13987  219 VPSQWRRFTPKALRMFKKLLAPEPERRCSikeVFKYLGDRW 259
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
12-274 2.03e-29

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: 118.85  E-value: 2.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELcEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREasICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd05607    5 YEF-RVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKE--ILEKVNSPFIVSLAYAFETKTHLCLVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 171
Cdd:cd05607   82 SLMNGGDLKYHIYNVGERGIEMERVI--FYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGN---CRLSDLGLAVEVKE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 sGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSH--ISESA 249
Cdd:cd05607  157 -GKPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELKRRTLEDEVKFEHqnFTEEA 235
                        250       260
                 ....*....|....*....|....*
gi 548961101 250 KDLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd05607  236 KDICRLFLAKKPENRLGSRTNDDDP 260
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-276 2.76e-29

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: 117.91  E-value: 2.76e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKI---VDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd08222    2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVlkeISVGELQPD---ETVDANREAKLLSKLDHPAIVKFHDSFVEKESFC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLasKENSapVKLGGFGVAIQ 168
Cdd:cd08222   79 IVTEYCEGGDLDDKISEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL--KNNV--IKVGDFGISRI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLsgCLpfygtkERLFEG---------IIKGKykmNP 239
Cdd:cd08222  155 LMGTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMC--CL------KHAFDGqnllsvmykIVEGE---TP 223
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 548961101 240 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd08222  224 SLPDKYSKELNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
12-277 3.51e-29

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: 117.34  E-value: 3.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsSPglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd06647    9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQ---QP--KKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCfEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGE 171
Cdd:cd06647   84 EYLAGGSLT-DVVTET----CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGM---DGSVKLTDFGFCAQITP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKD 251
Cdd:cd06647  156 EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRD 235
                        250       260
                 ....*....|....*....|....*.
gi 548961101 252 LVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd06647  236 FLNRCLEMDVEKRGSAKELLQHPFLK 261
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
12-276 7.54e-29

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: 116.60  E-value: 7.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakfTSSPGLSTEDLKrEASICHMLK------HPHIVELLETYSSDG 85
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKII-----KNNKDYLDQSLD-EIRLLELLNkkdkadKYHIVRLKDVFYFKN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 MLYMVFEfMDGADLcFEIVKraDAGFVY-SEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGFG 164
Cdd:cd14133   75 HLCIVFE-LLSQNL-YEFLK--QNKFQYlSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQ-IKIIDFG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 165 VAIQLGEsglvaggRVGT----PHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFEGIIKGKY 235
Cdd:cd14133  150 SSCFLTQ-------RLYSyiqsRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEvdqlaRIIGTIGIPPA 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 548961101 236 KMnprqwshISESA------KDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14133  223 HM-------LDQGKaddelfVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
10-277 1.01e-28

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: 117.02  E-value: 1.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstEDLKREASICHML-KHPHIVELLET-YSSD--- 84
Cdd:cd06639   22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVD------EEIEAEYNILRSLpNHPNVVKFYGMfYKADqyv 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  85 -GMLYMVFEFMDGADLCfEIVKRA-DAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGG 162
Cdd:cd06639   96 gGQLWLVLELCNGGSVT-ELVKGLlKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE---GGVKLVD 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 163 FGVAIQLGESGLVAGGRVGTPHFMAPEVVKRE-----PYGKPVDVWGCGVILFILLSGCLPFYGTKErlfegiIKGKYK- 236
Cdd:cd06639  172 FGVSAQLTSARLRRNTSVGTPFWMAPEVIACEqqydySYDARCDVWSLGITAIELADGDPPLFDMHP------VKALFKi 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 548961101 237 --------MNPRQWshiSESAKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd06639  246 prnppptlLNPEKW---CRGFSHFISQCLIKDFEKRPSVTHLLEHPFIK 291
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
17-265 1.35e-28

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: 116.52  E-value: 1.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDG 96
Cdd:cd05608    8 VLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGY--EGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  97 ADLCFEI--VKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGESGL 174
Cdd:cd05608   86 GDLRYHIynVDEENPGF--QEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLL---DDDGNVRISDLGLAVELKDGQT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 175 VAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWS-HISESAKDLV 253
Cdd:cd05608  161 KTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEKVENKELKQRILNDSVTYSeKFSPASKSIC 240
                        250
                 ....*....|..
gi 548961101 254 RRMLMLDPAERI 265
Cdd:cd05608  241 EALLAKDPEKRL 252
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
12-257 1.55e-28

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: 117.86  E-value: 1.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvAKFtsspglstEDLKREASIC-----HMLKH---PHIVELLETYSS 83
Cdd:cd05596   28 FDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLL--SKF--------EMIKRSDSAFfweerDIMAHansEWIVQLHYAFQD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLYMVFEFMDGADLCfEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGF 163
Cdd:cd05596   98 DKYLYMVMDYMPGGDLV-NLMSNYD----VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDA---SGHLKLADF 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 164 GVAIQLGESGLV-AGGRVGTPHFMAPEVVKREP----YGKPVDVWGCGVILFILLSGCLPFY-----GTkerlFEGIIKG 233
Cdd:cd05596  170 GTCMKMDKDGLVrSDTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYadslvGT----YGKIMNH 245
                        250       260
                 ....*....|....*....|....
gi 548961101 234 KYKMNPRQWSHISESAKDLVRRML 257
Cdd:cd05596  246 KNSLQFPDDVEISKDAKSLICAFL 269
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
9-276 1.55e-28

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: 116.28  E-value: 1.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakfTSSPGlSTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd06643    4 EDFWEIVGELGDGAFGKVYKAQNKETGILAAAKVID----TKSEE-ELEDYMVEIDILASCDHPNIVKLLDAFYYENNLW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGA--DLCFEIVKRAdagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVA 166
Cdd:cd06643   79 ILIEFCAGGavDAVMLELERP-----LTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGD---IKLADFGVS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQLGESGLVAGGRVGTPHFMAPEVV-----KREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKM--N 238
Cdd:cd06643  151 AKNTRTLQRRDSFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPmRVLLKIAKSEPPTlaQ 230
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 548961101 239 PRQWshiSESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd06643  231 PSRW---SPEFKDFLRKCLEKNVDARWTTSQLLQHPFV 265
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
12-277 1.97e-28

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: 116.36  E-value: 1.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsSPglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd06655   21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQK---QP--KKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCfEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQLGE 171
Cdd:cd06655   96 EYLAGGSLT-DVVTET----CMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMD---GSVKLTDFGFCAQITP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEGIIKGKYKM-NPRQWSHIses 248
Cdd:cd06655  168 EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENplRALYLIATNGTPELqNPEKLSPI--- 244
                        250       260
                 ....*....|....*....|....*....
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd06655  245 FRDFLNRCLEMDVEKRGSAKELLQHPFLK 273
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
17-265 2.14e-28

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: 116.73  E-value: 2.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFS---VVRRCINRETGQQFAVKIVDVAKFTSSPGLSTedlKREASICHMLKHPHIVELLETYSSDGMLYMVFEF 93
Cdd:cd05582    2 VLGQGSFGkvfLVRKITGPDAGTLYAMKVLKKATLKVRDRVRT---KMERDILADVNHPFIVKLHYAFQTEGKLYLILDF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  94 MDGADLCFEIVKRadagFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGESG 173
Cdd:cd05582   79 LRGGDLFTRLSKE----VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDE---DGHIKLTDFGLSKESIDHE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 174 LVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT-KERLFEGIIKGKYKMnPRqwsHISESAKDL 252
Cdd:cd05582  152 KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKdRKETMTMILKAKLGM-PQ---FLSPEAQSL 227
                        250
                 ....*....|...
gi 548961101 253 VRRMLMLDPAERI 265
Cdd:cd05582  228 LRALFKRNPANRL 240
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-270 3.39e-28

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: 114.91  E-value: 3.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQF-AVKIVdvakFTSSPGLSTEDLKREASICHM----------LKHPHIVELLET 80
Cdd:cd08528    2 YAVLELLGSGAFGCVYKVRKKSNGQTLlALKEI----NMTNPAFGRTEQERDKSVGDIisevniikeqLRHPNIVRYYKT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  81 YSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCH-DNNIIHRDVKPHCVLLASKENsapVK 159
Cdd:cd08528   78 FLENDRLYIVMELIEGAPLGEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDK---VT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 160 LGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKmn 238
Cdd:cd08528  155 ITDFGLAKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMlTLATKIVEAEYE-- 232
                        250       260       270
                 ....*....|....*....|....*....|..
gi 548961101 239 PRQWSHISESAKDLVRRMLMLDPAERITVYEA 270
Cdd:cd08528  233 PLPEGMYSDDITFVIRSCLTPDPEARPDIVEV 264
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
736-901 5.25e-28

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: 109.93  E-value: 5.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 736 LVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLE 815
Cdd:cd00071    2 IVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSKA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 816 TIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPtitpglnedeslqrlqkesdvlqrtyahyfDLTIINNEIDE 895
Cdd:cd00071   82 AVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP------------------------------DYVIVNDDLEK 131

                 ....*.
gi 548961101 896 TIRHLE 901
Cdd:cd00071  132 AYEELK 137
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
12-272 5.35e-28

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: 114.37  E-value: 5.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIV--------DVAKFTSSPGLSTEDLKREASichmlKHPHIVELLETYSS 83
Cdd:cd13993    2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLyksgpnskDGNDFQKLPQLREIDLHRRVS-----RHPNIITLHDVFET 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLYMVFEFMDGADLcFEIVkRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLGGF 163
Cdd:cd13993   77 EVAIYIVLEYCPNGDL-FEAI-TENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGT--VKLCDF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 164 GVAIQLGESGLVaggRVGTPHFMAPEV------VKREPYGKPVDVWGCGVILFILLSGCLPF-------------YGTKE 224
Cdd:cd13993  153 GLATTEKISMDF---GVGSEFYMAPECfdevgrSLKGYPCAAGDIWSLGIILLNLTFGRNPWkiasesdpifydyYLNSP 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 548961101 225 RLFegiikgkykmnpRQWSHISESAKDLVRRMLMLDPAERITVYEALN 272
Cdd:cd13993  230 NLF------------DVILPMSDDFYNLLRQIFTVNPNNRILLPELQL 265
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
12-275 5.59e-28

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: 115.49  E-value: 5.59e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVK--IVDVAKftssPGLSTEDLkREASICHMLKHPHIVELLE--------TY 81
Cdd:cd07866   10 YEILGKLGEGTFGEVYKARQIKTGRVVALKkiLMHNEK----DGFPITAL-REIKILKKLKHPNVVPLIDmaverpdkSK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  82 SSDGMLYMVFEFMDgADLCfEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLG 161
Cdd:cd07866   85 RKRGSVYMVTPYMD-HDLS-GLLENPSVKL--TESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGI---LKIA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 162 GFGVA------IQLGESGLVAGGR-----VGTPHFMAPEVV---KRepYGKPVDVWGCGVILFILLSG------------ 215
Cdd:cd07866  158 DFGLArpydgpPPNPKGGGGGGTRkytnlVVTRWYRPPELLlgeRR--YTTAVDIWGIGCVFAEMFTRrpilqgksdidq 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 216 -------C-------------LPfyGTKERLFEGIIKGKYKMnpRQWSHISESAkDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd07866  236 lhlifklCgtpteetwpgwrsLP--GCEGVHSFTNYPRTLEE--RFGKLGPEGL-DLLSKLLSLDPYKRLTASDALEHPY 310
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
18-277 7.74e-28

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: 114.37  E-value: 7.74e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd06658   30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRR-----ELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLCfEIVKRADAGfvySEAVASHYMrQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGESGLVAG 177
Cdd:cd06658  105 ALT-DIVTHTRMN---EEQIATVCL-SVLRALSYLHNQGVIHRDIKSDSILLTS---DGRIKLSDFGFCAQVSKEVPKRK 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 178 GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYgtKERLFEGIIKGKYKMNPR-QWSH-ISESAKDLVRR 255
Cdd:cd06658  177 SLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYF--NEPPLQAMRRIRDNLPPRvKDSHkVSSVLRGFLDL 254
                        250       260
                 ....*....|....*....|..
gi 548961101 256 MLMLDPAERITVYEALNHPWLK 277
Cdd:cd06658  255 MLVREPSQRATAQELLQHPFLK 276
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
10-278 9.68e-28

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: 114.36  E-value: 9.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakfTSSPGlSTEDLKREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd06644   12 EVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIE----TKSEE-ELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLCfEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQL 169
Cdd:cd06644   87 MIEFCPGGAVD-AIMLELDRGL--TEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGD---IKLADFGVSAKN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAGGRVGTPHFMAPEVV-----KREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYK--MNPRQ 241
Cdd:cd06644  161 VKTLQRRDSFIGTPYWMAPEVVmcetmKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPmRVLLKIAKSEPPtlSQPSK 240
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 548961101 242 WshiSESAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd06644  241 W---SMEFRDFLKTALDKHPETRPSAAQLLEHPFVSS 274
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
10-276 1.03e-27

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: 113.55  E-value: 1.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsspglsTEDLKREasICH---MLK----HPHIVELLETY- 81
Cdd:cd06608    6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDI----------IEDEEEE--IKLeinILRkfsnHPNIATFYGAFi 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  82 -----SSDGMLYMVFEFMDGADLCfEIVKRA-DAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNS 155
Cdd:cd06608   74 kkdppGGDDQLWLVMEYCGGGSVT-DLVKGLrKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLT---EE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 156 APVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVV----KREP-YGKPVDVWGCGVILFILLSGCLPF---YGTKErLF 227
Cdd:cd06608  150 AEVKLVDFGVSAQLDSTLGRRNTFIGTPYWMAPEVIacdqQPDAsYDARCDVWSLGITAIELADGKPPLcdmHPMRA-LF 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 548961101 228 EgIIKGKYK--MNPRQWSHiseSAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd06608  229 K-IPRNPPPtlKSPEKWSK---EFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
18-264 1.32e-27

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: 113.20  E-value: 1.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVakFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd08228   10 IGRGQFSEVYRATCLLDRKPVALKKVQI--FEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELADAG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGESGLVAG 177
Cdd:cd08228   88 DLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITA---TGVVKLGDLGLGRFFSSKTTAAH 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 178 GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLF---EGIIKGKYKMNPRQwsHISESAKDLVR 254
Cdd:cd08228  165 SLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFslcQKIEQCDYPPLPTE--HYSEKLRELVS 242
                        250
                 ....*....|
gi 548961101 255 RMLMLDPAER 264
Cdd:cd08228  243 MCIYPDPDQR 252
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
9-276 1.47e-27

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: 112.70  E-value: 1.47e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLstedlkREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd14110    2 EKTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQLVL------REYQVLRRLSHPRIAQLHSAYLSPRHLV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnsaPVKLGGFGVAIQ 168
Cdd:cd14110   76 LIEELCSGPELLYNLAERN----SYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKN---LLKIVDLGNAQP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LG-ESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY--GTKERLfEGIIKGKYKMNpRQWSHI 245
Cdd:cd14110  149 FNqGKVLMTDKKGDYVETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSsdLNWERD-RNIRKGKVQLS-RCYAGL 226
                        250       260       270
                 ....*....|....*....|....*....|.
gi 548961101 246 SESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14110  227 SGGAVNFLKSTLCAKPWGRPTASECLQNPWL 257
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
17-280 1.48e-27

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: 114.40  E-value: 1.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKIV--DVAkftsspgLSTEDLKreasiCHML---------KHPHIVELLETYSSDG 85
Cdd:cd05592    2 VLGKGSFGKVMLAELKGTNQYFAIKALkkDVV-------LEDDDVE-----CTMIerrvlalasQHPFLTHLFCTFQTES 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 MLYMVFEFMDGADLCFEIvkrADAGfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSapVKLGGFGV 165
Cdd:cd05592   70 HLFFVMEYLNGGDLMFHI---QQSG-RFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLL-DREGH--IKIADFGM 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 166 AIQ--LGESglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIikgkykMNPRQW 242
Cdd:cd05592  143 CKEniYGEN--KASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEdELFWSI------CNDTPH 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 548961101 243 --SHISESAKDLVRRMLMLDPAERITVYEAL-----NHPWLKERD 280
Cdd:cd05592  215 ypRWLTKEAASCLSLLLERNPEKRLGVPECPagdirDHPFFKTID 259
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
736-905 1.55e-27

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 110.54  E-value: 1.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 736 LVLLGAHGVGRRHIKNTLITKHPDrFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLE 815
Cdd:COG0194    5 IVLSGPSGAGKTTLVKALLERDPD-LRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGTPKA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 816 TIRKIHEQGLIAILDVEPQ-ALKVLRTAEFAPFvVFIAAPTItpglneDESLQRL----QKESDVLQR---------TYA 881
Cdd:COG0194   84 EVEEALAAGKDVLLEIDVQgARQVKKKFPDAVS-IFILPPSL------EELERRLrgrgTDSEEVIERrlakareelAHA 156
                        170       180
                 ....*....|....*....|....
gi 548961101 882 HYFDLTIINNEIDETIRHLEEAVE 905
Cdd:COG0194  157 DEFDYVVVNDDLDRAVEELKAIIR 180
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
10-275 1.67e-27

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: 113.47  E-value: 1.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvaKFTSS-PGLSTEDLkREASICHMLKHPHIVELLETYSSDGM-- 86
Cdd:cd07843    5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKL---KMEKEkEGFPITSL-REINILLKLQHPNIVTVKEVVVGSNLdk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 LYMVFEFMDgADLCfEIVKRADAGFVYSEaVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVA 166
Cdd:cd07843   81 IYMVMEYVE-HDLK-SLMETMKQPFLQSE-VKC-LMLQLLSGVAHLHDNWILHRDLKTSNLLL---NNRGILKICDFGLA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQLGESGLVAGGRVGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLF-------EGI--- 230
Cdd:cd07843  154 REYGSPLKPYTQLVVTLWYRAPELLLGAKeYSTAIDMWSVGCIFAELLTKKPLFPGKSEidqlnKIFkllgtptEKIwpg 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 231 ------IKGKYKMNPRQW--------SHISESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd07843  234 fselpgAKKKTFTKYPYNqlrkkfpaLSLSDNGFDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
10-276 1.72e-27

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: 112.32  E-value: 1.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRET-------GQQFAVKIVDVakfTSSPglstEDLKREASICHMLK-HPHIVELLETY 81
Cdd:cd14019    1 NKYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIYP---TSSP----SRILNELECLERLGgSNNVSGLITAF 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  82 SSDGMLYMVFEFMDGADlcfeivkRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSAPVkLG 161
Cdd:cd14019   74 RNEDQVVAVLPYIEHDD-------FRDFYRKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLY-NRETGKGV-LV 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 162 GFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKERlFEGIIkgkykmnpr 240
Cdd:cd14019  145 DFGLAQREEDRPEQRAPRAGTRGFRAPEVLFKCPHqTTAIDIWSAGVILLSILSGRFPFFFSSDD-IDALA--------- 214
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 548961101 241 QWSHI--SESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14019  215 EIATIfgSDEAYDLLDKLLELDPSKRITAEEALKHPFF 252
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
12-275 2.58e-27

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: 113.23  E-value: 2.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftSSPGLSTEDLkREASICHMLKHPHIVELLETYSSD------- 84
Cdd:cd07865   14 YEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMEN--EKEGFPITAL-REIKILQLLKHENVVNLIEICRTKatpynry 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  85 -GMLYMVFEFMDgADLcfeivkradAGFV------YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKEnsAP 157
Cdd:cd07865   91 kGSIYLVFEFCE-HDL---------AGLLsnknvkFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILI-TKD--GV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 158 VKLGGFGVA----IQLGESGLVAGGRVGTPHFMAPEVVKRE-PYGKPVDVWGCGVI---------------------LFI 211
Cdd:cd07865  158 LKLADFGLArafsLAKNSQPNRYTNRVVTLWYRPPELLLGErDYGPPIDMWGAGCImaemwtrspimqgnteqhqltLIS 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548961101 212 LLSGC-----------LPFYgTKERLFEGiikGKYKMNPRQWSHISE-SAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd07865  238 QLCGSitpevwpgvdkLELF-KKMELPQG---QKRKVKERLKPYVKDpYALDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
10-278 3.50e-27

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: 113.93  E-value: 3.50e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKivdvaKFtSSPGLSTEDLK---REASICHMLKHPHIVELLETYSSDGM 86
Cdd:cd07851   15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIK-----KL-SRPFQSAIHAKrtyRELRLLKHMKHENVIGLLDVFTPASS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 L------YMVFEFMdGADLcFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCvlLASKENSApVKL 160
Cdd:cd07851   89 LedfqdvYLVTHLM-GADL-NNIVKCQ----KLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSN--LAVNEDCE-LKI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 161 GGFGVAIQLGESglvAGGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGT----------------K 223
Cdd:cd07851  160 LDFGLARHTDDE---MTGYVATRWYRAPEIMlNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSdhidqlkrimnlvgtpD 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548961101 224 ERLFEGI--------IKGKYKMNPRQWSHI----SESAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd07851  237 EELLKKIssesarnyIQSLPQMPKKDFKEVfsgaNPLAIDLLEKMLVLDPDKRITAAEALAHPYLAE 303
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
12-278 3.89e-27

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: 112.21  E-value: 3.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVK-IVDVAKFTSspglstedlkREASICHMLKHPHIVELLE-TYSSDG---- 85
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKkVLQDKRYKN----------RELQIMRRLKHPNIVKLKYfFYSSGEkkde 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 -MLYMVFEFMDGaDLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLasKENSAPVKLGGFG 164
Cdd:cd14137   76 vYLNLVMEYMPE-TLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLV--DPETGVLKLCDFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 165 VAIQlgesgLVAGGR----VGTPHFMAPE-VVKREPYGKPVDVWGCG-VILFILLSGCLpFYGTK--ERLFEgIIK--GK 234
Cdd:cd14137  153 SAKR-----LVPGEPnvsyICSRYYRAPElIFGATDYTTAIDIWSAGcVLAELLLGQPL-FPGESsvDQLVE-IIKvlGT 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548961101 235 ------YKMNP------------RQWS-----HISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd14137  226 ptreqiKAMNPnytefkfpqikpHPWEkvfpkRTPPDAIDLLSKILVYNPSKRLTALEALAHPFFDE 292
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
13-264 4.03e-27

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: 111.49  E-value: 4.03e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101    13 ELCEVIGKGPFSVVRRCI----NRETGQQFAVKIVDVakftSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTlkgkGDGKEVEVAVKTLKE----DASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101    89 MVFEFMDGADLCFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQ 168
Cdd:smart00221  78 IVMEYMPGGDLLDYLRKNRPKELSLSDLL--SFALQIARGMEYLESKNFIHRDLAARNCLVGENLV---VKISDFGLSRD 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   169 LGESGL--VAGGRVgtP-HFMAPEVVKREPYGKPVDVWGCGVILFILLSGC-LPFYG-TKERLFEGIIKGKYKMNPrqws 243
Cdd:smart00221 153 LYDDDYykVKGGKL--PiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGeEPYPGmSNAEVLEYLKKGYRLPKP---- 226
                          250       260
                   ....*....|....*....|....
gi 548961101   244 hiSESAKDLVRRMLM---LDPAER 264
Cdd:smart00221 227 --PNCPPELYKLMLQcwaEDPEDR 248
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
16-275 5.61e-27

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: 111.33  E-value: 5.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDG--MLYMVFEF 93
Cdd:cd06651   13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAekTLTIFMEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  94 MDGAdlcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLlasKENSAPVKLGGFGVAIQLGE-- 171
Cdd:cd06651   93 MPGG----SVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDFGASKRLQTic 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 -SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFygTKERLFEGIIK-GKYKMNPRQWSHISESA 249
Cdd:cd06651  166 mSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW--AEYEAMAAIFKiATQPTNPQLPSHISEHA 243
                        250       260
                 ....*....|....*....|....*.
gi 548961101 250 KDLVRRmLMLDPAERITVYEALNHPW 275
Cdd:cd06651  244 RDFLGC-IFVEARHRPSAEELLRHPF 268
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
16-271 7.70e-27

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: 110.94  E-value: 7.70e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRetGQQFAVKIVdvaKFTSSPGLSTEDLKREASICHmLKHPHIVELL-----ETYSSDGMLYMv 90
Cdd:cd13979    9 EPLGSGGFGSVYKATYK--GETVAVKIV---RRRRKNRASRQSFWAELNAAR-LRHENIVRVLaaetgTDFASLGLIIM- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 fEFMDGADLCFEIVKRADAGFVYSEAVashYMRQILEALRYCHDNNIIHRDVKPHCVLLAskENSAPvKLGGFGVAIQLG 170
Cdd:cd13979   82 -EYCGNGTLQQLIYEGSEPLPLAHRIL---ISLDIARALRFCHSHGIVHLDVKPANILIS--EQGVC-KLCDFGCSVKLG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 EsGLVAGGRV----GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIkgKYKMNPRQwSHIS 246
Cdd:cd13979  155 E-GNEVGTPRshigGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYAVV--AKDLRPDL-SGLE 230
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 247 ESA-----KDLVRRMLMLDPAERITVYEAL 271
Cdd:cd13979  231 DSEfgqrlRSLISRCWSAQPAERPNADESL 260
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
12-265 9.12e-27

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: 112.87  E-value: 9.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKI----VDVAKFTSSPGLStedlkrEASICHMLKHPHIVELLETYSSDGML 87
Cdd:cd05593   17 FDYLKLLGKGTFGKVILVREKASGKYYAMKIlkkeVIIAKDEVAHTLT------ESRVLKNTRHPFLTSLKYSFQTKDRL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAI 167
Cdd:cd05593   91 CFVMEYVNGGELFFHLSRER----VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGLCK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnPRQwshIS 246
Cdd:cd05593  164 EGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDhEKLFELILMEDIKF-PRT---LS 239
                        250
                 ....*....|....*....
gi 548961101 247 ESAKDLVRRMLMLDPAERI 265
Cdd:cd05593  240 ADAKSLLSGLLIKDPNKRL 258
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
9-276 1.05e-26

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: 110.31  E-value: 1.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINR--ETGQQFAVKIVDvakftssPGLSTEDLKREASICHMLKHPHIVELLETYSSDGM 86
Cdd:cd14112    2 TGRFSFGSEIFRGRFSVIVKAVDSttETDAHCAVKIFE-------VSDEASEAVREFESLRTLQHENVQRLIAAFKPSNF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 LYMVFEfmdgaDLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnSAPVKLGGFGVA 166
Cdd:cd14112   75 AYLVME-----KLQEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVR-SWQVKLVDFGRA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQLGESGLVAGGrvGTPHFMAPEVVKREPYGKP-VDVWGCGVILFILLSGCLPF---YGTKERLFEGIIKGKYKMN--PR 240
Cdd:cd14112  149 QKVSKLGKVPVD--GDTDWASPEFHNPETPITVqSDIWGLGVLTFCLLSGFHPFtseYDDEEETKENVIFVKCRPNliFV 226
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 548961101 241 QwshISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14112  227 E---ATQEALRFATWALKKSPTRRMRTDEALEHRWL 259
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
10-281 1.11e-26

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: 110.34  E-value: 1.11e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpGLSTEdLKREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd14117    6 DDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKE-GVEHQ-LRREIEIQSHLRHPNILRLYNYFHDRKRIYL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQl 169
Cdd:cd14117   84 ILEYAPRGELYKELQKHGR----FDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYK---GELKIADFGWSVH- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 gESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF-YGTKERLFEGIIKGKYKMNPrqwsHISES 248
Cdd:cd14117  156 -APSLRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFeSASHTETYRRIVKVDLKFPP----FLSDG 230
                        250       260       270
                 ....*....|....*....|....*....|...
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNHPWLKERDR 281
Cdd:cd14117  231 SRDLISKLLRYHPSERLPLKGVMEHPWVKANSR 263
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
9-298 1.22e-26

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: 110.53  E-value: 1.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglsTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd06642    3 EELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDE----IEDIQQEITVLSQCDSPYITRYYGSYLKGTKLW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADlCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQ 168
Cdd:cd06642   79 IIMEYLGGGS-ALDLLKPGP----LEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGD---VKLADFGVAGQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKykmNPRQWSHISE 247
Cdd:cd06642  151 LTDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPmRVLFLIPKNS---PPTLEGQHSK 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 548961101 248 SAKDLVRRMLMLDPAERITVYEALNHPWLKerdRYAYKIH-LPETVEQLRKF 298
Cdd:cd06642  228 PFKEFVEACLNKDPRFRPTAKELLKHKFIT---RYTKKTSfLTELIDRYKRW 276
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
12-280 1.30e-26

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: 111.93  E-value: 1.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFS---VVRRCINRETGQQFAVKIVDVAKFTSSPGlSTEDLKREASIC-HMLKHPHIVELLETYSSDGML 87
Cdd:cd05614    2 FELLKVLGTGAYGkvfLVRKVSGHDANKLYAMKVLRKAALVQKAK-TVEHTRTERNVLeHVRQSPFLVTLHYAFQTDAKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAI 167
Cdd:cd05614   81 HLILDYVSGGELFTHLYQRDH----FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGH---VVLTDFGLSK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 Q-LGESGLVAGGRVGTPHFMAPEVVK-REPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGK-YKMNPRQWSH 244
Cdd:cd05614  154 EfLTEEKERTYSFCGTIEYMAPEIIRgKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRRiLKCDPPFPSF 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 548961101 245 ISESAKDLVRRMLMLDPAERI-----TVYEALNHPWLKERD 280
Cdd:cd05614  234 IGPVARDLLQKLLCKDPKKRLgagpqGAQEIKEHPFFKGLD 274
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
10-277 1.34e-26

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: 110.71  E-value: 1.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIV----DVAKFTSspglstedLKREASICHMLKHPHIVELLETYSSDG 85
Cdd:cd06622    1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIrlelDESKFNQ--------IIMELDILHKAVSPYIVDFYGAFFIEG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 MLYMVFEFMDGADLcfeivKRADAGFVYSEAVASHYMRQILEA----LRYCHDN-NIIHRDVKPHCVLLASKensAPVKL 160
Cdd:cd06622   73 AVYMCMEYMDAGSL-----DKLYAGGVATEGIPEDVLRRITYAvvkgLKFLKEEhNIIHRDVKPTNVLVNGN---GQVKL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 161 GGFGVAIQLGESglVAGGRVGTPHFMAPEVVKRE-PYGKPV-----DVWGCGVILFILLSGCLPF----YGTKERLFEGI 230
Cdd:cd06622  145 CDFGVSGNLVAS--LAKTNIGCQSYMAPERIKSGgPNQNPTytvqsDVWSLGLSILEMALGRYPYppetYANIFAQLSAI 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 548961101 231 IKGKykmNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd06622  223 VDGD---PPTLPSGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLV 266
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
12-265 1.41e-26

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: 112.43  E-value: 1.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKI----VDVAKFTSSPGLStedlkrEASICHMLKHPHIVELLETYSSDGML 87
Cdd:cd05594   27 FEYLKLLGKGTFGKVILVKEKATGRYYAMKIlkkeVIVAKDEVAHTLT------ENRVLQNSRHPFLTALKYSFQTHDRL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCH-DNNIIHRDVKPHCVLLaskENSAPVKLGGFGVA 166
Cdd:cd05594  101 CFVMEYANGGELFFHLSRER----VFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLML---DKDGHIKITDFGLC 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnPRQwshI 245
Cdd:cd05594  174 KEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDhEKLFELILMEEIRF-PRT---L 249
                        250       260
                 ....*....|....*....|
gi 548961101 246 SESAKDLVRRMLMLDPAERI 265
Cdd:cd05594  250 SPEAKSLLSGLLKKDPKQRL 269
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
10-292 1.45e-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: 113.18  E-value: 1.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd05622   73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLL--SKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYM 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLCfEIVKRADAgfvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQL 169
Cdd:cd05622  151 VMEYMPGGDLV-NLMSNYDV----PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADFGTCMKM 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLV-AGGRVGTPHFMAPEVVKREP----YGKPVDVWGCGVILFILLSGCLPFY-----GTkerlFEGIIKGKYKMNP 239
Cdd:cd05622  223 NKEGMVrCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYadslvGT----YSKIMNHKNSLTF 298
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 548961101 240 RQWSHISESAKDLVRRMLMlDPAERI---TVYEALNHPWLKErDRYAYKiHLPETV 292
Cdd:cd05622  299 PDDNDISKEAKNLICAFLT-DREVRLgrnGVEEIKRHLFFKN-DQWAWE-TLRDTV 351
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
18-276 1.48e-26

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: 110.88  E-value: 1.48e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd06657   28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRR-----ELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLCfEIVKRADAgfvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQLGESGLVAG 177
Cdd:cd06657  103 ALT-DIVTHTRM----NEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLT---HDGRVKLSDFGFCAQVSKEVPRRK 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 178 GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRML 257
Cdd:cd06657  175 SLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNLHKVSPSLKGFLDRLL 254
                        250
                 ....*....|....*....
gi 548961101 258 MLDPAERITVYEALNHPWL 276
Cdd:cd06657  255 VRDPAQRATAAELLKHPFL 273
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
18-274 1.53e-26

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: 109.40  E-value: 1.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTE--DLKREASICHMLK-HPHIVELLETYSSDGMLYMVFEFM 94
Cdd:cd13997    8 IGSGSFSEVFKVRSKVDGCLYAVK-----KSKKPFRGPKEraRALREVEAHAALGqHPNIVRYYSSWEEGGHLYIQMELC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  95 DGADLCfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESGL 174
Cdd:cd13997   83 ENGSLQ-DALEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGT---CKIGDFGLATRLETSGD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 175 VaggRVGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGC-LPFYGTkerLFEGIIKGKYKMNPRqwSHISESAKDL 252
Cdd:cd13997  159 V---EEGDSRYLAPELLNENYtHLPKADIFSLGVTVYEAATGEpLPRNGQ---QWQQLRQGKLPLPPG--LVLSQELTRL 230
                        250       260
                 ....*....|....*....|..
gi 548961101 253 VRRMLMLDPAERITVYEALNHP 274
Cdd:cd13997  231 LKVMLDPDPTRRPTADQLLAHD 252
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
17-277 1.60e-26

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: 109.79  E-value: 1.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFS---VVRRCINRETGQQFAVK------IVDVAKftsspglSTEDLKREASICHMLKH-PHIVELLETYSSDGM 86
Cdd:cd05583    1 VLGTGAYGkvfLVRKVGGHDAGKLYAMKvlkkatIVQKAK-------TAEHTMTERQVLEAVRQsPFLVTLHYAFQTDAK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 LYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVA 166
Cdd:cd05583   74 LHLILDYVNGGELFTHLYQREH----FTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGH---VVLTDFGLS 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 -IQLGESGLVAGGRVGTPHFMAPEVVKREPYG--KPVDVWGCGVILFILLSGCLPFYGTKERLFEG-IIKGKYKMNPRQW 242
Cdd:cd05583  147 kEFLPGENDRAYSFCGTIEYMAPEVVRGGSDGhdKAVDWWSLGVLTYELLTGASPFTVDGERNSQSeISKRILKSHPPIP 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 548961101 243 SHISESAKDLVRRMLMLDPAERI-----TVYEALNHPWLK 277
Cdd:cd05583  227 KTFSAEAKDFILKLLEKDPKKRLgagprGAHEIKEHPFFK 266
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
16-276 1.62e-26

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: 109.78  E-value: 1.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTED-----LKREASICHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd06629    7 ELIGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSDRADSRQKtvvdaLKSEIDTLKDLDHPNIVQYLGFEETEDYFSIF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADL--CFeivkRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQ 168
Cdd:cd06629   87 LEYVPGGSIgsCL----RKYGKF--EEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGI---CKISDFGISKK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 ----LGESGlvAGGRVGTPHFMAPEVV--KREPYGKPVDVWGCGVILFILLSGCLPFygTKERLFEGIIK-GKYKMNP-- 239
Cdd:cd06629  158 sddiYGNNG--ATSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPW--SDDEAIAAMFKlGNKRSAPpv 233
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 548961101 240 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd06629  234 PEDVNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
10-276 2.10e-26

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: 110.10  E-value: 2.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstEDLKREASICHMLK-HPHIVELLETY-----SS 83
Cdd:cd06638   18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDID------EEIEAEYNILKALSdHPNVVKFYGMYykkdvKN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLYMVFEFMDGA---DLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKL 160
Cdd:cd06638   92 GDQLWLVLELCNGGsvtDLVKGFLKRGER---MEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTE---GGVKL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 161 GGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKRE-----PYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFegiikg 233
Cdd:cd06638  166 VDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEqqldsTYDARCDVWSLGITAIELGDGDPPLADLHpmRALF------ 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 548961101 234 KYKMNP----RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd06638  240 KIPRNPpptlHQPELWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
12-277 2.14e-26

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: 110.58  E-value: 2.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsSPglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd06656   21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQ---QP--KKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCfEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGE 171
Cdd:cd06656   96 EYLAGGSLT-DVVTET----CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM---DGSVKLTDFGFCAQITP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEGIIKGKYKM-NPRQWSHIses 248
Cdd:cd06656  168 EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENplRALYLIATNGTPELqNPERLSAV--- 244
                        250       260
                 ....*....|....*....|....*....
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd06656  245 FRDFLNRCLEMDVDRRGSAKELLQHPFLK 273
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
16-265 2.34e-26

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: 110.83  E-value: 2.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDvaKFTSSPGLSTEDLKREASIC-HMLKHPHIVELLETYSSDGMLYMVFEFM 94
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQ--KKTILKKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVLDYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  95 DGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESGL 174
Cdd:cd05603   79 NGGELFFHLQRER----CFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGH---VVLTDFGLCKEGMEPEE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 175 VAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMNPRQwshiSESAKDLV 253
Cdd:cd05603  152 TTSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDvSQMYDNILHKPLHLPGGK----TVAACDLL 227
                        250
                 ....*....|..
gi 548961101 254 RRMLMLDPAERI 265
Cdd:cd05603  228 QGLLHKDQRRRL 239
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
12-273 2.81e-26

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: 108.98  E-value: 2.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftSSPGLSTE--DLKREASICHMLKHPHIVELLETY--SSDGML 87
Cdd:cd06652    4 WRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQFDP--ESPETSKEvnALECEIQLLKNLLHERIVQYYGCLrdPQERTL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGAdlcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLlasKENSAPVKLGGFGVAI 167
Cdd:cd06652   82 SIFMEYMPGG----SIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANIL---RDSVGNVKLGDFGASK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGESGLVAGGR---VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFygTKERLFEGIIK-GKYKMNPRQWS 243
Cdd:cd06652  155 RLQTICLSGTGMksvTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPW--AEFEAMAAIFKiATQPTNPQLPA 232
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 244 HISESAKDLVRRMLmLDPAERITVYEALNH 273
Cdd:cd06652  233 HVSDHCRDFLKRIF-VEAKLRPSADELLRH 261
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
10-278 3.49e-26

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 109.52  E-value: 3.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftSSPGLSTEDLkREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:PLN00009   2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQ--EDEGVPSTAI-REISLLKEMQHGNIVRLQDVVHSEKRLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDgadlcFEIVKRADAG--FVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLGGFGVAI 167
Cdd:PLN00009  79 VFEYLD-----LDLKKHMDSSpdFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNA--LKLADFGLAR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGESGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE--RLF----------EGIIKG- 233
Cdd:PLN00009 152 AFGIPVRTFTHEVVTLWYRAPEIlLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEidELFkifrilgtpnEETWPGv 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101 234 ----KYKMNPRQWS---------HISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:PLN00009 232 tslpDYKSAFPKWPpkdlatvvpTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKD 289
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
9-277 4.65e-26

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: 111.24  E-value: 4.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDvYELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd05621   52 ED-YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLL--SKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLY 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLCfEIVKRADAgfvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQ 168
Cdd:cd05621  129 MVMEYMPGGDLV-NLMSNYDV----PEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLL---DKYGHLKLADFGTCMK 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLV-AGGRVGTPHFMAPEVVKREP----YGKPVDVWGCGVILFILLSGCLPFY-----GTkerlFEGIIKGKYKMN 238
Cdd:cd05621  201 MDETGMVhCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYadslvGT----YSKIMDHKNSLN 276
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 548961101 239 PRQWSHISESAKDLVRRMLMlDPAERI---TVYEALNHPWLK 277
Cdd:cd05621  277 FPDDVEISKHAKNLICAFLT-DREVRLgrnGVEEIKQHPFFR 317
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
12-277 5.12e-26

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: 109.63  E-value: 5.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglSTEDLKR--------EASICHMLKHPHIVELLETYSS 83
Cdd:cd05574    3 FKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLD----------KEEMIKRnkvkrvltEREILATLDHPFLPTLYASFQT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLYMVFEFMDGADLcFEIVKRAdAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLL-------------- 149
Cdd:cd05574   73 STHLCFVMDYCPGGEL-FRLLQKQ-PGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLhesghimltdfdls 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 150 --ASKENSAPVKLGGFGVAIQLGESGL------VAGGR----VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCL 217
Cdd:cd05574  151 kqSSVTPPPVRKSLRKGSRRSSVKSIEketfvaEPSARsnsfVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTT 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548961101 218 PFYG-TKERLFEGIIKGK--YKMNPrqwsHISESAKDLVRRMLMLDPAERI----TVYEALNHPWLK 277
Cdd:cd05574  231 PFKGsNRDETFSNILKKEltFPESP----PVSSEAKDLIRKLLVKDPSKRLgskrGASEIKRHPFFR 293
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
16-276 5.92e-26

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: 109.67  E-value: 5.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDvAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 95
Cdd:cd05604    2 KVIGKGSFGKVLLAKRKRDGKYYAVKVLQ-KKVILNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV---AIQLGES 172
Cdd:cd05604   81 GGELFFHLQRER----SFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGH---IVLTDFGLckeGISNSDT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 173 GLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMNPrqwsHISESAKD 251
Cdd:cd05604  154 TTTF---CGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDtAEMYENILHKPLVLRP----GISLTAWS 226
                        250       260
                 ....*....|....*....|....*....
gi 548961101 252 LVRRMLMLDPAERITVYEAL----NHPWL 276
Cdd:cd05604  227 ILEELLEKDRQLRLGAKEDFleikNHPFF 255
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
13-264 6.29e-26

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 108.00  E-value: 6.29e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101    13 ELCEVIGKGPFSVVRRCI----NRETGQQFAVKIVDVakftSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLKE----DASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101    89 MVFEFMDGADLcFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQ 168
Cdd:smart00219  78 IVMEYMEGGDL-LSYLRKNRPKLSLSDLL--SFALQIARGMEYLESKNFIHRDLAARNCLVGENLV---VKISDFGLSRD 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   169 LGESGL--VAGGRVgtP-HFMAPEVVKREPYGKPVDVWGCGVILFILLSGC-LPFYG-TKERLFEGIIKGKYKMNPrqws 243
Cdd:smart00219 152 LYDDDYyrKRGGKL--PiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGeQPYPGmSNEEVLEYLKNGYRLPQP---- 225
                          250       260
                   ....*....|....*....|....
gi 548961101   244 hiSESAKDLVRRMLM---LDPAER 264
Cdd:smart00219 226 --PNCPPELYDLMLQcwaEDPEDR 247
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
12-265 6.33e-26

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: 108.93  E-value: 6.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFS---VVRRCINRETGQQFAVKIVDVAKFTSSpGLSTEDLKREASIC-HMLKHPHIVELLETYSSDGML 87
Cdd:cd05613    2 FELLKVLGTGAYGkvfLVRKVSGHDAGKLYAMKVLKKATIVQK-AKTAEHTRTERQVLeHIRQSPFLVTLHYAFQTDTKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAI 167
Cdd:cd05613   81 HLILDYINGGELFTHLSQRER----FTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDS---SGHVVLTDFGLSK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 Q-LGESGLVAGGRVGTPHFMAPEVVKREPYG--KPVDVWGCGVILFILLSGCLPFY--GTKERLFEgIIKGKYKMNPRQW 242
Cdd:cd05613  154 EfLLDENERAYSFCGTIEYMAPEIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTvdGEKNSQAE-ISRRILKSEPPYP 232
                        250       260
                 ....*....|....*....|...
gi 548961101 243 SHISESAKDLVRRMLMLDPAERI 265
Cdd:cd05613  233 QEMSALAKDIIQRLLMKDPKKRL 255
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
13-266 6.46e-26

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: 107.97  E-value: 6.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   13 ELCEVIGKGPFSVVRRCI----NRETGQQFAVKIVDvaKFTSSPglSTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGTlkgeGENTKIKVAVKTLK--EGADEE--EREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   89 MVFEFMDGADLcFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQ 168
Cdd:pfam07714  78 IVTEYMPGGDL-LDFLRKHKRKLTLKDLL--SMALQIAKGMEYLESKNFVHRDLAARNCLVSENLV---VKISDFGLSRD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  169 LGESG--LVAGGRVGTPHFMAPEVVKrepYGK---PVDVWGCGVILFILLSGC-LPFYG-TKERLFEGIIKGkYKMN-PR 240
Cdd:pfam07714 152 IYDDDyyRKRGGGKLPIKWMAPESLK---DGKftsKSDVWSFGVLLWEIFTLGeQPYPGmSNEEVLEFLEDG-YRLPqPE 227
                         250       260
                  ....*....|....*....|....*.
gi 548961101  241 QWshiSESAKDLVRRMLMLDPAERIT 266
Cdd:pfam07714 228 NC---PDELYDLMKQCWAYDPEDRPT 250
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
12-277 7.64e-26

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: 108.17  E-value: 7.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRE-TGQQFAVKIVDVAKFTSSPGLstedLKREASICHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd14201    8 YSRKDLVGHGAFAVVFKGRHRKkTDWEVAIKSINKKNLSKSQIL----LGKEIKILKELQHENIVALYDVQEMPNSVFLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLcfeiVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLL--ASKENSA----PVKLGGFG 164
Cdd:cd14201   84 MEYCNGGDL----ADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLsyASRKKSSvsgiRIKIADFG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 165 VAIQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSH 244
Cdd:cd14201  160 FARYL-QSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNKNLQPSIPRE 238
                        250       260       270
                 ....*....|....*....|....*....|...
gi 548961101 245 ISESAKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd14201  239 TSPYLADLLLGLLQRNQKDRMDFEAFFSHPFLE 271
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
16-273 9.35e-26

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: 107.41  E-value: 9.35e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKfTSSPGlSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 95
Cdd:cd14188    7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSR-VSKPH-QREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGESGLV 175
Cdd:cd14188   85 RRSMAHILKARK----VLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFI---NENMELKVGDFGLAARLEPLEHR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 176 AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMNprqwSHISESAKDLVR 254
Cdd:cd14188  158 RRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNlKETYRCIREARYSLP----SSLLAPAKHLIA 233
                        250
                 ....*....|....*....
gi 548961101 255 RMLMLDPAERITVYEALNH 273
Cdd:cd14188  234 SMLSKNPEDRPSLDEIIRH 252
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
12-276 9.41e-26

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: 108.79  E-value: 9.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLStedlkrEASICHMLKH------PHIVELLETYSSDG 85
Cdd:cd14210   15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKRFHQQALV------EVKILKHLNDndpddkHNIVRYKDSFIFRG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 MLYMVFEfMDGADLcFEIVKRAD-AGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSAPVKLGGFG 164
Cdd:cd14210   89 HLCIVFE-LLSINL-YELLKSNNfQGL--SLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILL-KQPSKSSIKVIDFG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 165 vaiqlgeSGLVAGGRVGT----PHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIK------- 232
Cdd:cd14210  164 -------SSCFEGEKVYTyiqsRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEeQLACIMEvlgvppk 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548961101 233 --------------GKYKMNPRQWSHI-----------------SESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14210  237 slidkasrrkkffdSNGKPRPTTNSKGkkrrpgskslaqvlkcdDPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
12-265 9.76e-26

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: 109.34  E-value: 9.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd05602    9 FHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQ-KKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 171
Cdd:cd05602   88 DYINGGELFYHLQRER----CFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGH---IVLTDFGLCKENIE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPrqwsHISESAK 250
Cdd:cd05602  161 PNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSrNTAEMYDNILNKPLQLKP----NITNSAR 236
                        250
                 ....*....|....*
gi 548961101 251 DLVRRMLMLDPAERI 265
Cdd:cd05602  237 HLLEGLLQKDRTKRL 251
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
12-278 9.92e-26

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: 108.61  E-value: 9.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftSSPGLSTEDLkREASICHMLKHPHIVELLETYSSDGM--LYM 89
Cdd:cd07845    9 FEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDN--ERDGIPISSL-REITLLLNLRHPNIVELKEVVVGKHLdsIFL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDgADLCfEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQL 169
Cdd:cd07845   86 VMEYCE-QDLA-SLLDNMPTPF--SESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDK---GCLKIADFGLARTY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAGGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGTKE----------------RLFEGIIK 232
Cdd:cd07845  159 GLPAKPMTPKVVTLWYRAPELLlGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEieqldliiqllgtpneSIWPGFSD 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101 233 ----GKYKMnPRQ--------WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd07845  239 lplvGKFTL-PKQpynnlkhkFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYFKE 295
PDZ_MPP3-MPP4-MPP7-like cd06799
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ...
482-563 1.05e-25

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: 101.17  E-value: 1.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 482 VRLVqfqKNtDEPMGITLKMNELNHCI-VARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFK 560
Cdd:cd06799    3 VRLV---KN-NEPLGATIKRDEKTGAIvVARIMRGGAADRSGLIHVGDELREVNGISVEGKDPEEVIQILANSQGPITFK 78

                 ...
gi 548961101 561 IVP 563
Cdd:cd06799   79 LIP 81
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
12-277 1.18e-25

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: 108.27  E-value: 1.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsSPglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd06654   22 YTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQ---QP--KKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVM 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCfEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGE 171
Cdd:cd06654   97 EYLAGGSLT-DVVTET----CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGM---DGSVKLTDFGFCAQITP 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEGIIKGKYKM-NPRQWSHIses 248
Cdd:cd06654  169 EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENplRALYLIATNGTPELqNPEKLSAI--- 245
                        250       260
                 ....*....|....*....|....*....
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd06654  246 FRDFLNRCLEMDVEKRGSAKELLQHQFLK 274
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
9-274 1.27e-25

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: 108.40  E-value: 1.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKI---VDVAKFtsspglstedlKREASICHMLK-HPHIVELL------ 78
Cdd:cd14132   17 QDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVlkpVKKKKI-----------KREIKILQNLRgGPNIVKLLdvvkdp 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  79 --ETYSsdgmlyMVFEFMDGADLcfeivKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSa 156
Cdd:cd14132   86 qsKTPS------LIFEYVNNTDF-----KTLYPTLTDYDIR--YYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRK- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 157 pVKLGGFGVA----------IqlgesglvaggRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFY----- 220
Cdd:cd14132  152 -LRLIDWGLAefyhpgqeynV-----------RVASRYYKGPELlVDYQYYDYSLDMWSLGCMLASMIFRKEPFFhghdn 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 221 -----------GTKErLFE-----GI--------IKGKYKMNPrqWSH---------ISESAKDLVRRMLMLDPAERITV 267
Cdd:cd14132  220 ydqlvkiakvlGTDD-LYAyldkyGIelpprlndILGRHSKKP--WERfvnsenqhlVTPEALDLLDKLLRYDHQERITA 296

                 ....*..
gi 548961101 268 YEALNHP 274
Cdd:cd14132  297 KEAMQHP 303
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
12-275 1.40e-25

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: 107.52  E-value: 1.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftSSPGLSTEDLkREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd07839    2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDD--DDEGVPSSAL-REICLLKELKHKNIVRLYDVLHSDKKLTLVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDgADLcfeiVKRADA--GFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQL 169
Cdd:cd07839   79 EYCD-QDL----KKYFDScnGDIDPEIVKS-FMFQLLKGLAFCHSHNVLHRDLKPQNLLI---NKNGELKLADFGLARAF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAGGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFY----------------GT-KERLFEGII 231
Cdd:cd07839  150 GIPVRCYSAEVVTLWYRPPDVLfGAKLYSTSIDMWSAGCIFAELANAGRPLFpgndvddqlkrifrllGTpTEESWPGVS 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 548961101 232 K-GKYKMNPRQ-----WSHI----SESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd07839  230 KlPDYKPYPMYpattsLVNVvpklNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
12-277 1.45e-25

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 111.50  E-value: 1.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkftsspGLSTEDLKR-EASICHMLKHPH--IVELLETYS-SD--- 84
Cdd:PTZ00283  34 YWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDME------GMSEADKNRaQAEVCCLLNCDFfsIVKCHEDFAkKDprn 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  85 ----GMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKL 160
Cdd:PTZ00283 108 penvLMIALVLDYANAGDLRQEIKSRAKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCS---NGLVKL 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 161 GGFGVAIQLGE--SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKM 237
Cdd:PTZ00283 185 GDFGFSKMYAAtvSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENmEEVMHKTLAGRYDP 264
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 548961101 238 NPrqwSHISESAKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:PTZ00283 265 LP---PSISPEMQEIVTALLSSDPKRRPSSSKLLNMPICK 301
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
10-280 1.69e-25

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: 108.59  E-value: 1.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPF---SVVRRcinRETGQQFAVKIVDvaKFtsspglstEDLKREASICH-----MLKH---PHIVELL 78
Cdd:cd05597    1 DDFEILKVIGRGAFgevAVVKL---KSTEKVYAMKILN--KW--------EMLKRAETACFreerdVLVNgdrRWITKLH 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  79 ETYSSDGMLYMVFEFMDGADLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPV 158
Cdd:cd05597   68 YAFQDENYLYLVMDYYCGGDLLTLLSKFEDR---LPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLL---DRNGHI 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 159 KLGGFGVAIQLGESGLVAGG-RVGTPHFMAPEVVK-----REPYGKPVDVWGCGVILFILLSGCLPFYGtkERLFE--GI 230
Cdd:cd05597  142 RLADFGSCLKLREDGTVQSSvAVGTPDYISPEILQamedgKGRYGPECDWWSLGVCMYEMLYGETPFYA--ESLVEtyGK 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 548961101 231 I---KGKYKMnPRQWSHISESAKDLVRRmLMLDPAERI---TVYEALNHPWLKERD 280
Cdd:cd05597  220 ImnhKEHFSF-PDDEDDVSEEAKDLIRR-LICSRERRLgqnGIDDFKKHPFFEGID 273
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
9-298 2.34e-25

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: 106.70  E-value: 2.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglsTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd06641    3 EELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDE----IEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGAdlcfEIVKRADAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQ 168
Cdd:cd06641   79 IIMEYLGGG----SALDLLEPGPLDETQIAT-ILREILKGLDYLHSEKKIHRDIKAANVLLSEH---GEVKLADFGVAGQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKgkyKMNPRQWS-HISE 247
Cdd:cd06641  151 LTDTQIKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIP---KNNPPTLEgNYSK 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 548961101 248 SAKDLVRRMLMLDPAERITVYEALNHPWLKerdRYAYKI-HLPETVEQLRKF 298
Cdd:cd06641  228 PLKEFVEACLNKEPSFRPTAKELLKHKFIL---RNAKKTsYLTELIDRYKRW 276
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
9-277 3.29e-25

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 110.49  E-value: 3.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGP----FSVVRrcinretGQQFAVKIVdvAKFTSspgLSTEdlkREA----SICHML---KHPHIVEL 77
Cdd:PTZ00267  66 EHMYVLTTLVGRNPttaaFVATR-------GSDPKEKVV--AKFVM---LNDE---RQAayarSELHCLaacDHFGIVKH 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  78 LETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAP 157
Cdd:PTZ00267 131 FDDFKSDDKLLLIMEYGSGGDLNKQIKQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMP---TGI 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 158 VKLGGFGVAIQLGESGL--VAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGK 234
Cdd:PTZ00267 208 IKLGDFGFSKQYSDSVSldVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQReIMQQVLYGK 287
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 548961101 235 YKMNPrqwSHISESAKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:PTZ00267 288 YDPFP---CPVSSGMKALLDPLLSKNPALRPTTQQLLHTEFLK 327
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
12-265 3.96e-25

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: 107.39  E-value: 3.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIV---DVAKFTSSPGLSTEdlKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd05589    1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALkkgDIIARDEVESLMCE--KRIFETVNSARHPFLVNLFACFQTPEHVC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLCFEIvkRADagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGvaiq 168
Cdd:cd05589   79 FVMEYAAGGDLMMHI--HED---VFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDT---EGYVKIADFG---- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAGGRV----GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnPRqws 243
Cdd:cd05589  147 LCKEGMGFGDRTstfcGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGdDEEEVFDSIVNDEVRY-PR--- 222
                        250       260
                 ....*....|....*....|..
gi 548961101 244 HISESAKDLVRRMLMLDPAERI 265
Cdd:cd05589  223 FLSTEAISIMRRLLRKNPERRL 244
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
12-280 5.26e-25

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: 107.01  E-value: 5.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvaKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd05601    3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLK--KSETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENLYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGE 171
Cdd:cd05601   81 EYHPGGDL-LSLLSRYDDIF--EESMARFYLAELVLAIHSLHSMGYVHRDIKPENILI---DRTGHIKLADFGSAAKLSS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLV-AGGRVGTPHFMAPEV------VKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWS 243
Cdd:cd05601  155 DKTVtSKMPVGTPDYIAPEVltsmngGSKGTYGVECDWWSLGIVAYEMLYGKTPFTEdTVIKTYSNIMNFKKFLKFPEDP 234
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 548961101 244 HISESAKDLVRRmLMLDPAERITvYEAL-NHPWLKERD 280
Cdd:cd05601  235 KVSESAVDLIKG-LLTDAKERLG-YEGLcCHPFFSGID 270
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
12-275 6.17e-25

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: 105.11  E-value: 6.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYS--SDGMLYM 89
Cdd:cd06653    4 WRLGKLLGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRdpEEKKLSI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGAdlcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLlasKENSAPVKLGGFGVA--I 167
Cdd:cd06653   84 FVEYMPGG----SVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDFGASkrI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 Q-LGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFygTKERLFEGIIK-GKYKMNPRQWSHI 245
Cdd:cd06653  157 QtICMSGTGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPW--AEYEAMAAIFKiATQPTKPQLPDGV 234
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 246 SESAKDLVRRmLMLDPAERITVYEALNHPW 275
Cdd:cd06653  235 SDACRDFLRQ-IFVEEKRRPTAEFLLRHPF 263
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
12-273 7.61e-25

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: 105.14  E-value: 7.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftSSPGLSteDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14046    8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRS--ESKNNS--RILREVMLLSRLNHQHVVRYYQAWIERANLYIQM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIvkraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQL-- 169
Cdd:cd14046   84 EYCEKSTLRDLI----DSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGN---VKIGDFGLATSNkl 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 ---------GESGLVAG-------GRVGTPHFMAPEVVKREP--YGKPVDVWGCGVILFILlsgCLPFYGTKERLFE-GI 230
Cdd:cd14046  157 nvelatqdiNKSTSAALgssgdltGNVGTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEM---CYPFSTGMERVQIlTA 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 548961101 231 IKGKYKMNPRQW--SHISESAKdLVRRMLMLDPAERITVYEALNH 273
Cdd:cd14046  234 LRSVSIEFPPDFddNKHSKQAK-LIRWLLNHDPAKRPSAQELLKS 277
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
17-265 7.99e-25

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: 106.32  E-value: 7.99e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKIV--DVAkftsspgLSTEDLKreasiCHML---------KHPHIVELLETYSSDG 85
Cdd:cd05587    3 VLGKGSFGKVMLAERKGTDELYAIKILkkDVI-------IQDDDVE-----CTMVekrvlalsgKPPFLTQLHSCFQTMD 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 MLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGV 165
Cdd:cd05587   71 RLYFVMEYVNGGDLMYHIQQVGK----FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML---DAEGHIKIADFGM 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 166 AIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIkgkyKMNPRQWSH 244
Cdd:cd05587  144 CKEGIFGGKTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEdELFQSIM----EHNVSYPKS 219
                        250       260
                 ....*....|....*....|.
gi 548961101 245 ISESAKDLVRRMLMLDPAERI 265
Cdd:cd05587  220 LSKEAVSICKGLLTKHPAKRL 240
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
12-275 1.19e-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: 104.66  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVK-----IVDVAKFTSSPGLSTedLKREASichmlkHPHIVELLETY--SSD 84
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKcmkkhFKSLEQVNNLREIQA--LRRLSP------HPNILRLIEVLfdRKT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  85 GMLYMVFEFMDGAdlCFEIVKradaGFVY--SEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnsapVKLGG 162
Cdd:cd07831   73 GRLALVFELMDMN--LYELIK----GRKRplPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDI----LKLAD 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 163 FG----VAIQLGESGLVAggrvgTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPFYGTKE------------- 224
Cdd:cd07831  143 FGscrgIYSKPPYTEYIS-----TRWYRAPECLLTDGyYGPKMDIWAVGCVFFEILSLFPLFPGTNEldqiakihdvlgt 217
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548961101 225 ------RLFEGIIKGKYKMNPRQWS-------HISESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd07831  218 pdaevlKKFRKSRHMNYNFPSKKGTglrkllpNASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
12-221 1.96e-24

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 108.73  E-value: 1.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRR--CI--NRETgqqfAVKIVD---------VAKFtsspglstedlKREA----SichmLKHPHI 74
Cdd:NF033483   9 YEIGERIGRGGMAEVYLakDTrlDRDV----AVKVLRpdlardpefVARF-----------RREAqsaaS----LSHPNI 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  75 VELLETYSSDGMLYMVFEFMDGADLcFEIVkRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeN 154
Cdd:NF033483  70 VSVYDVGEDGGIPYIVMEYVDGRTL-KDYI-REHGPLSPEEAV--EIMIQILSALEHAHRNGIVHRDIKPQNILIT---K 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101 155 SAPVKLGGFGVAIQLGESGLVAGGRV-GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 221
Cdd:NF033483 143 DGRVKVTDFGIARALSSTTMTQTNSVlGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDG 210
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
9-298 2.11e-24

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: 103.98  E-value: 2.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglsTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd06640    3 EELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDE----IEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADlCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQ 168
Cdd:cd06640   79 IIMEYLGGGS-ALDLLRAGP----FDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQ---GDVKLADFGVAGQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKykmNPRQWSHISE 247
Cdd:cd06640  151 LTDTQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPmRVLFLIPKNN---PPTLVGDFSK 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 548961101 248 SAKDLVRRMLMLDPAERITVYEALNHPWL-KERDRYAYkihLPETVEQLRKF 298
Cdd:cd06640  228 PFKEFIDACLNKDPSFRPTAKELLKHKFIvKNAKKTSY---LTELIDRFKRW 276
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
12-265 2.37e-24

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: 105.08  E-value: 2.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIV--DVAkftsspgLSTEDLKreasiCHML---------KHPHIVELLET 80
Cdd:cd05616    2 FNFLMVLGKGSFGKVMLAERKGTDELYAVKILkkDVV-------IQDDDVE-----CTMVekrvlalsgKPPFLTQLHSC 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  81 YSSDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKL 160
Cdd:cd05616   70 FQTMDRLYFVMEYVNGGDLMYHIQQVGR----FKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGH---IKI 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 161 GGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMnP 239
Cdd:cd05616  143 ADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEdELFQSIMEHNVAY-P 221
                        250       260
                 ....*....|....*....|....*.
gi 548961101 240 RQwshISESAKDLVRRMLMLDPAERI 265
Cdd:cd05616  222 KS---MSKEAVAICKGLMTKHPGKRL 244
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
10-275 2.89e-24

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: 104.15  E-value: 2.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkfTSSPGLSTEDLkREASICHMLKH-PHIVELL--ETYSSDG- 85
Cdd:cd07837    1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLE--MEEEGVPSTAL-REVSLLQMLSQsIYIVRLLdvEHVEENGk 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 -MLYMVFEFMDgADL--CFEIVKRADAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENS---APVK 159
Cdd:cd07837   78 pLLYLVFEYLD-TDLkkFIDSYGRGPHNPLPAKTIQS-FMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLlkiADLG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 160 LG-GFGVAIQLGESGLVaggrvgTPHFMAPEV-VKREPYGKPVDVWGCGVI---------LFI------LLSGCLPFYGT 222
Cdd:cd07837  156 LGrAFTIPIKSYTHEIV------TLWYRAPEVlLGSTHYSTPVDMWSVGCIfaemsrkqpLFPgdselqQLLHIFRLLGT 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548961101 223 -KERLFEGIIKGKYKMNPRQWS---------HISESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd07837  230 pNEEVWPGVSKLRDWHEYPQWKpqdlsravpDLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
18-276 3.41e-24

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: 104.76  E-value: 3.41e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVK--------IVDvAKFTSspglstedlkREASICHMLKHPHIVELLETYSSDGM--- 86
Cdd:cd07858   13 IGRGAYGIVCSAKNSETNEKVAIKkianafdnRID-AKRTL----------REIKLLRHLDHENVIAIKDIMPPPHReaf 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 --LYMVFEFMDgADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFG 164
Cdd:cd07858   82 ndVYIVYELMD-TDL-HQIIRSSQT---LSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNAN---CDLKICDFG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 165 VAIQLGESGLVAGGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGT----KERLFEGIIKG------ 233
Cdd:cd07858  154 LARTTSEKGDFMTEYVVTRWYRAPELLlNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKdyvhQLKLITELLGSpseedl 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548961101 234 ---------KYKMN----PRQ-----WSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd07858  234 gfirnekarRYIRSlpytPRQsfarlFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYL 294
gmk PRK00300
guanylate kinase; Provisional
736-901 4.29e-24

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 100.93  E-value: 4.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 736 LVLLGAHGVGrrhiKNTLIT---KHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGT 812
Cdd:PRK00300   8 IVLSGPSGAG----KSTLVKallERDPNLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYYGT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 813 KLETIRKIHEQGLIAILDVEPQ-ALKVLRTAEFAPFvVFIAAPTItpglneDESLQRLQK---ES-DVLQR--------- 878
Cdd:PRK00300  84 PRSPVEEALAAGKDVLLEIDWQgARQVKKKMPDAVS-IFILPPSL------EELERRLRGrgtDSeEVIARrlakareei 156
                        170       180
                 ....*....|....*....|...
gi 548961101 879 TYAHYFDLTIINNEIDETIRHLE 901
Cdd:PRK00300 157 AHASEYDYVIVNDDLDTALEELK 179
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
8-279 4.29e-24

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: 104.37  E-value: 4.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKivDVAKFTSSPGLSTEDLkREASICHMLKHPHIVELLETYSSDGML 87
Cdd:cd07855    3 VGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIK--KIPNAFDVVTTAKRTL-RELKILRHFKHDNIIAIRDILRPKVPY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 ------YMVFEFMDGaDLCFEIvkRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLG 161
Cdd:cd07855   80 adfkdvYVVLDLMES-DLHHII--HSDQPL--TLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNE---NCELKIG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 162 GFGVAIQLGESGL----VAGGRVGTPHFMAPEVVKREP-YGKPVDVWGCGVIL--------------------------- 209
Cdd:cd07855  152 DFGMARGLCTSPEehkyFMTEYVATRWYRAPELMLSLPeYTQAIDMWSVGCIFaemlgrrqlfpgknyvhqlqliltvlg 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 210 -----FILLSGClpfygtkERLfEGIIKGKYKMNPRQWSHI----SESAKDLVRRMLMLDPAERITVYEALNHPWLKER 279
Cdd:cd07855  232 tpsqaVINAIGA-------DRV-RRYIQNLPNKQPVPWETLypkaDQQALDLLSQMLRFDPSERITVAEALQHPFLAKY 302
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
7-276 4.52e-24

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: 104.18  E-value: 4.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   7 LFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIV-DVAKFTsspglstEDLKREASICHMLKH------PHIVELLE 79
Cdd:cd14134    9 LLTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIrNVEKYR-------EAAKIEIDVLETLAEkdpngkSHCVQLRD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  80 TYSSDGMLYMVFEFMdGADLcFEIVKRADAGFVYSEAVAsHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE------ 153
Cdd:cd14134   82 WFDYRGHMCIVFELL-GPSL-YDFLKKNNYGPFPLEHVQ-HIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDyvkvyn 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 154 ----------NSAPVKLGGFGVAIQLGE--SGLVAggrvgTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF-- 219
Cdd:cd14134  159 pkkkrqirvpKSTDIKLIDFGSATFDDEyhSSIVS-----TRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFqt 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 220 --------------------------YGTKERLF--------EGIIKGKY-KMNPRQWSHISESAK-------DLVRRML 257
Cdd:cd14134  234 hdnlehlammerilgplpkrmirrakKGAKYFYFyhgrldwpEGSSSGRSiKRVCKPLKRLMLLVDpehrllfDLIRKML 313
                        330
                 ....*....|....*....
gi 548961101 258 MLDPAERITVYEALNHPWL 276
Cdd:cd14134  314 EYDPSKRITAKEALKHPFF 332
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
16-277 6.27e-24

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: 103.49  E-value: 6.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIV--DVAkftsspgLSTEDLKreasiCHMLK---------HPHIVELLETYSSD 84
Cdd:cd05620    1 KVLGKGSFGKVLLAELKGKGEYFAVKALkkDVV-------LIDDDVE-----CTMVEkrvlalaweNPFLTHLYCTFQTK 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  85 GMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFG 164
Cdd:cd05620   69 EHLFFVMEFLNGGDLMFHIQDKGR----FDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVML---DRDGHIKIADFG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 165 VAIQ--LGESGlvAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGiIKGKYKMNPRq 241
Cdd:cd05620  142 MCKEnvFGDNR--ASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEdELFES-IRVDTPHYPR- 217
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 548961101 242 WshISESAKDLVRRMLMLDPAERITVYEALN-HPWLK 277
Cdd:cd05620  218 W--ITKESKDILEKLFERDPTRRLGVVGNIRgHPFFK 252
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
16-276 9.66e-24

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: 101.53  E-value: 9.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF--EF 93
Cdd:cd13983    7 EVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKA---ERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIFitEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  94 MDGADLcFEIVKRADagfVYSEAVASHYMRQILEALRYCH--DNNIIHRDVKphCVLLASKENSAPVKLGGFGVAIQLGE 171
Cdd:cd13983   84 MTSGTL-KQYLKRFK---RLKLKVIKSWCRQILEGLNYLHtrDPPIIHRDLK--CDNIFINGNTGEVKIGDLGLATLLRQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SglVAGGRVGTPHFMAPEVVKrEPYGKPVDVWGCGVILFILLSGCLPFYGTKE--RLFEGIIKGKykmNPRQWSHI-SES 248
Cdd:cd13983  158 S--FAKSVIGTPEFMAPEMYE-EHYDEKVDIYAFGMCLLEMATGEYPYSECTNaaQIYKKVTSGI---KPESLSKVkDPE 231
                        250       260
                 ....*....|....*....|....*...
gi 548961101 249 AKDLVrRMLMLDPAERITVYEALNHPWL 276
Cdd:cd13983  232 LKDFI-EKCLKPPDERPSARELLEHPFF 258
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
24-276 1.45e-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: 100.58  E-value: 1.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  24 SVVRRCINRETGQQFAVKIVDVAKFTSspglstedlKREASIChMLKHPHIVELLETYSSDGMLYMVFEfMDGADLCFEI 103
Cdd:cd13976    7 SSLYRCVDIHTGEELVCKVVPVPECHA---------VLRAYFR-LPSHPNISGVHEVIAGETKAYVFFE-RDHGDLHSYV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 104 VKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKpHCVLLASKENSAPVKLGGF-GVAIQLGESGLVAGgRVGT 182
Cdd:cd13976   76 RSRKR----LREPEAARLFRQIASAVAHCHRNGIVLRDLK-LRKFVFADEERTKLRLESLeDAVILEGEDDSLSD-KHGC 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 183 PHFMAPEVVK-REPY-GKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMnPrqwSHISESAKDLVRRMLML 259
Cdd:cd13976  150 PAYVSPEILNsGATYsGKAADVWSLGVILYTMLVGRYPFHDSEPaSLFAKIRRGQFAI-P---ETLSPRARCLIRSLLRR 225
                        250
                 ....*....|....*..
gi 548961101 260 DPAERITVYEALNHPWL 276
Cdd:cd13976  226 EPSERLTAEDILLHPWL 242
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
17-273 1.72e-23

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: 100.77  E-value: 1.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKIVD---VAKFTSSPGLSTE-DLKREasichmLKHPHIVELLETYSSDGMLYMVFE 92
Cdd:cd14189    8 LLGKGGFARCYEMTDLATNKTYAVKVIPhsrVAKPHQREKIVNEiELHRD------LHHKHVVKFSHHFEDAENIYIFLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  93 FMDGADLCfEIVKradAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGES 172
Cdd:cd14189   82 LCSRKSLA-HIWK---ARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFI---NENMELKVGDFGLAARLEPP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 173 GLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMNprqwSHISESAKD 251
Cdd:cd14189  155 EQRKKTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDlKETYRCIKQVKYTLP----ASLSLPARH 230
                        250       260
                 ....*....|....*....|..
gi 548961101 252 LVRRMLMLDPAERITVYEALNH 273
Cdd:cd14189  231 LLAGILKRNPGDRLTLDQILEH 252
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
6-280 2.04e-23

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: 102.31  E-value: 2.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   6 VLFEDvYELCEVIGKGPFSVVRRCINRETGQQFAVKIV--DVAkftsspgLSTEDLKreasiCHMLK---------HPHI 74
Cdd:cd05619    2 LTIED-FVLHKMLGKGSFGKVFLAELKGTNQFFAIKALkkDVV-------LMDDDVE-----CTMVEkrvlslaweHPFL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  75 VELLETYSSDGMLYMVFEFMDGADLCFEIvkraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskEN 154
Cdd:cd05619   69 THLFCTFQTKENLFFVMEYLNGGDLMFHI----QSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILL---DK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 155 SAPVKLGGFGVAIQ--LGESGlvAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT-KERLFEGiI 231
Cdd:cd05619  142 DGHIKIADFGMCKEnmLGDAK--TSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQdEEELFQS-I 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 548961101 232 KGKYKMNPRqWshISESAKDLVRRMLMLDPAERITVYEAL-NHPWLKERD 280
Cdd:cd05619  219 RMDNPFYPR-W--LEKEAKDILVKLFVREPERRLGVRGDIrQHPFFREIN 265
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
18-219 2.28e-23

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: 101.37  E-value: 2.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAkfTSSPGLSTEDLKREASICHMLKHPHIV------ELLETYSSDGMLYMVF 91
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQE--LSPSDKNRERWCLEVQIMKKLNHPNVVsardvpPELEKLSPNDLPLLAM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGE 171
Cdd:cd13989   79 EYCSGGDL-RKVLNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIYKLIDLGYAKELDQ 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 548961101 172 SGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF 219
Cdd:cd13989  158 GSLCTS-FVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
SH3_MPP7 cd12033
Src Homology 3 domain of Membrane Protein, Palmitoylated 7 (or MAGUK p55 subfamily member 7); ...
610-668 2.48e-23

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: 93.93  E-value: 2.48e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 610 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPS 668
Cdd:cd12033    1 FIKALFDYNPNEDKAIPCKEAGLSFKKGDILQIMSQDDATWWQAKHEGDANPRAGLIPS 59
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
12-275 2.49e-23

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: 101.98  E-value: 2.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVV--RRCINRETGQQFAVKivdvaKFTSSP----GLSTEDLkREASICHMLKHPHIVELLETY--SS 83
Cdd:cd07842    2 YEIEGCIGRGTYGRVykAKRKNGKDGKEYAIK-----KFKGDKeqytGISQSAC-REIALLRELKHENVVSLVEVFleHA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLYMVFEFMDgADLcFEIVK---RADAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASK-ENSAPVK 159
Cdd:cd07842   76 DKSVYLLFDYAE-HDL-WQIIKfhrQAKRVSIPPSMVKS-LLWQILNGIHYLHSNWVLHRDLKPANILVMGEgPERGVVK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 160 LGGFGVAiQLGESGLVA----GGRVGTPHFMAPEVV--KREpYGKPVDVWGCGVILFILLSGCLPFYGTK---------- 223
Cdd:cd07842  153 IGDLGLA-RLFNAPLKPladlDPVVVTIWYRAPELLlgARH-YTKAIDIWAIGCIFAELLTLEPIFKGREakikksnpfq 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 224 ----ERLFE-----------GIIK-------------GKY-KMNPRQWSHI----SESAKDLVRRMLMLDPAERITVYEA 270
Cdd:cd07842  231 rdqlERIFEvlgtptekdwpDIKKmpeydtlksdtkaSTYpNSLLAKWMHKhkkpDSQGFDLLRKLLEYDPTKRITAEEA 310

                 ....*
gi 548961101 271 LNHPW 275
Cdd:cd07842  311 LEHPY 315
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
7-257 2.59e-23

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: 103.56  E-value: 2.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   7 LFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglSTEDLKREASICHMLKHPHIVE--------LL 78
Cdd:cd05623   69 LHKEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILN----------KWEMLKRAETACFREERDVLVNgdsqwittLH 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  79 ETYSSDGMLYMVFEFMDGADLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPV 158
Cdd:cd05623  139 YAFQDDNNLYLVMDYYVGGDLLTLLSKFEDR---LPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILM---DMNGHI 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 159 KLGGFGVAIQLGESGLVAGG-RVGTPHFMAPEVVK-----REPYGKPVDVWGCGVILFILLSGCLPFYGtkERLFE---G 229
Cdd:cd05623  213 RLADFGSCLKLMEDGTVQSSvAVGTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGETPFYA--ESLVEtygK 290
                        250       260
                 ....*....|....*....|....*....
gi 548961101 230 IIKGKYKMN-PRQWSHISESAKDLVRRML 257
Cdd:cd05623  291 IMNHKERFQfPTQVTDVSENAKDLIRRLI 319
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
71-274 3.49e-23

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: 100.04  E-value: 3.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  71 HPHIVELLETYSSDGMLYMVFEfmdgadLC----FEIVKRADAG--FVYSEAVASHYMRQILEALRYCHDNNIIHRDVKP 144
Cdd:cd13982   54 HPNVIRYFCTEKDRQFLYIALE------LCaaslQDLVESPRESklFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKP 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 145 HCVLLA--SKENSAPVKLGGFGVAIQL--GESGLVA-GGRVGTPHFMAPEVVKREPYGKP---VDVWGCGVILFILLSGC 216
Cdd:cd13982  128 QNILIStpNAHGNVRAMISDFGLCKKLdvGRSSFSRrSGVAGTSGWIAPEMLSGSTKRRQtraVDIFSLGCVFYYVLSGG 207
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 217 L-PFYGTKERlfEG-IIKGKYKMNP--RQWSHISEsAKDLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd13982  208 ShPFGDKLER--EAnILKGKYSLDKllSLGEHGPE-AQDLIERMIDFDPEKRPSAEEVLNHP 266
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
16-266 4.70e-23

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: 99.54  E-value: 4.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCI---NRETGQQFAVKIVDvaKFTSSPGLstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFE 92
Cdd:cd00192    1 KKLGEGAFGEVYKGKlkgGDGKTVDVAVKTLK--EDASESER--KDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  93 FMDGADL-CFEIVKRADAGFVYSEAVAS----HYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVA- 166
Cdd:cd00192   77 YMEGGDLlDFLRKSRPVFPSPEPSTLSLkdllSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLV---VKISDFGLSr 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 -IQLGESGLVAGGRVgTP-HFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYG-TKERLFEGIIKGkYKMNprQW 242
Cdd:cd00192  154 dIYDDDYYRKKTGGK-LPiRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGlSNEEVLEYLRKG-YRLP--KP 229
                        250       260
                 ....*....|....*....|....
gi 548961101 243 SHISESAKDLVRRMLMLDPAERIT 266
Cdd:cd00192  230 ENCPDELYELMLSCWQLDPEDRPT 253
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
7-257 5.07e-23

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: 102.78  E-value: 5.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   7 LFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglSTEDLKREASICHMLKHPHIVE--------LL 78
Cdd:cd05624   69 LHRDDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILN----------KWEMLKRAETACFREERNVLVNgdcqwittLH 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  79 ETYSSDGMLYMVFEFMDGADLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPV 158
Cdd:cd05624  139 YAFQDENYLYLVMDYYVGGDLLTLLSKFEDK---LPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLL---DMNGHI 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 159 KLGGFGVAIQLGESGLVAGG-RVGTPHFMAPEVVKRE-----PYGKPVDVWGCGVILFILLSGCLPFYGtkERLFEgiIK 232
Cdd:cd05624  213 RLADFGSCLKMNDDGTVQSSvAVGTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFYA--ESLVE--TY 288
                        250       260       270
                 ....*....|....*....|....*....|..
gi 548961101 233 GKYkMN-------PRQWSHISESAKDLVRRML 257
Cdd:cd05624  289 GKI-MNheerfqfPSHVTDVSEEAKDLIQRLI 319
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
18-209 6.79e-23

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: 99.10  E-value: 6.79e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVdvaKFTSSPGlsteDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKEL---KRFDEQR----SFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLcFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAG 177
Cdd:cd14065   74 TL-EELLKSMDEQLPWSQRV--SLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVVADFGLAREMPDEKTKKP 150
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 548961101 178 GR------VGTPHFMAPEVVKREPYGKPVDVWGCGVIL 209
Cdd:cd14065  151 DRkkrltvVGSPYWMAPEMLRGESYDEKVDVFSFGIVL 188
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
12-277 9.09e-23

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: 98.77  E-value: 9.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVD---VAKFTSSPGLSTEDLKRE--ASICHMLKHPHIVELLETYSSDGM 86
Cdd:cd14101    2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISrnrVQQWSKLPGVNPVPNEVAllQSVGGGPGHRGVIRLLDWFEIPEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 LYMVFEFMDGADLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApvKLGGFGVA 166
Cdd:cd14101   82 FLLVLERPQHCQDLFDYITERGA---LDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRTGDI--KLIDFGSG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQLGESGLV--AGGRVGTPhfmaPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFygtkERlFEGIIKGKYKMNprqwS 243
Cdd:cd14101  157 ATLKDSMYTdfDGTRVYSP----PEWILYHQYhALPATVWSLGILLYDMVCGDIPF----ER-DTDILKAKPSFN----K 223
                        250       260       270
                 ....*....|....*....|....*....|....
gi 548961101 244 HISESAKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd14101  224 RVSNDCRSLIRSCLAYNPSDRPSLEQILLHPWMM 257
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
12-278 9.62e-23

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: 100.46  E-value: 9.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKivDVAKFtSSPGLSTEDLkREASICHMLKHPHIVELLE-----TYSSDGM 86
Cdd:cd07849    7 YQNLSYIGEGAYGMVCSAVHKPTGQKVAIK--KISPF-EHQTYCLRTL-REIKILLRFKHENIIGILDiqrppTFESFKD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 LYMVFEFMDgADLCfEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFG-- 164
Cdd:cd07849   83 VYIVQELME-TDLY-KLIKTQH----LSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNT---NCDLKICDFGla 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 165 -VAIQLGESGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSgCLPFYGTKERL---------------- 226
Cdd:cd07849  154 rIADPEHDHTGFLTEYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLS-NRPLFPGKDYLhqlnlilgilgtpsqe 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548961101 227 -FEGIIKGKYK-------MNPRQ-----WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd07849  233 dLNCIISLKARnyikslpFKPKVpwnklFPNADPKALDLLDKMLTFNPHKRITVEEALAHPYLEQ 297
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
48-274 2.43e-22

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: 97.43  E-value: 2.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  48 FTSSPGLSTEDLKREA--------SICHmLKHPHIVELLE------TYSSDGMLYMVFEFMDGADLcFEIVKRAdaGFVY 113
Cdd:cd14012   27 LTSQEYFKTSNGKKQIqllekeleSLKK-LRHPNLVSYLAfsierrGRSDGWKVYLLTEYAPGGSL-SELLDSV--GSVP 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 114 SEAVaSHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFG----VAIQLGESGLVAggrVGTPHFMAPE 189
Cdd:cd14012  103 LDTA-RRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTGIVKLTDYSlgktLLDMCSRGSLDE---FKQTYWLPPE 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 190 VVK-REPYGKPVDVWGCGVILFILLSGCLPF-YGTKERLFEGIIKgkykmnprqwshISESAKDLVRRMLMLDPAERITV 267
Cdd:cd14012  179 LAQgSKSPTRKTDVWDLGLLFLQMLFGLDVLeKYTSPNPVLVSLD------------LSASLQDFLSKCLSLDPKKRPTA 246

                 ....*..
gi 548961101 268 YEALNHP 274
Cdd:cd14012  247 LELLPHE 253
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
18-277 2.54e-22

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 99.06  E-value: 2.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFA---VKIVDVAKFTSSPGLSTED------LKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAikkVKIIEISNDVTKDRQLVGMcgihftTLRELKIMNEIKHENIMGLVDVYVEGDFIN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGaDLcfeiVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQ 168
Cdd:PTZ00024  97 LVMDIMAS-DL----KKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSK---GICKIADFGLARR 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAG--------------GRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFE 228
Cdd:PTZ00024 169 YGYPPYSDTlskdetmqrreemtSKVVTLWYRAPELLmGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEidqlgRIFE 248
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548961101 229 giIKGK------------------YKMNPRQWS----HISESAKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:PTZ00024 249 --LLGTpnednwpqakklplytefTPRKPKDLKtifpNASDDAIDLLQSLLKLNPLERISAKEALKHEYFK 317
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
26-276 2.83e-22

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: 97.03  E-value: 2.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  26 VRRCINRETGQQFAVKIVDVAKFTSSpglstedlkreASICHML-KHPHIVELLETYSSDGMLYMVFEFMDGADLCF-EI 103
Cdd:cd14022    9 VFRAVHLHSGEELVCKVFDIGCYQES-----------LAPCFCLpAHSNINQITEIILGETKAYVFFERSYGDMHSFvRT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 104 VKRadagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGFGVAIQLGESGLVAGGRVGTP 183
Cdd:cd14022   78 CKK------LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTR-VKLESLEDAYILRGHDDSLSDKHGCP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 184 HFMAPEVVKRE-PY-GKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnPRQwshISESAKDLVRRMLMLD 260
Cdd:cd14022  151 AYVSPEILNTSgSYsGKAADVWSLGVMLYTMLVGRYPFHDIEpSSLFSKIRRGQFNI-PET---LSPKAKCLIRSILRRE 226
                        250
                 ....*....|....*.
gi 548961101 261 PAERITVYEALNHPWL 276
Cdd:cd14022  227 PSERLTSQEILDHPWF 242
SH3_MPP2 cd12037
Src Homology 3 domain of Membrane Protein, Palmitoylated 2 (or MAGUK p55 subfamily member 2); ...
610-668 2.90e-22

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: 90.78  E-value: 2.90e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 610 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLenSKNGTAGLIPS 668
Cdd:cd12037    1 FVKCHFDYDPSSDSLIPCKEAGLKFRAGDLLQIVNQEDPNWWQACH--VEGGSAGLIPS 57
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
12-276 3.20e-22

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: 97.73  E-value: 3.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTedlKREASICHMLK---HPHIVELLETYSS----- 83
Cdd:cd07863    2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGLPLST---VREVALLKRLEafdHPNIVRLMDVCATsrtdr 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLYMVFEFMDgADLCFEIVKRADAGFVySEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGF 163
Cdd:cd07863   79 ETKVTLVFEHVD-QDLRTYLDKVPPPGLP-AETIKD-LMRQFLRGLDFLHANCIVHRDLKPENILVTSG---GQVKLADF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 164 GVAiQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFEGI-------- 230
Cdd:cd07863  153 GLA-RIYSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEadqlgKIFDLIglppeddw 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 548961101 231 ----IKGKYKMNPRQWS-------HISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd07863  232 prdvTLPRGAFSPRGPRpvqsvvpEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
17-280 3.30e-22

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: 98.41  E-value: 3.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLsTEDLKrEASICHMLKHPHIVELLETYSSDGMLYMVFEFMDG 96
Cdd:cd05585    1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEV-THTLA-ERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFING 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  97 ADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApvkLGGFGVA-IQLGESGlV 175
Cdd:cd05585   79 GELFHHLQREGR----FDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIA---LCDFGLCkLNMKDDD-K 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 176 AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMNprqwSHISESAKDLVR 254
Cdd:cd05585  151 TNTFCGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENtNEMYRKILQEPLRFP----DGFDRDAKDLLI 226
                        250       260
                 ....*....|....*....|....*....
gi 548961101 255 RMLMLDPAERITV---YEALNHPWLKERD 280
Cdd:cd05585  227 GLLNRDPTKRLGYngaQEIKNHPFFDQID 255
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
12-277 3.35e-22

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: 99.09  E-value: 3.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAV-KIVDVAKFTSSpglSTEDLkREASICHMLKHPHIVELLETyssdgML--- 87
Cdd:cd07859    2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIkKINDVFEHVSD---ATRIL-REIKLLRLLRHPDIVEIKHI-----MLpps 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 -------YMVFEFMDgADLcFEIVKRADagfvysEAVASHY---MRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAP 157
Cdd:cd07859   73 rrefkdiYVVFELME-SDL-HQVIKAND------DLTPEHHqffLYQLLRALKYIHTANVFHRDLKPKNILANA---DCK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 158 VKLGGFG---VAIQLGESGLVAGGRVGTPHFMAPEVVKR--EPYGKPVDVWGCGVILFILLSGCLPFYGT---------- 222
Cdd:cd07859  142 LKICDFGlarVAFNDTPTAIFWTDYVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKnvvhqldlit 221
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548961101 223 -----------------KERLFEGIIKGKykmNPRQWSH----ISESAKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd07859  222 dllgtpspetisrvrneKARRYLSSMRKK---QPVPFSQkfpnADPLALRLLERLLAFDPKDRPTAEEALADPYFK 294
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
12-219 5.48e-22

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: 96.81  E-value: 5.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCE-VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstedlkREASICHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd13991    7 WATHQlRIGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRA----------EELMACAGLTSPRVVPLYGAVREGPWVNIF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApvKLGGFGVAIQLG 170
Cdd:cd13991   77 MDLKEGGSLGQLIKEQG----CLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDA--FLCDFGHAECLD 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 548961101 171 ESG----LVAGGRV-GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF 219
Cdd:cd13991  151 PDGlgksLFTGDYIpGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
18-280 7.08e-22

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: 97.64  E-value: 7.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKH-PHIVELLETYSSDGMLYMVFEFMDG 96
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILVRTALDEsPFIVGLKFSFQTPTDLYLVTDYMSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  97 ADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApvkLGGFGVAIQLGESGLVA 176
Cdd:cd05586   81 GELFWHLQKEGR----FSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIA---LCDFGLSKADLTDNKTT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 177 GGRVGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnPRqwSHISESAKDLVR 254
Cdd:cd05586  154 NTFCGTTEYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPFYAEDtQQMYRNIAFGKVRF-PK--DVLSDEGRSFVK 230
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 255 RMLMLDPAERITVY----EALNHPWLKERD 280
Cdd:cd05586  231 GLLNRNPKHRLGAHddavELKEHPFFADID 260
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
12-276 1.25e-21

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 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: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 96.91  E-value: 1.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQ-FAVKIV---DVAKFTSspglstedlKREASICHMLKHP------HIVELLETY 81
Cdd:cd14135    2 YRVYGYLGKGVFSNVVRARDLARGNQeVAIKIIrnnELMHKAG---------LKELEILKKLNDAdpddkkHCIRLLRHF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  82 SSDGMLYMVFEFMDGaDLcFEIVKR--ADAGFVYSeAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVK 159
Cdd:cd14135   73 EHKNHLCLVFESLSM-NL-REVLKKygKNVGLNIK-AVRS-YAQQLFLALKHLKKCNILHADIKPDNILVNEKKNT--LK 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 160 LGGFGVAIQLGESGLvaggrvgTPH-----FMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT------------ 222
Cdd:cd14135  147 LCDFGSASDIGENEI-------TPYlvsrfYRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKtnnhmlklmmdl 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 223 --------------KERLFE--------------------------------GIIKGKYKMN---PRQWSHIsesaKDLV 253
Cdd:cd14135  220 kgkfpkkmlrkgqfKDQHFDenlnfiyrevdkvtkkevrrvmsdikptkdlkTLLIGKQRLPdedRKKLLQL----KDLL 295
                        330       340
                 ....*....|....*....|...
gi 548961101 254 RRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14135  296 DKCLMLDPEKRITPNEALQHPFI 318
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
12-265 1.30e-21

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: 97.80  E-value: 1.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEDLKREASICHMLK----HPHIVELLETYSSDGML 87
Cdd:cd05618   22 FDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDD-----EDIDWVQTEKHVFEqasnHPFLVGLHSCFQTESRL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAI 167
Cdd:cd05618   97 FFVIEYVNGGDLMFHMQRQRK----LPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGH---IKLTDYGMCK 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF----------YGTKERLFEGIIKGKYKM 237
Cdd:cd05618  170 EGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgssdnpdQNTEDYLFQVILEKQIRI 249
                        250       260
                 ....*....|....*....|....*...
gi 548961101 238 nPRQwshISESAKDLVRRMLMLDPAERI 265
Cdd:cd05618  250 -PRS---LSVKAASVLKSFLNKDPKERL 273
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
18-271 1.32e-21

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: 95.80  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCInRETGQQFAVKIVDVAKFTSSPglstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd14066    1 IGSGGFGTVYKGV-LENGTVVAVKRLNEMNCAASK----KEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLcFEIVKRADAGFVYS----EAVASHymrqILEALRYCH---DNNIIHRDVKPHCVLLasKENSAPvKLGGFGVA--IQ 168
Cdd:cd14066   76 SL-EDRLHCHKGSPPLPwpqrLKIAKG----IARGLEYLHeecPPPIIHGDIKSSNILL--DEDFEP-KLTDFGLArlIP 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYgtKERLFEGiikgkyKMNPRQW--SHIS 246
Cdd:cd14066  148 PSESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVD--ENRENAS------RKDLVEWveSKGK 219
                        250       260
                 ....*....|....*....|....*
gi 548961101 247 ESAKDLVRRMLMLDPAERITVYEAL 271
Cdd:cd14066  220 EELEDILDKRLVDDDGVEEEEVEAL 244
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
4-265 1.45e-21

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: 96.99  E-value: 1.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   4 DDVLFEDvYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREAsICHMLKHPHIVELLETYSS 83
Cdd:cd05615    5 DRVRLTD-FNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRV-LALQDKPPFLTQLHSCFQT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGF 163
Cdd:cd05615   83 VDRLYFVMEYVNGGDLMYHIQQVGK----FKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGH---IKIADF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 164 GVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIkgkyKMNPRQW 242
Cdd:cd05615  156 GMCKEHMVEGVTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEdELFQSIM----EHNVSYP 231
                        250       260
                 ....*....|....*....|...
gi 548961101 243 SHISESAKDLVRRMLMLDPAERI 265
Cdd:cd05615  232 KSLSKEAVSICKGLMTKHPAKRL 254
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
11-274 1.78e-21

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: 94.68  E-value: 1.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIvdvakfTSSPGLSTEDLKR---EASiCHML--KHPHIVELLETYSSDG 85
Cdd:cd14050    2 CFTILSKLGEGSFGEVFKVRSREDGKLYAVKR------SRSRFRGEKDRKRkleEVE-RHEKlgEHPNCVRFIKAWEEKG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 MLYMVFEFMDG--ADLCFEIVKradagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGF 163
Cdd:cd14050   75 ILYIQTELCDTslQQYCEETHS-------LPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLS---KDGVCKLGDF 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 164 GVAIQLGESGlVAGGRVGTPHFMAPEVVkREPYGKPVDVWGCGVIlfILLSGC---LPFYGTK-ERLFEGIIKgkykmnP 239
Cdd:cd14050  145 GLVVELDKED-IHDAQEGDPRYMAPELL-QGSFTKAADIFSLGIT--ILELACnleLPSGGDGwHQLRQGYLP------E 214
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 548961101 240 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd14050  215 EFTAGLSPELRSIIKLMMDPDPERRPTAEDLLALP 249
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
18-281 2.24e-21

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 96.82  E-value: 2.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVdvakFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:PLN00034  82 IGSGAGGTVYKVIHRPTGRLYALKVI----YGNHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGG 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLcfeivkraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESGLVAG 177
Cdd:PLN00034 158 SL--------EGTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKN---VKIADFGVSRILAQTMDPCN 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 178 GRVGTPHFMAPEVVKRE----PY-GKPVDVWGCGVILFILLSGCLPF----YGTKERLFEGIIkgkYKMNPRQWSHISES 248
Cdd:PLN00034 227 SSVGTIAYMSPERINTDlnhgAYdGYAGDIWSLGVSILEFYLGRFPFgvgrQGDWASLMCAIC---MSQPPEAPATASRE 303
                        250       260       270
                 ....*....|....*....|....*....|...
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNHPWLKERDR 281
Cdd:PLN00034 304 FRHFISCCLQREPAKRWSAMQLLQHPFILRAQP 336
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
16-276 2.57e-21

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: 95.03  E-value: 2.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTedlkREASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 95
Cdd:cd07870    6 EKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTAI----REASLLKGLKHANIVLLHDIIHTKETLTFVFEYMH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 gADLCFEIVKRAdaGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQLGESGLV 175
Cdd:cd07870   82 -TDLAQYMIQHP--GGLHPYNVRL-FMFQLLRGLAYIHGQHILHRDLKPQNLLIS---YLGELKLADFGLARAKSIPSQT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 176 AGGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGTK-----------------ERLFEGIIK-GKYK 236
Cdd:cd07870  155 YSSEVVTLWYRPPDVLlGATDYSSALDIWGAGCIFIEMLQGQPAFPGVSdvfeqlekiwtvlgvptEDTWPGVSKlPNYK 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 548961101 237 ------MNPRQ----WSHISE--SAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd07870  235 pewflpCKPQQlrvvWKRLSRppKAEDLASQMLMMFPKDRISAQDALLHPYF 286
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
12-273 2.84e-21

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: 94.94  E-value: 2.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkftsSPGLSTEDLKREASICHMLKHPHIVELLETYSS-------- 83
Cdd:cd14048    8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLP----NNELAREKVLREVRALAKLDHPGIVRYFNAWLErppegwqe 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 ---DGMLYMVFEfmdgadLCF-EIVKRADAGFVYSEAVASHYM----RQILEALRYCHDNNIIHRDVKPHCVLLASKENs 155
Cdd:cd14048   84 kmdEVYLYIQMQ------LCRkENLKDWMNRRCTMESRELFVClnifKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDV- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 156 apVKLGGFGVA------------IQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLsgcLPFYGTK 223
Cdd:cd14048  157 --VKVGDFGLVtamdqgepeqtvLTPMPAYAKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI---YSFSTQM 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 548961101 224 ERL--FEGIIKGKYkmnPRQWSHISESAKDLVRRMLMLDPAERITVYEALNH 273
Cdd:cd14048  232 ERIrtLTDVRKLKF---PALFTNKYPEERDMVQQMLSPSPSERPEAHEVIEH 280
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
12-265 3.44e-21

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: 96.24  E-value: 3.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEDLKREASICHMLK----HPHIVELLETYSSDGML 87
Cdd:cd05617   17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDD-----EDIDWVQTEKHVFEqassNPFLVGLHSCFQTTSRL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAI 167
Cdd:cd05617   92 FLVIEYVNGGDLMFHMQRQRK----LPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLL---DADGHIKLTDYGMCK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF--------YGTKERLFEGIIKGKYKMnP 239
Cdd:cd05617  165 EGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiitdnpdMNTEDYLFQVILEKPIRI-P 243
                        250       260
                 ....*....|....*....|....*.
gi 548961101 240 RqwsHISESAKDLVRRMLMLDPAERI 265
Cdd:cd05617  244 R---FLSVKASHVLKGFLNKDPKERL 266
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
10-290 3.72e-21

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: 95.85  E-value: 3.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIV---DVAKFTSSPGLSTE-DLKREASichmlkHPHIVELLETYSSDG 85
Cdd:cd05598    1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLrkkDVLKRNQVAHVKAErDILAEAD------NEWVVKLYYSFQDKE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 MLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGV 165
Cdd:cd05598   75 NLYFVMDYIPGGDLMSLLIKKG----IFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILI---DRDGHIKLTDFGL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 166 AiqlgeSGL---------VAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-----TKERlfegII 231
Cdd:cd05598  148 C-----TGFrwthdskyyLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAqtpaeTQLK----VI 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548961101 232 KGKYKMNPRQWSHISESAKDLVRRmLMLDPAERI---TVYEALNHPWLK----ERDRYAYKIHLPE 290
Cdd:cd05598  219 NWRTTLKIPHEANLSPEAKDLILR-LCCDAEDRLgrnGADEIKAHPFFAgidwEKLRKQKAPYIPT 283
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
18-264 3.95e-21

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: 94.71  E-value: 3.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVakFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd08229   32 IGRGQFSEVYRATCLLDGVPVALKKVQI--FDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGESGLVAG 177
Cdd:cd08229  110 DLSRMIKHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITA---TGVVKLGDLGLGRFFSSKTTAAH 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 178 GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIK-GKYKMNPRQWSHISESAKDLVRRM 256
Cdd:cd08229  187 SLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKiEQCDYPPLPSDHYSEELRQLVNMC 266

                 ....*...
gi 548961101 257 LMLDPAER 264
Cdd:cd08229  267 INPDPEKR 274
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
16-280 4.59e-21

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: 95.25  E-value: 4.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIvdvakftsspglstedLKREASI------CHML---------KHPHIVELLET 80
Cdd:cd05591    1 KVLGKGSFGKVMLAERKGTDEVYAIKV----------------LKKDVILqdddvdCTMTekrilalaaKHPFLTALHSC 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  81 YSSDGMLYMVFEFMDGADLCFEIvKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKL 160
Cdd:cd05591   65 FQTKDRLFFVMEYVNGGDLMFQI-QRARK---FDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGH---CKL 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 161 GGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGK--YKM 237
Cdd:cd05591  138 ADFGMCKEGILNGKTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEdDLFESILHDDvlYPV 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 548961101 238 nprqWshISESAKDLVRRMLMLDPAERITVYEA-------LNHPWLKERD 280
Cdd:cd05591  218 ----W--LSKEAVSILKAFMTKNPAKRLGCVASqggedaiRQHPFFREID 261
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
11-297 5.20e-21

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: 94.40  E-value: 5.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkftsspGLSTEDLKREASIchMLKHPHIVELLETYSS------- 83
Cdd:cd06637    7 IFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVT------GDEEEEIKQEINM--LKKYSHHRNIATYYGAfikknpp 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 --DGMLYMVFEFMdGADLCFEIVKRADAGFVYSEAVAsHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLG 161
Cdd:cd06637   79 gmDDQLWLVMEFC-GAGSVTDLIKNTKGNTLKEEWIA-YICREILRGLSHLHQHKVIHRDIKGQNVLLTE---NAEVKLV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 162 GFGVAIQLGESGLVAGGRVGTPHFMAPEVVKRE-----PYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEGIIKGK 234
Cdd:cd06637  154 DFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDenpdaTYDFKSDLWSLGITAIEMAEGAPPLCDMHpmRALFLIPRNPA 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548961101 235 YKMNPRQWSHISESakdLVRRMLMLDPAERITVYEALNHPWLKER-DRYAYKIHLPETVEQLRK 297
Cdd:cd06637  234 PRLKSKKWSKKFQS---FIESCLVKNHSQRPSTEQLMKHPFIRDQpNERQVRIQLKDHIDRTKK 294
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
12-274 5.90e-21

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: 94.03  E-value: 5.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINR-ETGQQFAVKivdVAKFTSSPGLSTEDLKREASICHMLK---HPHIVELLETYSSDGML 87
Cdd:cd14052    2 FANVELIGSGEFSQVYKVSERvPTGKVYAVK---KLKPNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRADAGfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAI 167
Cdd:cd14052   79 YIQTELCENGSLDVFLSELGLLG-RLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGT---LKIGDFGMAT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLG-ESGL-VAGGRVgtphFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYGTK------------ERLFEGIIK 232
Cdd:cd14052  155 VWPlIRGIeREGDRE----YIAPEILSEHMYDKPADIFSLGLILLeAAANVVLPDNGDAwqklrsgdlsdaPRLSSTDLH 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 548961101 233 G--KYKMNPRQW----SHISESAKDLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd14052  231 SasSPSSNPPPDppnmPILSGSLDRVVRWMLSPEPDRRPTADDVLATP 278
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
33-296 8.91e-21

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 98.76  E-value: 8.91e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101    33 ETGQQFAVKIV---------DVAKFtsspglstedlKREASICHMLKHPHIVELLET-YSSDGMLYMVFEFMDGADLcfe 102
Cdd:TIGR03903    1 MTGHEVAIKLLrtdapeeehQRARF-----------RRETALCARLYHPNIVALLDSgEAPPGLLFAVFEYVPGRTL--- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   103 iVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGR--- 179
Cdd:TIGR03903   67 -REVLAADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIGTLLPGVRDADVATltr 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   180 ----VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG--TKERLFEGIIKGKYKMNPRQWSHiseSAKDLV 253
Cdd:TIGR03903  146 ttevLGTPTYCAPEQLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGasVAEILYQQLSPVDVSLPPWIAGH---PLGQVL 222
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 548961101   254 RRMLMLDPAERitvyeALNHPWLKERDRyayKIHLPETVEQLR 296
Cdd:TIGR03903  223 RKALNKDPRQR-----AASAPALAERFR---ALELCALVGILR 257
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
8-264 9.60e-21

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: 92.94  E-value: 9.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspgLSTEDLKREASICHMLKHPHIVELLETYS-SDGM 86
Cdd:cd14047    4 FRQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVK---------LNNEKAEREVKALAKLDHPNIVRYNGCWDgFDYD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 ---------------LYMVFEFMDGADLCFEIVKRadaGFVYSEAVASHYM-RQILEALRYCHDNNIIHRDVKPHCVLLA 150
Cdd:cd14047   75 petsssnssrsktkcLFIQMEFCEKGTLESWIEKR---NGEKLDKVLALEIfEQITKGVEYIHSKKLIHRDLKPSNIFLV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 151 skeNSAPVKLGGFGVAIQLGESGLVAGGRvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKErLFEGI 230
Cdd:cd14047  152 ---DTGKVKIGDFGLVTSLKNDGKRTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEKSK-FWTDL 226
                        250       260       270
                 ....*....|....*....|....*....|....
gi 548961101 231 IKGKYKMNPRQWSHISESakdLVRRMLMLDPAER 264
Cdd:cd14047  227 RNGILPDIFDKRYKIEKT---IIKKMLSKKPEDR 257
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
11-276 1.01e-20

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: 93.53  E-value: 1.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsspglsTEDLKRE--ASICHMLKHPHIVELLETYSS----- 83
Cdd:cd06636   17 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDV----------TEDEEEEikLEINMLKKYSHHRNIATYYGAfikks 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 ----DGMLYMVFEFMdGADLCFEIVKRADaGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskENsAPVK 159
Cdd:cd06636   87 ppghDDQLWLVMEFC-GAGSVTDLVKNTK-GNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT--EN-AEVK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 160 LGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKRE-----PYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEGIIK 232
Cdd:cd06636  162 LVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPLCDMHpmRALFLIPRN 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 548961101 233 GKYKMNPRQWshiSESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd06636  242 PPPKLKSKKW---SKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
14-221 1.04e-20

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: 93.18  E-value: 1.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  14 LCEVIGKGPFSVVRRCInrETGQQFAVKivdVAKFTSSPGLST--EDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14145   10 LEEIIGIGGFGKVYRAI--WIGDEVAVK---AARHDPDEDISQtiENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcfeivKRADAGFVYSEAVASHYMRQILEALRYCHDNNI---IHRDVKPHCVLLASK-EN----SAPVKLGGF 163
Cdd:cd14145   85 EFARGGPL-----NRVLSGKRIPPDILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILILEKvENgdlsNKILKITDF 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101 164 GVAIQLGESGLVAGGrvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 221
Cdd:cd14145  160 GLAREWHRTTKMSAA--GTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRG 215
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
17-221 1.10e-20

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: 92.46  E-value: 1.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRetGQQFAVKI--VDVAKftsSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFM 94
Cdd:cd14061    1 VIGVGGFGKVYRGIWR--GEEVAVKAarQDPDE---DISVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  95 DGADLcfeivKRADAGFVYSEAVASHYMRQILEALRYCHDNN---IIHRDVKPHCVLLASKENSAPV-----KLGGFGVA 166
Cdd:cd14061   76 RGGAL-----NRVLAGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAIENEDLenktlKITDFGLA 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 548961101 167 IQLGESGLVAGGrvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 221
Cdd:cd14061  151 REWHKTTRMSAA--GTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKG 203
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
7-277 1.73e-20

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: 93.92  E-value: 1.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   7 LFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAK-FTSSPGLSTEDLKReasichMLKHP-----HIVELLET 80
Cdd:cd14226   10 KWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKaFLNQAQIEVRLLEL------MNKHDtenkyYIVRLKRH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  81 YSSDGMLYMVFEFMDgADLcFEIVKRADAGFVySEAVASHYMRQILEALRYCH--DNNIIHRDVKPHCVLLASKENSApV 158
Cdd:cd14226   84 FMFRNHLCLVFELLS-YNL-YDLLRNTNFRGV-SLNLTRKFAQQLCTALLFLStpELSIIHCDLKPENILLCNPKRSA-I 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 159 KLGGFGVAIQLGEsglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-------------- 224
Cdd:cd14226  160 KIIDFGSSCQLGQ---RIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEvdqmnkivevlgmp 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 225 ------------RLFEGIIKGKY-------KMNPRQWSHISESA---------------------------KDLVRRMLM 258
Cdd:cd14226  237 pvhmldqapkarKFFEKLPDGTYylkktkdGKKYKPPGSRKLHEilgvetggpggrragepghtvedylkfKDLILRMLD 316
                        330
                 ....*....|....*....
gi 548961101 259 LDPAERITVYEALNHPWLK 277
Cdd:cd14226  317 YDPKTRITPAEALQHSFFK 335
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
18-274 1.90e-20

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: 93.79  E-value: 1.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd05610   12 ISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKN--MVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DlcfeiVKRADAGFVY-SEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVA-IQLGE---- 171
Cdd:cd05610   90 D-----VKSLLHIYGYfDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLIS---NEGHIKLTDFGLSkVTLNRelnm 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 ---------------------------SGL--------------------VAGGRV-GTPHFMAPEVVKREPYGKPVDVW 203
Cdd:cd05610  162 mdilttpsmakpkndysrtpgqvlsliSSLgfntptpyrtpksvrrgaarVEGERIlGTPDYLAPELLLGKPHGPAVDWW 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 204 GCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd05610  242 ALGVCLFEFLTGIPPFNDeTPQQVFQNILNRDIPW-PEGEEELSVNAQNAIEILLTMDPTKRAGLKELKQHP 312
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
17-274 2.21e-20

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: 92.29  E-value: 2.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCinRETGQQFAVKIVDVAKFTSSPGLSTE----------------DLKREASICHMLKHPHIVELLET 80
Cdd:cd14000    1 LLGDGGFGSVYRA--SYKGEPVAVKIFNKHTSSNFANVPADtmlrhlratdamknfrLLRQELTVLSHLHHPSIVYLLGI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  81 YSSDGMLYMVFEFMDGADLCFEIVKRADA--GFVYSEAVASHymrqILEALRYCHDNNIIHRDVKPHCVLLAS--KENSA 156
Cdd:cd14000   79 GIHPLMLVLELAPLGSLDHLLQQDSRSFAslGRTLQQRIALQ----VADGLRYLHSAMIIYRDLKSHNVLVWTlyPNSAI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 157 PVKLGGFGVAIQLGESGlvAGGRVGTPHFMAPEVVKRE-PYGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFEGI 230
Cdd:cd14000  155 IIKIADYGISRQCCRMG--AKGSEGTPGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSGGAPMVGHLKfpnefDIHGGL 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 548961101 231 IKGKYKMNPRQWSHIsesaKDLVRRMLMLDPAER---ITVYEALNHP 274
Cdd:cd14000  233 RPPLKQYECAPWPEV----EVLMKKCWKENPQQRptaVTVVSILNSP 275
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
12-278 2.30e-20

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: 93.24  E-value: 2.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLE----TYSSDGML 87
Cdd:cd07857    2 YELIKELGQGAYGIVCSARNAETSEEETVAIKKITNVFSKKILAKRALRELKLLRHFRGHKNITCLYDmdivFPGNFNEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDgADLCfEIVKradAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAI 167
Cdd:cd07857   82 YLYEELME-ADLH-QIIR---SGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNA---DCELKICDFGLAR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGES-GLVAG---GRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGcLPFYGTK---ERLFEgIIK------- 232
Cdd:cd07857  154 GFSENpGENAGfmtEYVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLGR-KPVFKGKdyvDQLNQ-ILQvlgtpde 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548961101 233 ------------------GKYKMNPRQWSHISES--AKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd07857  232 etlsrigspkaqnyirslPNIPKKPFESIFPNANplALDLLEKLLAFDPTKRISVEEALEHPYLAI 297
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
8-277 2.31e-20

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 91.84  E-value: 2.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCEVIGK-----GPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstedlkrEASICHMLK-HPHIVELLETY 81
Cdd:PHA03390   9 LVQFLKNCEIVKKlklidGKFGKVSVLKHKPTQKLFVQKIIKAKNFNAI----------EPMVHQLMKdNPNFIKLYYSV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  82 SSDGMLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapvklg 161
Cdd:PHA03390  79 TTLKGHVLIMDYIKDGDL-FDLLKKEGK---LSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDR------ 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 162 gfgvaIQLGESGLVAggRVGTPH-------FMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEgiIKgk 234
Cdd:PHA03390 149 -----IYLCDYGLCK--IIGTPScydgtldYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEELD--LE-- 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 548961101 235 yKMNPRQW------SHISESAKDLVRRMLMLDPAERITVYEA-LNHPWLK 277
Cdd:PHA03390 218 -SLLKRQQkklpfiKNVSKNANDFVQSMLKYNINYRLTNYNEiIKHPFLK 266
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
18-219 2.72e-20

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: 92.33  E-value: 2.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKivdvakfTSSPGLSTEDLKR---EASICHMLKHPHIV------ELLETYSSDGMLY 88
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIK-------QCRQELSPKNRERwclEIQIMKRLNHPNVVaardvpEGLQKLAPNDLPL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLCFEIVKRADAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQ 168
Cdd:cd14038   75 LAMEYCQGGDLRKYLNQFENCCGLREGAILT-LLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLIHKIIDLGYAKE 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 548961101 169 LGESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF 219
Cdd:cd14038  154 LDQGSLCT-SFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
67-276 2.95e-20

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: 90.88  E-value: 2.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  67 HMLKHPHIVELLETYSSDGMLYMVFEfMDGADLCFEIVKRADAGfvysEAVASHYMRQILEALRYCHDNNIIHRDVKPHC 146
Cdd:cd14023   40 QLPSHRNITGIVEVILGDTKAYVFFE-KDFGDMHSYVRSCKRLR----EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRK 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 147 VLLASKENSApVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKRE-PY-GKPVDVWGCGVILFILLSGCLPFYGTK- 223
Cdd:cd14023  115 FVFSDEERTQ-LRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILNTTgTYsGKSADVWSLGVMLYTLLVGRYPFHDSDp 193
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 548961101 224 ERLFEGIIKGKYKMNprqwSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14023  194 SALFSKIRRGQFCIP----DHVSPKARCLIRSLLRREPSERLTAPEILLHPWF 242
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
12-276 3.40e-20

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: 92.06  E-value: 3.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDV-----AKFTSSpglstedlkREASICHMLKHPHIVELLETYSSDGM 86
Cdd:cd07844    2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLeheegAPFTAI---------REASLLKDLKHANIVTLHDIIHTKKT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 LYMVFEFMDgADLCFEIvkrADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVA 166
Cdd:cd07844   73 LTLVFEYLD-TDLKQYM---DDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISER---GELKLADFGLA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 iqlgesglvAGGRVGTpHFMAPEVVK---REP--------YGKPVDVWGCGVILFILLSGCLPFYGTK------ERLFE- 228
Cdd:cd07844  146 ---------RAKSVPS-KTYSNEVVTlwyRPPdvllgsteYSTSLDMWGVGCIFYEMATGRPLFPGSTdvedqlHKIFRv 215
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548961101 229 ----------GIIK---------GKYKMNP--RQWSHIS--ESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd07844  216 lgtpteetwpGVSSnpefkpysfPFYPPRPliNHAPRLDriPHGEELALKFLQYEPKKRISAAEAMKHPYF 286
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
28-276 3.61e-20

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: 90.71  E-value: 3.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  28 RCINRETGQQFAVKIVDVAKFTSSPGLSTEdlkreasichMLKHPHIVELLETYSSDGMLYMVFEFMDGaDLCFEIVKRA 107
Cdd:cd14024   11 RAEHYQTEKEYTCKVLSLRSYQECLAPYDR----------LGPHEGVCSVLEVVIGQDRAYAFFSRHYG-DMHSHVRRRR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 108 DagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapvKLggfgVAIQLGESGLVAGG------RVG 181
Cdd:cd14024   80 R----LSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRT---KL----VLVNLEDSCPLNGDddsltdKHG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 182 TPHFMAPEVV--KREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNprqwSHISESAKDLVRRMLM 258
Cdd:cd14024  149 CPAYVGPEILssRRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAaLFAKIRRGAFSLP----AWLSPGARCLVSCMLR 224
                        250
                 ....*....|....*...
gi 548961101 259 LDPAERITVYEALNHPWL 276
Cdd:cd14024  225 RSPAERLKASEILLHPWL 242
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
12-276 4.28e-20

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: 92.84  E-value: 4.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIV-DVAKFTSSPGLSTEDL----KREASICHmlkhpHIVELLETYSSDGM 86
Cdd:cd14225   45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIrNKKRFHHQALVEVKILdalrRKDRDNSH-----NVIHMKEYFYFRNH 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 LYMVFEFMdGADLcFEIVKRAD-AGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSAPVKLGGFGv 165
Cdd:cd14225  120 LCITFELL-GMNL-YELIKKNNfQGF--SLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILL-RQRGQSSIKVIDFG- 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 166 aiqlgeSGLVAGGRVGT----PHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE----------------- 224
Cdd:cd14225  194 ------SSCYEHQRVYTyiqsRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEveqlacimevlglpppe 267
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548961101 225 --------RLF-------EGII--KG-KYKMNPRQWSHISESAK----DLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14225  268 lienaqrrRLFfdskgnpRCITnsKGkKRRPNSKDLASALKTSDplflDFIRRCLEWDPSKRMTPDEALQHEWI 341
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
18-281 4.84e-20

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: 91.35  E-value: 4.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAkftSSPGLSTEDLkREASICHMLKHPHIVELLETYSSD-GMLYMVFEFMDG 96
Cdd:cd06620   13 LGAGNGGSVSKVLHIPTGTIMAKKVIHID---AKSSVRKQIL-RELQILHECHSPYIVSFYGAFLNEnNNIIICMEYMDC 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  97 ADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHD-NNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQLGESglV 175
Cdd:cd06620   89 GSLD-KILKKKGP---FPEEVLGKIAVAVLEGLTYLYNvHRIIHRDIKPSNILVNSK---GQIKLCDFGVSGELINS--I 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 176 AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLF-----EGIIKGKYKM----NPRQWSHI- 245
Cdd:cd06620  160 ADTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDgyngpMGILDLLQRIvnepPPRLPKDRi 239
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 548961101 246 -SESAKDLVRRMLMLDPAERITVYEALNHPWLKERDR 281
Cdd:cd06620  240 fPKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQAVR 276
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
12-277 4.98e-20

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: 92.99  E-value: 4.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftsspgLSTEDLKR--------EASICHMLKHPHIVELLETYSS 83
Cdd:cd05629    3 FHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTL----------LKSEMFKKdqlahvkaERDVLAESDSPWVVSLYYSFQD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGF 163
Cdd:cd05629   73 AQYLYLIMEFLPGGDLMTMLIKYD----TFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGH---IKLSDF 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 164 GV-----------------------------------AIQLGESG------------LVAGGRVGTPHFMAPEVVKREPY 196
Cdd:cd05629  146 GLstgfhkqhdsayyqkllqgksnknridnrnsvavdSINLTMSSkdqiatwkknrrLMAYSTVGTPDYIAPEIFLQQGY 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 197 GKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRmLMLDPAERITVY---EALN 272
Cdd:cd05629  226 GQECDWWSLGAIMFECLIGWPPFCSeNSHETYRKIINWRETLYFPDDIHLSVEAEDLIRR-LITNAENRLGRGgahEIKS 304

                 ....*
gi 548961101 273 HPWLK 277
Cdd:cd05629  305 HPFFR 309
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
74-276 1.09e-19

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: 89.64  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  74 IVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLasKE 153
Cdd:cd14100   67 VIRLLDWFERPDSFVLVLERPEPVQDLFDFITERGA---LPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILI--DL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 154 NSAPVKLGGFGVAIQLGESGLV--AGGRVGTPhfmaPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKErlfegI 230
Cdd:cd14100  142 NTGELKLIDFGSGALLKDTVYTdfDGTRVYSP----PEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPFEHDEE-----I 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 548961101 231 IKGKYKMNPRqwshISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14100  213 IRGQVFFRQR----VSSECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
10-278 1.12e-19

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: 90.91  E-value: 1.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTedlkREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd07869    5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAI----REASLLKGLKHANIVLLHDIIHTKETLTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDgADLCFEIVKRAdaGFVYSEAVaSHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQL 169
Cdd:cd07869   81 VFEYVH-TDLCQYMDKHP--GGLHPENV-KLFLFQLLRGLSYIHQRYILHRDLKPQNLLIS---DTGELKLADFGLARAK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGTK------ERLF-------EGIIKGKY 235
Cdd:cd07869  154 SVPSHTYSNEVVTLWYRPPDVlLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKdiqdqlERIFlvlgtpnEDTWPGVH 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 236 KM--------------NPRQ-WSHIS--ESAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd07869  234 SLphfkperftlyspkNLRQaWNKLSyvNHAEDLASKLLQCFPKNRLSAQAALSHEYFSD 293
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
125-273 1.51e-19

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: 90.16  E-value: 1.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 125 ILEALrycHDNNIIHRDVKPHCVLLASKENSapVKLGGFGVAIQL-GESGLVAGGRvGTPHFMAPEVVKREPY-GKPVDV 202
Cdd:cd13974  144 VVEAL---HKKNIVHRDLKLGNMVLNKRTRK--ITITNFCLGKHLvSEDDLLKDQR-GSPAYISPDVLSGKPYlGKPSDM 217
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 203 WGCGVILFILLSGCLPFY-GTKERLFEGIIKGKYKMnPRQwSHISESAKDLVRRMLMLDPAERITVYEALNH 273
Cdd:cd13974  218 WALGVVLFTMLYGQFPFYdSIPQELFRKIKAAEYTI-PED-GRVSENTVCLIRKLLVLNPQKRLTASEVLDS 287
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
12-275 1.81e-19

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: 89.71  E-value: 1.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQF-AVKIVDVAkfTSSPGLSTEDLKREASICHM--LKHPHIVELLETYS-----S 83
Cdd:cd07862    3 YECVAEIGEGAYGKVFKARDLKNGGRFvALKRVRVQ--TGEEGMPLSTIREVAVLRHLetFEHPNVVRLFDVCTvsrtdR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLYMVFEFMDgADLCFEIVKRADAGfVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGF 163
Cdd:cd07862   81 ETKLTLVFEHVD-QDLTTYLDKVPEPG-VPTETIKD-MMFQLLRGLDFLHSHRVVHRDLKPQNILVTS---SGQIKLADF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 164 GVA----IQLGESGLVAggrvgTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFE------ 228
Cdd:cd07862  155 GLAriysFQMALTSVVV-----TLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDvdqlgKILDviglpg 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 229 --------GIIKGKYKMNPRQ-----WSHISESAKDLVRRMLMLDPAERITVYEALNHPW 275
Cdd:cd07862  230 eedwprdvALPRQAFHSKSAQpiekfVTDIDELGKDLLLKCLTFNPAKRISAYSALSHPY 289
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
10-280 2.04e-19

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: 91.27  E-value: 2.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSteDLKREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd05627    2 DDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVA--HIRAERDILVEADGAWVVKMFYSFQDKRNLYL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQL 169
Cdd:cd05627   80 IMEFLPGGDMMTLLMKKD----TLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGH---VKLSDFGLCTGL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESG-----------------------------------LVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLS 214
Cdd:cd05627  153 KKAHrtefyrnlthnppsdfsfqnmnskrkaetwkknrrQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLI 232
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 215 GCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRmLMLDPAERI---TVYEALNHPWLKERD 280
Cdd:cd05627  233 GYPPFCSeTPQETYRKVMNWKETLVFPPEVPISEKAKDLILR-FCTDAENRIgsnGVEEIKSHPFFEGVD 301
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
9-280 2.13e-19

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: 90.19  E-value: 2.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEvIGKGPFSVVRRCINRETGQQFAVKIVdvaKFTSSPGLSTEDLkREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd06615    1 DDFEKLGE-LGAGNGGVVTKVLHRPSGLIMARKLI---HLEIKPAIRNQII-RELKVLHECNSPYIVGFYGAFYSDGEIS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGA--DLCFEIVKRADAGFVYSEAVAshymrqILEALRYCHDN-NIIHRDVKPHCVLLASkenSAPVKLGGFGV 165
Cdd:cd06615   76 ICMEHMDGGslDQVLKKAGRIPENILGKISIA------VLRGLTYLREKhKIMHRDVKPSNILVNS---RGEIKLCDFGV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 166 AIQLGESglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGII-----KGKYKMNPR 240
Cdd:cd06615  147 SGQLIDS--MANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKELEAMFgrpvsEGEAKESHR 224
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 241 QWS------------------------------HISESAKDLVRRMLMLDPAERITVYEALNHPWLKERD 280
Cdd:cd06615  225 PVSghppdsprpmaifelldyivnepppklpsgAFSDEFQDFVDKCLKKNPKERADLKELTKHPFIKRAE 294
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
11-276 2.30e-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: 88.86  E-value: 2.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREasICHMLKHPH----IVELLETYSS-DG 85
Cdd:cd14102    1 VYQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVPLE--IVLLKKVGSgfrgVIKLLDWYERpDG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 MLyMVFEFMDGADLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKenSAPVKLGGFGV 165
Cdd:cd14102   79 FL-IVMERPEPVKDLFDFITEKGA---LDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLR--TGELKLIDFGS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 166 AIQLGESGLV--AGGRVGTPhfmaPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKErlfegIIKGKYKMNPRqw 242
Cdd:cd14102  153 GALLKDTVYTdfDGTRVYSP----PEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPFEQDEE-----ILRGRLYFRRR-- 221
                        250       260       270
                 ....*....|....*....|....*....|....
gi 548961101 243 shISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14102  222 --VSPECQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
17-280 2.41e-19

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: 89.03  E-value: 2.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPG--LSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFM 94
Cdd:cd05606    1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGetLALNERIMLSLVSTGGDCPFIVCMTYAFQTPDKLCFILDLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  95 DGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGESGL 174
Cdd:cd05606   81 NGGDLHYHLSQHG----VFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILL---DEHGHVRISDLGLACDFSKKKP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 175 VAGgrVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLV 253
Cdd:cd05606  154 HAS--VGTHGYMAPEVLqKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKHEIDRMTLTMNVELPDSFSPELKSLL 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 548961101 254 RRMLMLDPAERI-----TVYEALNHPWLKERD 280
Cdd:cd05606  232 EGLLQRDVSKRLgclgrGATEVKEHPFFKGVD 263
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
17-221 2.66e-19

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: 88.94  E-value: 2.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRetGQQFAVKIV------DVAKftsspglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd14146    1 IIGVGGFGKVYRATWK--GQEVAVKAArqdpdeDIKA-------TAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLcfeivKRADAGFVYSEA----------VASHYMRQILEALRYCHDNN---IIHRDVKPHCVLLASK-EN-- 154
Cdd:cd14146   72 MEFARGGTL-----NRALAAANAAPGprrarripphILVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLLEKiEHdd 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 155 --SAPVKLGGFGVAIQLGESGLVAGGrvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 221
Cdd:cd14146  147 icNKTLKITDFGLAREWHRTTKMSAA--GTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRG 213
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
12-277 2.79e-19

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 93.65  E-value: 2.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftSSPGLSTED---LKREASICHMLKHPHIVELLETY--SSDGM 86
Cdd:PTZ00266   15 YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAI------SYRGLKEREksqLVIEVNVMRELKHKNIVRYIDRFlnKANQK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   87 LYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHD-------NNIIHRDVKPHCVLL---------- 149
Cdd:PTZ00266   89 LYILMEFCDAGDLSRNIQKCYKMFGKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLstgirhigki 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  150 ---ASKENSAPV-KLGGFGVAIQLG-ESglVAGGRVGTPHFMAPEVVKRE--PYGKPVDVWGCGVILFILLSGCLPFYgt 222
Cdd:PTZ00266  169 taqANNLNGRPIaKIGDFGLSKNIGiES--MAHSCVGTPYYWSPELLLHEtkSYDDKSDMWALGCIIYELCSGKTPFH-- 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101  223 KERLFEGIIKgKYKMNPRQwsHISESAKD---LVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:PTZ00266  245 KANNFSQLIS-ELKRGPDL--PIKGKSKElniLIKNLLNLSAKERPSALQCLGYQIIK 299
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
10-299 2.84e-19

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: 90.40  E-value: 2.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVdVAKFTSSpgLSTEDLKREASICHMLKHPHIVELLETYSSDGML-- 87
Cdd:cd07880   15 DRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKL-YRPFQSE--LFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLdr 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 ----YMVFEFMdGADLCfEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCvlLASKENsAPVKLGGF 163
Cdd:cd07880   92 fhdfYLVMPFM-GTDLG-KLMKHEK----LSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGN--LAVNED-CELKILDF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 164 GVAIQlGESGLVagGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFE------------ 228
Cdd:cd07880  163 GLARQ-TDSEMT--GYVVTRWYRAPEVIlNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDhlDQLMEimkvtgtpskef 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 229 ----------GIIKGKYKMNPRQWSHI----SESAKDLVRRMLMLDPAERITVYEALNHPWLKErdryaykIHLPETVEQ 294
Cdd:cd07880  240 vqklqsedakNYVKKLPRFRKKDFRSLlpnaNPLAVNVLEKMLVLDAESRITAAEALAHPYFEE-------FHDPEDETE 312

                 ....*
gi 548961101 295 LRKFN 299
Cdd:cd07880  313 APPYD 317
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
12-276 3.08e-19

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: 90.00  E-value: 3.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakfTSSPGLSTEDLKrEASICHML--------KHpHIVELLETYSS 83
Cdd:cd14212    1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVL-----KNKPAYFRQAML-EIAILTLLntkydpedKH-HIVRLLDHFMH 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLYMVFEfMDGADLcFEIVK-RADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkENSAPVKLGG 162
Cdd:cd14212   74 HGHLCIVFE-LLGVNL-YELLKqNQFRGL--SLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVN-LDSPEIKLID 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 163 FGVA----------IQlgesglvaggrvgTPHFMAPEVVKREPYGKPVDVW--GC-------GVILF------------I 211
Cdd:cd14212  149 FGSAcfenytlytyIQ-------------SRFYRSPEVLLGLPYSTAIDMWslGCiaaelflGLPLFpgnseynqlsriI 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 212 LLSGCLPFY----GTK-----ERLFEGIIKGKYKM--------------------------------NPRQWSHISESAK 250
Cdd:cd14212  216 EMLGMPPDWmlekGKNtnkffKKVAKSGGRSTYRLktpeefeaenncklepgkryfkyktlediimnYPMKKSKKEQIDK 295
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 548961101 251 ---------DLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14212  296 emetrlafiDFLKGLLEYDPKKRWTPDQALNHPFI 330
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
18-276 3.84e-19

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: 88.91  E-value: 3.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTedlkREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDgA 97
Cdd:cd07871   13 LGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAI----REVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLD-S 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLCFEIvkrADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQLGESGLVAG 177
Cdd:cd07871   88 DLKQYL---DNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEK---GELKLADFGLARAKSVPTKTYS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 178 GRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGT--KERL-----------------------FEGII 231
Cdd:cd07871  162 NEVVTLWYRPPDVlLGSTEYSTPIDMWGVGCILYEMATGRPMFPGStvKEELhlifrllgtpteetwpgvtsneeFRSYL 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 548961101 232 KGKYKMNP--RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd07871  242 FPQYRAQPliNHAPRLDTDGIDLLSSLLLYETKSRISAEAALRHSYF 288
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
17-272 3.98e-19

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: 88.55  E-value: 3.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKivdVAKFTSSPglSTEDLKREASICHML-KHPHIVELL--ETYSSDGML--YMVF 91
Cdd:cd13985    7 QLGEGGFSYVYLAHDVNTGRRYALK---RMYFNDEE--QLRVAIKEIEIMKRLcGHPNIVQYYdsAILSSEGRKevLLLM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGAdLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLASKENsapVKLGGFGVA--- 166
Cdd:cd13985   82 EYCPGS-LVDILEKSPPSPL--SEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGR---FKLCDFGSAtte 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 ---------IQLGESGLvagGRVGTPHFMAPEVV---KREPYGKPVDVWGCGVILFILLSGCLPFygtKERLFEGIIKGK 234
Cdd:cd13985  156 hypleraeeVNIIEEEI---QKNTTPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPF---DESSKLAIVAGK 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 548961101 235 YKM--NPRQwshiSESAKDLVRRMLMLDPAERITVYEALN 272
Cdd:cd13985  230 YSIpeQPRY----SPELHDLIRHMLTPDPAERPDIFQVIN 265
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
3-281 4.15e-19

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: 89.33  E-value: 4.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   3 DDDVLFEDVYElcevIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTE---DLKREASICHMLKHPHIVELLE 79
Cdd:cd06633   18 DPEEIFVDLHE----IGHGSFGAVYFATNSHTNEVVAIK-----KMSYSGKQTNEkwqDIIKEVKFLQQLKHPNTIEYKG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  80 TYSSDGMLYMVFEFMDGA--DLcFEIVKRAdagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAP 157
Cdd:cd06633   89 CYLKDHTAWLVMEYCLGSasDL-LEVHKKP-----LQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTE---PGQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 158 VKLGGFGVAIQLGEsglvAGGRVGTPHFMAPEVV---KREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEGIIK 232
Cdd:cd06633  160 VKLADFGSASIASP----ANSFVGTPYWMAPEVIlamDEGQYDGKVDIWSLGITCIELAERKPPLFNMNamSALYHIAQN 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 548961101 233 GKYKMNPRQWshiSESAKDLVRRMLMLDPAERITVYEALNHPWLKeRDR 281
Cdd:cd06633  236 DSPTLQSNEW---TDSFRGFVDYCLQKIPQERPSSAELLRHDFVR-RER 280
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
17-219 5.38e-19

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: 87.73  E-value: 5.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRetGQQFAVKIVDVAKfTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDG 96
Cdd:cd14148    1 IIGVGGFGKVYKGLWR--GEEVAVKAARQDP-DEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  97 ADLcfeivKRADAGFVYSEAVASHYMRQILEALRYCHDNN---IIHRDVKPHCVLLASK-EN----SAPVKLGGFGVAIQ 168
Cdd:cd14148   78 GAL-----NRALAGKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEPiENddlsGKTLKITDFGLARE 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 548961101 169 LGESGLVAGGrvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF 219
Cdd:cd14148  153 WHKTTKMSAA--GTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
7-276 9.30e-19

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: 87.12  E-value: 9.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   7 LFEDVYElcevIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTE---DLKREASICHMLKHPHIVELLETYSS 83
Cdd:cd06607    2 IFEDLRE----IGHGSFGAVYYARNKRTSEVVAIK-----KMSYSGKQSTEkwqDIIKEVKFLRQLRHPNTIEYKGCYLR 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLYMVFEFMDG--ADLcFEIVKRAdagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLG 161
Cdd:cd06607   73 EHTAWLVMEYCLGsaSDI-VEVHKKP-----LQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTE---PGTVKLA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 162 GFGVAiqlgesGLV--AGGRVGTPHFMAPEVV---KREPYGKPVDVWGCGVIlfillsgCLPFYGTKERLFegiikgkyK 236
Cdd:cd06607  144 DFGSA------SLVcpANSFVGTPYWMAPEVIlamDEGQYDGKVDVWSLGIT-------CIELAERKPPLF--------N 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 548961101 237 MNPR--------------QWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd06607  203 MNAMsalyhiaqndsptlSSGEWSDDFRNFVDSCLQKIPQDRPSAEDLLKHPFV 256
PLN02772 PLN02772
guanylate kinase
734-911 1.08e-18

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 89.51  E-value: 1.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 734 KTLVLLGAHGVGrrhiKNTLITK----HPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAM 809
Cdd:PLN02772 136 KPIVISGPSGVG----KGTLISMlmkeFPSMFGFSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFASVHGNL 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 810 YGTKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTITP--------GLNEDESLQ-RLQK-ESDVLQRT 879
Cdd:PLN02772 212 YGTSIEAVEVVTDSGKRCILDIDVQGARSVRASSLEAIFIFICPPSMEElekrlrarGTETEEQIQkRLRNaEAELEQGK 291
                        170       180       190
                 ....*....|....*....|....*....|..
gi 548961101 880 YAHYFDLTIINNEIDETIRHLEEAVELVCTAP 911
Cdd:PLN02772 292 SSGIFDHILYNDNLEECYKNLKKLLGLDGLAA 323
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
17-265 1.24e-18

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: 88.25  E-value: 1.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEDLKREASICHMLK----HPHIVELLETYSSDGMLYMVFE 92
Cdd:cd05588    2 VIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDD-----EDIDWVQTEKHVFEtasnHPFLVGLHSCFQTESRLFFVIE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  93 FMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGES 172
Cdd:cd05588   77 FVNGGDLMFHMQRQRR----LPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGH---IKLTDYGMCKEGLRP 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 173 GLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF----------YGTKERLFEGIIKGKYKMnPRQw 242
Cdd:cd05588  150 GDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgssdnpdQNTEDYLFQVILEKPIRI-PRS- 227
                        250       260
                 ....*....|....*....|...
gi 548961101 243 shISESAKDLVRRMLMLDPAERI 265
Cdd:cd05588  228 --LSVKAASVLKGFLNKNPAERL 248
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
12-283 1.37e-18

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: 88.24  E-value: 1.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftSSPGLSTEDLKR---EASICHMLKHPHIVELLETYSSDGML- 87
Cdd:cd07850    2 YQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKL------SRPFQNVTHAKRayrELVLMKLVNHKNIIGLLNVFTPQKSLe 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 -----YMVFEFMDgADLCFEIVKRADagfvysEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGG 162
Cdd:cd07850   76 efqdvYLVMELMD-ANLCQVIQMDLD------HERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD---CTLKILD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 163 FGVAIQLGESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK------------------- 223
Cdd:cd07850  146 FGLARTAGTSFMMT-PYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDhidqwnkiieqlgtpsdef 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 224 -ERLfeGIIKGKYKMN-PRQWSH---------------------ISESAKDLVRRMLMLDPAERITVYEALNHP----WL 276
Cdd:cd07850  225 mSRL--QPTVRNYVENrPKYAGYsfeelfpdvlfppdseehnklKASQARDLLSKMLVIDPEKRISVDDALQHPyinvWY 302

                 ....*..
gi 548961101 277 KERDRYA 283
Cdd:cd07850  303 DPSEVEA 309
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
8-276 2.92e-18

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: 86.99  E-value: 2.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCEVIGKGPFSVVRRCINRETGQ-QFAVKIV-DVAKFTSSPGLSTEDLKR-------EASICHMLKhphivell 78
Cdd:cd14214   11 LQERYEIVGDLGEGTFGKVVECLDHARGKsQVALKIIrNVGKYREAARLEINVLKKikekdkeNKFLCVLMS-------- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  79 ETYSSDGMLYMVFEFMDGAdlCFEIVKRADagFV-YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE---- 153
Cdd:cd14214   83 DWFNFHGHMCIAFELLGKN--TFEFLKENN--FQpYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVNSEfdtl 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 154 ------------NSAPVKLGGFGVAIQLGESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 221
Cdd:cd14214  159 ynesksceeksvKNTSIRVADFGSATFDHEHHTTI---VATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 222 TKER----LFEGII------------KGKY--------KMNPRQWSHISESAK-----------------DLVRRMLMLD 260
Cdd:cd14214  236 HENRehlvMMEKILgpipshmihrtrKQKYfykgslvwDENSSDGRYVSENCKplmsymlgdslehtqlfDLLRRMLEFD 315
                        330
                 ....*....|....*.
gi 548961101 261 PAERITVYEALNHPWL 276
Cdd:cd14214  316 PALRITLKEALLHPFF 331
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
9-278 3.26e-18

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: 85.87  E-value: 3.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd06645   10 QEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKL-----EPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLW 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLcfeivkrADAGFV---YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGV 165
Cdd:cd06645   85 ICMEFCGGGSL-------QDIYHVtgpLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLT---DNGHVKLADFGV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 166 AIQLGESGLVAGGRVGTPHFMAPEVV---KREPYGKPVDVWGCGVILFILLSGCLP----------FYGTKERLFEGIIK 232
Cdd:cd06645  155 SAQITATIAKRKSFIGTPYWMAPEVAaveRKGGYNQLCDIWAVGITAIELAELQPPmfdlhpmralFLMTKSNFQPPKLK 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 548961101 233 GKYKmnprqWSHiseSAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd06645  235 DKMK-----WSN---SFHHFVKMALTKNPKKRPTAEKLLQHPFVTQ 272
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
18-274 3.44e-18

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: 85.58  E-value: 3.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDvakftSSPGLSTE--DLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 95
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLH-----SSPNCIEErkALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYME 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLcFEIVKRADAGFVYSeaVASHYMRQILEALRYCH--DNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGESG 173
Cdd:cd13978   76 NGSL-KSLLEREIQDVPWS--LRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILL---DNHFHVKISDFGLSKLGMKSI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 174 LVAGGRV-----GTPHFMAPEVVkREPYGKPV---DVWGCGVILFILLSGCLPFYGTKERL--FEGIIKGKYKM-----N 238
Cdd:cd13978  150 SANRRRGtenlgGTPIYMAPEAF-DDFNKKPTsksDVYSFAIVIWAVLTRKEPFENAINPLliMQIVSKGDRPSlddigR 228
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 548961101 239 PRQWSHISEsAKDLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd13978  229 LKQIENVQE-LISLMIRCWDGNPDARPTFLECLDRL 263
SH3_MPP5 cd12036
Src Homology 3 domain of Membrane Protein, Palmitoylated 5 (or MAGUK p55 subfamily member 5); ...
610-670 4.03e-18

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: 78.99  E-value: 4.03e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548961101 610 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQG--KLENSKNGTAGLIPSPE 670
Cdd:cd12036    1 HVRAHFDYDPEDDPYIPCRELGLSFQKGDILHVISQEDPNWWQAyrEGEEDNQSLAGLIPSKS 63
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
12-276 4.35e-18

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: 87.01  E-value: 4.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftSSPGLSTEDLKR---EASICHMLKHPHIVELLETYSSDGML- 87
Cdd:cd07876   23 YQQLKPIGSGAQGIVCAAFDTVLGINVAVKKL------SRPFQNQTHAKRayrELVLLKCVNHKNIISLLNVFTPQKSLe 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 -----YMVFEFMDgADLCFEIVKRADagfvysEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGG 162
Cdd:cd07876   97 efqdvYLVMELMD-ANLCQVIHMELD------HERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS---DCTLKILD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 163 FGVAiQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE------------------ 224
Cdd:cd07876  167 FGLA-RTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHidqwnkvieqlgtpsaef 245
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548961101 225 --RLFEGIikGKYKMNPRQ------------WSHISES---------AKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd07876  246 mnRLQPTV--RNYVENRPQypgisfeelfpdWIFPSESerdklktsqARDLLSKMLVIDPDKRISVDEALRHPYI 318
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
18-209 4.47e-18

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: 84.83  E-value: 4.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIvdvAKFTSSPGlsteDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKM---NTLSSNRA----NMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLcfeiVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVA--IQLGESGLV 175
Cdd:cd14155   74 NL----EQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVVGDFGLAekIPDYSDGKE 149
                        170       180       190
                 ....*....|....*....|....*....|....
gi 548961101 176 AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVIL 209
Cdd:cd14155  150 KLAVVGSPYWMAPEVLRGEPYNEKADVFSYGIIL 183
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
12-255 9.18e-18

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: 86.25  E-value: 9.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSteDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd05628    3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVG--HIRAERDILVEADSLWVVKMFYSFQDKLNLYLIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 171
Cdd:cd05628   81 EFLPGGDMMTLLMKKD----TLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGH---VKLSDFGLCTGLKK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SG-----------------------------------LVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGC 216
Cdd:cd05628  154 AHrtefyrnlnhslpsdftfqnmnskrkaetwkrnrrQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGY 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 548961101 217 LPFYG-TKERLFEGIIKGKYKMNPRQWSHISESAKDLVRR 255
Cdd:cd05628  234 PPFCSeTPQETYKKVMNWKETLIFPPEVPISEKAKDLILR 273
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
14-267 9.58e-18

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: 84.44  E-value: 9.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  14 LCEVIGKGPFSVVRR--CINRETGQQFAVKIVDVAKFTSSPGLStEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd05049    9 LKRELGEGAFGKVFLgeCYNLEPEQDKMLVAVKTLKDASSPDAR-KDFEREAELLTNLQHENIVKFYGVCTEGDPLLMVF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCfEIVKR--ADAGFVYSEAVAS---------HYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKL 160
Cdd:cd05049   88 EYMEHGDLN-KFLRShgPDAAFLASEDSAPgeltlsqllHIAVQIASGMVYLASQHFVHRDLATRNCLVGTN---LVVKI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 161 GGFGVA--IQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYG-TKERLFEGIIKGKYK 236
Cdd:cd05049  164 GDFGMSrdIYSTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWeIFTYGKQPWFQlSNTEVIECITQGRLL 243
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 548961101 237 MNPRqwshiseSAKDLVRRmLML-----DPAERITV 267
Cdd:cd05049  244 QRPR-------TCPSEVYA-VMLgcwkrEPQQRLNI 271
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
12-276 9.92e-18

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: 84.72  E-value: 9.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglSTEDLK---------REASICHMLKHPHIVELLETYS 82
Cdd:cd14040    8 YLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNK-------SWRDEKkenyhkhacREYRIHKELDHPRIVKLYDYFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  83 SDGMLY-MVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLASKENSAPVK 159
Cdd:cd14040   81 LDTDTFcTVLEYCEGNDLDFYLKQHK----LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 160 LGGFGVAIQLGESGLVAGGR------VGTPHFMAPE--VVKREP--YGKPVDVWGCGVILFILLSGCLPF---YGTKERL 226
Cdd:cd14040  157 ITDFGLSKIMDDDSYGVDGMdltsqgAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFghnQSQQDIL 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 548961101 227 FEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14040  237 QENTILKATEVQFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
10-278 1.02e-17

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: 85.86  E-value: 1.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftSSPGLSTEDLKR---EASICHMLKHPHIVELLETYSSDGM 86
Cdd:cd07877   17 ERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKL------SRPFQSIIHAKRtyrELRLLKHMKHENVIGLLDVFTPARS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 L------YMVFEFMdGADLCfEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCvlLASKENsAPVKL 160
Cdd:cd07877   91 LeefndvYLVTHLM-GADLN-NIVKCQK----LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSN--LAVNED-CELKI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 161 GGFGVAIQLGESglvAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE--------------- 224
Cdd:cd07877  162 LDFGLARHTDDE---MTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHidqlklilrlvgtpg 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548961101 225 -RLFEGI--------IKGKYKMNPRQWSHI----SESAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd07877  239 aELLKKIssesarnyIQSLTQMPKMNFANVfigaNPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQ 305
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
62-280 1.10e-17

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 85.42  E-value: 1.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  62 EASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRD 141
Cdd:PTZ00426  81 ERKILNYINHPFCVNLYGSFKDESYLYLVLEFVIGGEF-FTFLRRNKR---FPNDVGCFYAAQIVLIFEYLQSLNIVYRD 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 142 VKPHCVLLaskENSAPVKLGGFGVAIQLGESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 221
Cdd:PTZ00426 157 LKPENLLL---DKDGFIKMTDFGFAKVVDTRTYTL---CGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYA 230
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 222 TK-----ERLFEGIIkgkykMNPRqwsHISESAKDLVRRMLMLDPAERI-----TVYEALNHPWLKERD 280
Cdd:PTZ00426 231 NEplliyQKILEGII-----YFPK---FLDNNCKHLMKKLLSHDLTKRYgnlkkGAQNVKEHPWFGNID 291
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
12-273 1.11e-17

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: 84.27  E-value: 1.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkftsspglSTEDLK---REASICHMLKHPHIVELLET---YSSDG 85
Cdd:cd13986    2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCH--------SKEDVKeamREIENYRLFNHPNILRLLDSqivKEAGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 --MLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNII---HRDVKPHCVLLAskENSAPVkL 160
Cdd:cd13986   74 kkEVYLLLPYYKRGSLQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLS--EDDEPI-L 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 161 GGFGVAIQlgeSGLVAGGRV------------GTPHFMAPEVVKREPYG---KPVDVWGCGVILFILLSGCLPF---YGT 222
Cdd:cd13986  151 MDLGSMNP---ARIEIEGRRealalqdwaaehCTMPYRAPELFDVKSHCtidEKTDIWSLGCTLYALMYGESPFeriFQK 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 548961101 223 KERLFEGIIKGKYKMnPRQwSHISESAKDLVRRMLMLDPAERITVYEALNH 273
Cdd:cd13986  228 GDSLALAVLSGNYSF-PDN-SRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
18-276 1.18e-17

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: 85.32  E-value: 1.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKivDVAKFTSSPGLSTEDLkREASICHMLKHPHIVELLETYSSDGM-LYMVFEFMdG 96
Cdd:cd07856   18 VGMGAFGLVCSARDQLTGQNVAVK--KIMKPFSTPVLAKRTY-RELKLLKHLRHENIISLSDIFISPLEdIYFVTELL-G 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  97 ADLCFEIVKRAdagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLasKENsAPVKLGGFGVAiQLGESGLVa 176
Cdd:cd07856   94 TDLHRLLTSRP-----LEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILV--NEN-CDLKICDFGLA-RIQDPQMT- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 177 gGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGcLPFYGTKERLFEGIIKGKYKMNP---------------- 239
Cdd:cd07856  164 -GYVSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEG-KPLFPGKDHVNQFSIITELLGTPpddvinticsentlrf 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 548961101 240 ------RQWSHISE-------SAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd07856  242 vqslpkRERVPFSEkfknadpDAIDLLEKMLVFDPKKRISAAEALAHPYL 291
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
18-256 1.52e-17

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: 83.26  E-value: 1.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRetGQQFAVKIVDVAKftsspglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd14058    1 VGRGSFGVVCKARWR--NQIVAVKIIESES-------EKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLcFEIVKRADAGFVYSEAVASHYMRQILEALRYCH---DNNIIHRDVKPHCVLLASKENSapVKLGGFGVAIQLgeSGL 174
Cdd:cd14058   72 SL-YNVLHGKEPKPIYTAAHAMSWALQCAKGVAYLHsmkPKALIHRDLKPPNLLLTNGGTV--LKICDFGTACDI--STH 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 175 VAGGRvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF---------------YGTKERLFEGIIKGKYKMNP 239
Cdd:cd14058  147 MTNNK-GSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFdhiggpafrimwavhNGERPPLIKNCPKPIESLMT 225
                        250       260
                 ....*....|....*....|
gi 548961101 240 RQWSHISE---SAKDLVRRM 256
Cdd:cd14058  226 RCWSKDPEkrpSMKEIVKIM 245
PDZ_MPP5-like cd06798
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related ...
483-563 1.64e-17

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: 77.77  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 483 RLVQFQKnTDEPMGITLKmNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIV 562
Cdd:cd06798    1 KIVRIEK-TREPLGATVR-NEGDSVIISRIVKGGAAEKSGLLHEGDEILEINGIEIRGKDVNEVCDLLADMHGTLTFLLI 78

                 .
gi 548961101 563 P 563
Cdd:cd06798   79 P 79
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
14-221 1.70e-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: 83.54  E-value: 1.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  14 LCEVIGKGPFSVVRRCINRetGQQFAVKivdVAKFTSSPGLST--EDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14147    7 LEEVIGIGGFGKVYRGSWR--GELVAVK---AARQDPDEDISVtaESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcfeivKRADAGFVYSEAVASHYMRQILEALRYCHDNNI---IHRDVKPHCVLLASK-ENSA----PVKLGGF 163
Cdd:cd14147   82 EYAAGGPL-----SRALAGRRVPPHVLVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLLQPiENDDmehkTLKITDF 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101 164 GVAIQLGESGLVAGGrvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 221
Cdd:cd14147  157 GLAREWHKTTQMSAA--GTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRG 212
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
18-278 2.12e-17

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: 83.62  E-value: 2.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSS----DGMLYMVFEF 93
Cdd:cd14031   18 LGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKA---EQQRFKEEAEMLKGLQHPNIVRFYDSWESvlkgKKCIVLVTEL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  94 MDGADLCfEIVKRADagfVYSEAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLASKENSapVKLGGFGVAIQLGE 171
Cdd:cd14031   95 MTSGTLK-TYLKRFK---VMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTGS--VKIGDLGLATLMRT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SglVAGGRVGTPHFMAPEVVKrEPYGKPVDVWGCGVILFILLSGCLPFYGTKE--RLFEGIIKGkykMNPRQWSHISE-S 248
Cdd:cd14031  169 S--FAKSVIGTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPYSECQNaaQIYRKVTSG---IKPASFNKVTDpE 242
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd14031  243 VKEIIEGCIRQNKSERLSIKDLLNHAFFAE 272
SH3_MPP3 cd12039
Src Homology 3 domain of Membrane Protein, Palmitoylated 3 (or MAGUK p55 subfamily member 3); ...
610-668 2.12e-17

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: 76.92  E-value: 2.12e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 610 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPS 668
Cdd:cd12039    1 FMRALFDYNPYEDRAIPCQEAGLPFKRRDILEVVSQDDPTWWQAKRVGDTNLRAGLIPS 59
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
15-277 2.37e-17

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: 83.57  E-value: 2.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  15 CEVIGKGPFSVVRRCINRETGQQFAVK----IVDvakftsspGLSTEDLKRE------ASIChmlkhPHIVELLETYSSD 84
Cdd:cd06616   11 LGEIGRGAFGTVNKMLHKPSGTIMAVKrirsTVD--------EKEQKRLLMDldvvmrSSDC-----PYIVKFYGALFRE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  85 GMLYMVFEFMDGA-DLCFEIVKRADAGfVYSEAVASHYMRQILEALRYCHDN-NIIHRDVKPHCVLLASKENsapVKLGG 162
Cdd:cd06616   78 GDCWICMELMDISlDKFYKYVYEVLDS-VIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGN---IKLCD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 163 FGVAIQLGESglVAGGR-VGTPHFMAPEVV----KREPYGKPVDVWGCGVILFILLSGCLPFYGTKErLFEGI---IKGK 234
Cdd:cd06616  154 FGISGQLVDS--IAKTRdAGCRPYMAPERIdpsaSRDGYDVRSDVWSLGITLYEVATGKFPYPKWNS-VFDQLtqvVKGD 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 548961101 235 Y-KMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd06616  231 PpILSNSEEREFSPSFVNFVNLCLIKDESKRPKYKELLKHPFIK 274
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1-280 3.12e-17

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: 83.95  E-value: 3.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   1 MADDDvlFEDVYELceviGKGPFSVVRRCINRETGQQFAVKIVdvaKFTSSPGLSTEdLKREASICHMLKHPHIVELLET 80
Cdd:cd06650    2 LKDDD--FEKISEL----GAGNGGVVFKVSHKPSGLVMARKLI---HLEIKPAIRNQ-IIRELQVLHECNSPYIVGFYGA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  81 YSSDGMLYMVFEFMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHD-NNIIHRDVKPHCVLLASKensAPVK 159
Cdd:cd06650   72 FYSDGEISICMEHMDGGSLD-QVLKKAGR---IPEQILGKVSIAVIKGLTYLREkHKIMHRDVKPSNILVNSR---GEIK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 160 LGGFGVAIQLGESglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF----YGTKERLFEGIIKG-- 233
Cdd:cd06650  145 LCDFGVSGQLIDS--MANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIpppdAKELELMFGCQVEGda 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 234 ---------------KYKMNPRQWSHISE--------------------SAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd06650  223 aetpprprtpgrplsSYGMDSRPPMAIFElldyivnepppklpsgvfslEFQDFVNKCLIKNPAERADLKQLMVHAFIKR 302

                 ..
gi 548961101 279 RD 280
Cdd:cd06650  303 SD 304
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
10-292 3.20e-17

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: 83.50  E-value: 3.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTedlkREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd07872    6 ETYIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAI----REVSLLKDLKHANIVTLHDIVHTDKSLTL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDgADLCFEIvkrADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQL 169
Cdd:cd07872   82 VFEYLD-KDLKQYM---DDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINER---GELKLADFGLARAK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGT----------------KERLFEGIIK 232
Cdd:cd07872  155 SVPTKTYSNEVVTLWYRPPDVlLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGStvedelhlifrllgtpTEETWPGISS 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 233 G---------KYKMNP--RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKErdrYAYKIH-LPETV 292
Cdd:cd07872  235 NdefknynfpKYKPQPliNHAPRLDTEGIELLTKFLQYESKKRISAEEAMKHAYFRS---LGTRIHsLPESI 303
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
484-561 3.23e-17

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


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 76.94  E-value: 3.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  484 LVQFQKNTDEPMGITLKMNELNH---CIVARIMHGGMIHRQGtLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFK 560
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGdpgIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                  .
gi 548961101  561 I 561
Cdd:pfam00595  80 I 80
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
18-209 4.30e-17

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: 82.18  E-value: 4.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIV--DVAKftsspglstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 95
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIYknDVDQ---------HKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLCfEIVKRADAGFVYSEAVAshYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLV 175
Cdd:cd14156   72 GGCLE-ELLAREELPLSWREKVE--LACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAVVTDFGLAREVGEMPAN 148
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 548961101 176 AGGR----VGTPHFMAPEVVKREPYGKPVDVWGCGVIL 209
Cdd:cd14156  149 DPERklslVGSAFWMAPEMLRGEPYDRKVDVFSFGIVL 186
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
12-207 4.97e-17

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: 82.00  E-value: 4.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd06646   11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIKL-----EPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcfeivkrADAGFV---YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQ 168
Cdd:cd06646   86 EYCGGGSL-------QDIYHVtgpLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLT---DNGDVKLADFGVAAK 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 548961101 169 LGESGLVAGGRVGTPHFMAPEVVKREP---YGKPVDVWGCGV 207
Cdd:cd06646  156 ITATIAKRKSFIGTPYWMAPEVAAVEKnggYNQLCDIWAVGI 197
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
8-277 5.78e-17

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: 83.29  E-value: 5.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELceviGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDG-- 85
Cdd:cd07854    7 YMDLRPL----GCGSNGLVFSAVDSDCDKRVAVK-----KIVLTDPQSVKHALREIKIIRRLDHDNIVKVYEVLGPSGsd 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 ------------MLYMVFEFMDgADLCFEIVKRAdagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE 153
Cdd:cd07854   78 ltedvgsltelnSVYIVQEYME-TDLANVLEQGP-----LSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTED 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 154 nsAPVKLGGFGVAIQL----GESGLVAGGRVgTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLF 227
Cdd:cd07854  152 --LVLKIGDFGLARIVdphySHKGYLSEGLV-TKWYRSPRLLlSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHElEQM 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548961101 228 EGIIK---------------------GKYKMNPRQ-----WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLK 277
Cdd:cd07854  229 QLILEsvpvvreedrnellnvipsfvRNDGGEPRRplrdlLPGVNPEALDFLEQILTFNPMDRLTAEEALMHPYMS 304
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
7-276 6.49e-17

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: 82.62  E-value: 6.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   7 LFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAK-FTSSPGLSTEDLK--REASICHMLKHpHIVELLETYSS 83
Cdd:cd14136    7 VYNGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQhYTEAALDEIKLLKcvREADPKDPGRE-HVVQLLDDFKH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGM----LYMVFEFMdGADLCFEIvKRADAGFVYSEAVAShYMRQILEALRYCHDN-NIIHRDVKPHCVLLASKEnsAPV 158
Cdd:cd14136   86 TGPngthVCMVFEVL-GPNLLKLI-KRYNYRGIPLPLVKK-IARQVLQGLDYLHTKcGIIHTDIKPENVLLCISK--IEV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 159 KLGGFGVA----------IQlgesglvaggrvgTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY-------- 220
Cdd:cd14136  161 KIADLGNAcwtdkhftedIQ-------------TRQYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFDphsgedys 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 221 -----------------------GTKERLF------------------EGIIKGKYKMNPRQWSHISesakDLVRRMLML 259
Cdd:cd14136  228 rdedhlaliiellgriprsiilsGKYSREFfnrkgelrhisklkpwplEDVLVEKYKWSKEEAKEFA----SFLLPMLEY 303
                        330
                 ....*....|....*..
gi 548961101 260 DPAERITVYEALNHPWL 276
Cdd:cd14136  304 DPEKRATAAQCLQHPWL 320
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
9-280 8.30e-17

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: 81.85  E-value: 8.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELcEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftssPGLSTEDLKR----EASICHMLKHPHIVELLETYSSD 84
Cdd:cd06619    1 QDIQYQ-EILGHGNGGTVYKAYHLLTRRILAVKVI--------PLDITVELQKqimsELEILYKCDSPYIIGFYGAFFVE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  85 GMLYMVFEFMDGADLcfEIVKRADAGFVYSEAVAshymrqILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFG 164
Cdd:cd06619   72 NRISICTEFMDGGSL--DVYRKIPEHVLGRIAVA------VVKGLTYLWSLKILHRDVKPSNMLVNTR---GQVKLCDFG 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 165 VAIQLGESglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE--------RLFEGIIKGKYK 236
Cdd:cd06619  141 VSTQLVNS--IAKTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKnqgslmplQLLQCIVDEDPP 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 548961101 237 MNPRqwSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERD 280
Cdd:cd06619  219 VLPV--GQFSEKFVHFITQCMRKQPKERPAPENLMDHPFIVQYN 260
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
10-278 1.19e-16

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: 81.59  E-value: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTedlkREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd07873    2 ETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTAI----REVSLLKDLKHANIVTLHDIIHTEKSLTL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDgADLCFEIvkrADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQL 169
Cdd:cd07873   78 VFEYLD-KDLKQYL---DDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINER---GELKLADFGLARAK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGT----------------KERLFEGIIK 232
Cdd:cd07873  151 SIPTKTYSNEVVTLWYRPPDIlLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGStveeqlhfifrilgtpTEETWPGILS 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101 233 G---------KYKMNPRQwSH---ISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd07873  231 NeefksynypKYRADALH-NHaprLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFHS 287
gmk PRK14737
guanylate kinase; Provisional
734-911 1.70e-16

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 78.50  E-value: 1.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 734 KTLVLLGAHGVGRRHIKNTLITKHPDrFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTK 813
Cdd:PRK14737   5 KLFIISSVAGGGKSTIIQALLEEHPD-FLFSISCTTRAPRPGDEEGKTYFFLTIEEFKKGIADGEFLEWAEVHDNYYGTP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 814 LETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFV-VFIAAPT--------ITPGLNEDES-LQRLQKESDVLQRtyAHY 883
Cdd:PRK14737  84 KAFIEDAFKEGRSAIMDIDVQGAKIIKEKFPERIVtIFIEPPSeeeweerlIHRGTDSEESiEKRIENGIIELDE--ANE 161
                        170       180
                 ....*....|....*....|....*...
gi 548961101 884 FDLTIINNEIDETIRHLEeavELVCTAP 911
Cdd:PRK14737 162 FDYKIINDDLEDAIADLE---AIICGKK 186
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
8-276 2.01e-16

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: 81.26  E-value: 2.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLST--EDLKREASICHMLKHPHIVELLETYSSDG 85
Cdd:cd14041    4 LNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENyhKHACREYRIHKELDHPRIVKLYDYFSLDT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  86 MLY-MVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLASKENSAPVKLGG 162
Cdd:cd14041   84 DSFcTVLEYCEGNDLDFYLKQHK----LMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTACGEIKITD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 163 FGVAIQLGES--GLVAGGRV-----GTPHFMAPE--VVKREP--YGKPVDVWGCGVILFILLSGCLPF---YGTKERLFE 228
Cdd:cd14041  160 FGLSKIMDDDsyNSVDGMELtsqgaGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFYQCLYGRKPFghnQSQQDILQE 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 548961101 229 GIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14041  240 NTILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
SH3_MPP6 cd12038
Src Homology 3 domain of Membrane Protein, Palmitoylated 6 (or MAGUK p55 subfamily member 6); ...
610-668 2.49e-16

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: 73.94  E-value: 2.49e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 610 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKlENSKNGTAGLIPS 668
Cdd:cd12038    1 FVKCHFDYNPYNDNLIPCKEAGLKFSKGEILQIVNREDPNWWQAS-HVKEGGSAGLIPS 58
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
18-271 2.88e-16

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: 80.24  E-value: 2.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLStedLKREASICHMLKHPHIVELlETYSSDGMLYMVFEFMDGA 97
Cdd:cd14049   14 LGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMK---VLREVKVLAGLQHPNIVGY-HTAWMEHVQLMLYIQMQLC 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DL-------------CFEIVKRADAGFVYSEaVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLGGFG 164
Cdd:cd14049   90 ELslwdwivernkrpCEEEFKSAPYTPVDVD-VTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDIH--VRIGDFG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 165 VAIQL------------GESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSgclPFYGTKER--LFEGI 230
Cdd:cd14049  167 LACPDilqdgndsttmsRLNGLTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELFQ---PFGTEMERaeVLTQL 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 548961101 231 IKGKYKMN-PRQWSHISESAKDLVRRmlmlDPAERITVYEAL 271
Cdd:cd14049  244 RNGQIPKSlCKRWPVQAKYIKLLTST----EPSERPSASQLL 281
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
35-219 3.45e-16

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: 79.08  E-value: 3.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  35 GQQFAVKIVdvakftsspglstEDLKrEASICHM--LKHPHIVELLETYSSDGMLYMVFEFMDGADLcFEIVKradAGFV 112
Cdd:cd14059   16 GEEVAVKKV-------------RDEK-ETDIKHLrkLNHPNIIKFKGVCTQAPCYCILMEYCPYGQL-YEVLR---AGRE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 113 YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESGlVAGGRVGTPHFMAPEVVK 192
Cdd:cd14059   78 ITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDV---LKISDFGTSKELSEKS-TKMSFAGTVAWMAPEVIR 153
                        170       180
                 ....*....|....*....|....*..
gi 548961101 193 REPYGKPVDVWGCGVILFILLSGCLPF 219
Cdd:cd14059  154 NEPCSEKVDIWSFGVVLWELLTGEIPY 180
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
18-280 5.28e-16

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: 80.85  E-value: 5.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDvaKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd05600   19 VGQGGYGSVFLARKKDTGEICALKIMK--KKVLFKLNEVNHVLTERDILTTTNSPWLVKLLYAFQDPENVYLAMEYVPGG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLcfeivkRA---DAGfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVA-------- 166
Cdd:cd05600   97 DF------RTllnNSG-ILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDS---SGHIKLTDFGLAsgtlspkk 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 -----IQLGESGLVAGGR------------------------VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCL 217
Cdd:cd05600  167 iesmkIRLEEVKNTAFLEltakerrniyramrkedqnyansvVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFP 246
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548961101 218 PFYG-TKERLFEGIIKGKYKM------NPRQWSHISESAKDLVRRMLMlDPAERITVYEAL-NHPWLKERD 280
Cdd:cd05600  247 PFSGsTPNETWANLYHWKKTLqrpvytDPDLEFNLSDEAWDLITKLIT-DPQDRLQSPEQIkNHPFFKNID 316
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
18-278 6.61e-16

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: 80.09  E-value: 6.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVdvakftSSPGLS---TEDLKREASICHMLKHPHIVELLETYSSDGML------Y 88
Cdd:cd07878   23 VGSGAYGSVCSAYDTRLRQKVAVKKL------SRPFQSlihARRTYRELRLLKHMKHENVIGLLDVFTPATSIenfnevY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMdGADLCfEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVllASKENsAPVKLGGFGVAIQ 168
Cdd:cd07878   97 LVTNLM-GADLN-NIVKCQK----LSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNV--AVNED-CELRILDFGLARQ 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESglvAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-----ERLFEGI------------ 230
Cdd:cd07878  168 ADDE---MTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDyidqlKRIMEVVgtpspevlkkis 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 231 -------IKGKYKMNPRQWSHISESAK----DLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd07878  245 seharkyIQSLPHMPQQDLKKIFRGANplaiDLLEKMLVLDSDKRISASEALAHPYFSQ 303
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
12-269 9.22e-16

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: 79.52  E-value: 9.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVD----------VAKFTSSPGLSTED----------LKREASICHMLKH 71
Cdd:cd13977    2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRcnapenvelaLREFWALSSIQRQHpnviqleecvLQRDGLAQRMSHG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  72 PHI----VELLET---------YSSDGMLYMVFEFMDGADLCFEIVKRADagfvySEAVASHYMRQILEALRYCHDNNII 138
Cdd:cd13977   82 SSKsdlyLLLVETslkgercfdPRSACYLWFVMEFCDGGDMNEYLLSRRP-----DRQTNTSFMLQLSSALAFLHRNQIV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 139 HRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGRV-----------GTPHFMAPEVVKREpYGKPVDVWGCGV 207
Cdd:cd13977  157 HRDLKPDNILISHKRGEPILKVADFGLSKVCSGSGLNPEEPAnvnkhflssacGSDFYMAPEVWEGH-YTAKADIFALGI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 208 ILFILLSGCLPFYG-TKERLFEGIIKGKYKM---------NPRQWSHI--------SESAKDLVRRMLMLDPAERITVYE 269
Cdd:cd13977  236 IIWAMVERITFRDGeTKKELLGTYIQQGKEIvplgealleNPKLELQIplkkkksmNDDMKQLLRDMLAANPQERPDAFQ 315
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
12-276 9.38e-16

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: 80.18  E-value: 9.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAK-FTSSPGLST---EDLKREASICHMlkhpHIVELLETYSSDGML 87
Cdd:cd14224   67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKrFHRQAAEEIrilEHLKKQDKDNTM----NVIHMLESFTFRNHI 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDgADLcFEIVKRAD-AGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGFGva 166
Cdd:cd14224  143 CMTFELLS-MNL-YELIKKNKfQGF--SLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSG-IKVIDFG-- 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 iqlgeSGLVAGGRVGT----PHFMAPEVVKREPYGKPVDVWGCGVILFILLSG--------------CL----------- 217
Cdd:cd14224  216 -----SSCYEHQRIYTyiqsRFYRAPEVILGARYGMPIDMWSFGCILAELLTGyplfpgedegdqlaCMiellgmppqkl 290
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 218 ----------------PFYGTKERLFEGII--------KGKYKMNP--RQWSHISESAKD-----LVRRMLMLDPAERIT 266
Cdd:cd14224  291 letskraknfisskgyPRYCTVTTLPDGSVvlnggrsrRGKMRGPPgsKDWVTALKGCDDplfldFLKRCLEWDPAARMT 370
                        330
                 ....*....|
gi 548961101 267 VYEALNHPWL 276
Cdd:cd14224  371 PSQALRHPWL 380
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
18-282 1.16e-15

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: 79.79  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVK-IVDVakFTSSpgLSTEDLKREASICHMLKHPHI---VELLETYSSDGM--LYMVF 91
Cdd:cd07853    8 IGYGAFGVVWSVTDPRDGKRVALKkMPNV--FQNL--VSCKRVFRELKMLCFFKHDNVlsaLDILQPPHIDPFeeIYVVT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDgADLCFEIVKradagfvySEAVASHYMR----QILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVA- 166
Cdd:cd07853   84 ELMQ-SDLHKIIVS--------PQPLSSDHVKvflyQILRGLKYLHSAGILHRDIKPGNLLVNS---NCVLKICDFGLAr 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQLGESGLVAGGRVGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPF---------------YGTK--ERLF- 227
Cdd:cd07853  152 VEEPDESKHMTQEVVTQYYRAPEILMGSRhYTSAVDIWSVGCIFAELLGRRILFqaqspiqqldlitdlLGTPslEAMRs 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548961101 228 --EG----IIKGKYKMNPRQW-----SHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE-RDRY 282
Cdd:cd07853  232 acEGarahILRGPHKPPSLPVlytlsSQATHEAVHLLCRMLVFDPDKRISAADALAHPYLDEgRLRY 298
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
18-209 1.56e-15

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: 77.69  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKivDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMK--ELIRFDEE---TQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLcFEIVKRADAGFVYSEAVAshYMRQILEALRYCHDNNIIHRDVKPHCVLLasKENSAPVkLGGFGVA-IQLGESGLVA 176
Cdd:cd14221   76 TL-RGIIKSMDSHYPWSQRVS--FAKDIASGMAYLHSMNIIHRDLNSHNCLV--RENKSVV-VADFGLArLMVDEKTQPE 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 548961101 177 GGR-------------VGTPHFMAPEVVKREPYGKPVDVWGCGVIL 209
Cdd:cd14221  150 GLRslkkpdrkkrytvVGNPYWMAPEMINGRSYDEKVDVFSFGIVL 195
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
3-305 1.87e-15

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: 78.14  E-value: 1.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   3 DDDVLFEDVYElcevIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTE---DLKREASICHMLKHPHIVELLE 79
Cdd:cd06634   12 DPEKLFSDLRE----IGHGSFGAVYFARDVRNNEVVAIK-----KMSYSGKQSNEkwqDIIKEVKFLQKLRHPNTIEYRG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  80 TYSSDGMLYMVFEFMDGA--DLcFEIVKRAdagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAP 157
Cdd:cd06634   83 CYLREHTAWLVMEYCLGSasDL-LEVHKKP-----LQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTE---PGL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 158 VKLGGFGVAIQLGEsglvAGGRVGTPHFMAPEVV---KREPYGKPVDVWGCGVIlfillsgCLPFYGTKERLFE-GIIKG 233
Cdd:cd06634  154 VKLGDFGSASIMAP----ANSFVGTPYWMAPEVIlamDEGQYDGKVDVWSLGIT-------CIELAERKPPLFNmNAMSA 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 234 KYKMNPR-----QWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL-KERDRYAYKIHLPETVEQLRKFN--ARRKLK 305
Cdd:cd06634  223 LYHIAQNespalQSGHWSEYFRNFVDSCLQKIPQDRPTSDVLLKHRFLlRERPPTVIMDLIQRTKDAVRELDnlQYRKMK 302
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
18-237 2.11e-15

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: 78.30  E-value: 2.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglsTEDLKREASICHMLKHPHIVELL--ETYSSDGMLYMVFEFMD 95
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRP----LDVQMREFEVLKKLNHKNIVKLFaiEEELTTRHKVLVMELCP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLcFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPV-KLGGFGVAIQLGESGL 174
Cdd:cd13988   77 CGSL-YTVLEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVyKLTDFGAARELEDDEQ 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548961101 175 VAgGRVGTPHFMAPEVVKR--------EPYGKPVDVWGCGVILFILLSGCLPFygtkeRLFEGIIKGKYKM 237
Cdd:cd13988  156 FV-SLYGTEEYLHPDMYERavlrkdhqKKYGATVDLWSIGVTFYHAATGSLPF-----RPFEGPRRNKEVM 220
SH3_MPP4 cd12034
Src Homology 3 domain of Membrane Protein, Palmitoylated 4 (or MAGUK p55 subfamily member 4); ...
610-668 2.37e-15

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: 71.08  E-value: 2.37e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 610 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPS 668
Cdd:cd12034    1 YVRAMVDYWPQQDPSIPCADAGLPFRKGDILQIVDQNDSLWWQARKLSDLAACAGLIPS 59
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
18-290 2.60e-15

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: 76.91  E-value: 2.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETgQQFAVKIVdvakftSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd05112   12 IGSGQFGLVHLGYWLNK-DKVAIKTI------REGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 dlCFEIVKRADAGFVYSEAVASHYMrQILEALRYCHDNNIIHRDVKPHCVLLAskENSApVKLGGFGVA-IQLGESGLVA 176
Cdd:cd05112   85 --CLSDYLRTQRGLFSAETLLGMCL-DVCEGMAYLEEASVIHRDLAARNCLVG--ENQV-VKVSDFGMTrFVLDDQYTSS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 177 GGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYG-TKERLFEGIIKGKYKMNPRQWSHisesakdlvr 254
Cdd:cd05112  159 TGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENrSNSEVVEDINAGFRLYKPRLAST---------- 228
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 548961101 255 rmlmldpaeriTVYEALNHPWlKER--DRYAYKIHLPE 290
Cdd:cd05112  229 -----------HVYEIMNHCW-KERpeDRPSFSLLLRQ 254
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
18-280 2.78e-15

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: 78.41  E-value: 2.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDvAKFTSSpgLSTEDLKREASICHMLKHPHIVELLETYSS----DGM--LYMVF 91
Cdd:cd07879   23 VGSGAYGSVCSAIDKRTGEKVAIKKLS-RPFQSE--IFAKRAYRELTLLKHMQHENVIGLLDVFTSavsgDEFqdFYLVM 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDgADLcfeivkRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCvlLASKENsAPVKLGGFGVAIQLGE 171
Cdd:cd07879  100 PYMQ-TDL------QKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGN--LAVNED-CELKILDFGLARHADA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SglvAGGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGTK--------------------ERLFEGI 230
Cdd:cd07879  170 E---MTGYVVTRWYRAPEVIlNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDyldqltqilkvtgvpgpefvQKLEDKA 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 231 IKGKYKMNPRQ--------WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE-RD 280
Cdd:cd07879  247 AKSYIKSLPKYprkdfstlFPKASPQAVDLLEKMLELDVDKRLTATEALEHPYFDSfRD 305
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
16-273 2.90e-15

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: 76.94  E-value: 2.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVakfTSSPGLstEDLKREASICHMLK-HPHIVELLE---TYSSDGM--LYM 89
Cdd:cd14037    9 KYLAEGGFAHVYLVKTSNGGNRAALKRVYV---NDEHDL--NVCKREIEIMKRLSgHKNIVGYIDssaNRSGNGVyeVLL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLCFEIVKRADAGFVYSEAVasHYMRQILEALRYCH--DNNIIHRDVKPHCVLLASKENsapVKLGGFGVA- 166
Cdd:cd14037   84 LMEYCKGGGVIDLMNQRLQTGLTESEIL--KIFCDVCEAVAAMHylKPPLIHRDLKVENVLISDSGN---YKLCDFGSAt 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 -----------IQLGESGLVaggRVGTPHFMAPEVVkrEPY-GKPV----DVWGCGVILFILLSGCLPFygtKERLFEGI 230
Cdd:cd14037  159 tkilppqtkqgVTYVEEDIK---KYTTLQYRAPEMI--DLYrGKPIteksDIWALGCLLYKLCFYTTPF---EESGQLAI 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 548961101 231 IKGKYKM--NPRQwshiSESAKDLVRRMLMLDPAERITVYEALNH 273
Cdd:cd14037  231 LNGNFTFpdNSRY----SKRLHKLIRYMLEEDPEKRPNIYQVSYE 271
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
17-272 2.98e-15

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: 76.53  E-value: 2.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRetGQQFAVKIVDvaKFTSSpglstEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDG 96
Cdd:cd14068    1 LLGDGGFGSVYRAVYR--GEDVAVKIFN--KHTSF-----RLLRQELVVLSHLHHPSLVALLAAGTAPRMLVMELAPKGS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  97 ADLCFEivkRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAS-KENSAPV-KLGGFGVAIQLGESGL 174
Cdd:cd14068   72 LDALLQ---QDNASL--TRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTlYPNCAIIaKIADYGIAQYCCRMGI 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 175 VAGgrVGTPHFMAPEVVKRE-PYGKPVDVWGCGVILFILLSGclpfygtKERLFEGI----------IKGK-------YK 236
Cdd:cd14068  147 KTS--EGTPGFRAPEVARGNvIYNQQADVYSFGLLLYDILTC-------GERIVEGLkfpnefdelaIQGKlpdpvkeYG 217
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 548961101 237 MNPrqWSHISEsakdLVRRMLMLDPAER---ITVYEALN 272
Cdd:cd14068  218 CAP--WPGVEA----LIKDCLKENPQCRptsAQVFDILN 250
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
12-265 3.84e-15

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: 77.79  E-value: 3.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKR-EASICHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd05633    7 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERiMLSLVSTGDCPFIVCMTYAFHTPDKLCFI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLG 170
Cdd:cd05633   87 LDLMNGGDLHYHLSQHG----VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHVRISDLGLACDFS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAGgrVGTPHFMAPEVVKR-EPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESA 249
Cdd:cd05633  160 KKKPHAS--VGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDSFSPEL 237
                        250
                 ....*....|....*.
gi 548961101 250 KDLVRRMLMLDPAERI 265
Cdd:cd05633  238 KSLLEGLLQRDVSKRL 253
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
12-265 4.16e-15

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: 77.40  E-value: 4.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKR-EASICHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd14223    2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERiMLSLVSTGDCPFIVCMSYAFHTPDKLSFI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLG 170
Cdd:cd14223   82 LDLMNGGDLHYHLSQHG----VFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILL---DEFGHVRISDLGLACDFS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESGLVAGgrVGTPHFMAPEVVKRE-PYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESA 249
Cdd:cd14223  155 KKKPHAS--VGTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPEL 232
                        250
                 ....*....|....*.
gi 548961101 250 KDLVRRMLMLDPAERI 265
Cdd:cd14223  233 RSLLEGLLQRDVNRRL 248
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
62-215 4.55e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 78.11  E-value: 4.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  62 EASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAgfvYSEAVASHymRQILEALRYCHDNNIIHRD 141
Cdd:PHA03212 133 EAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKTDLYCYLAAKRNIA---ICDILAIE--RSVLRAIQYLHENRIIHRD 207
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548961101 142 VKPHCVLLaskENSAPVKLGGFGVA---IQLGESGLVagGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSG 215
Cdd:PHA03212 208 IKAENIFI---NHPGDVCLGDFGAAcfpVDINANKYY--GWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATC 279
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
8-276 4.81e-15

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: 77.36  E-value: 4.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYELCEVIGKGPFSVVRRCIN-RETGQQFAVKIV-DVAKFTSSPGLSTEDLKREASichmlKHPH----IVELLETY 81
Cdd:cd14215   10 LQERYEIVSTLGEGTFGRVVQCIDhRRGGARVALKIIkNVEKYKEAARLEINVLEKINE-----KDPEnknlCVQMFDWF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  82 SSDGMLYMVFEFMdgADLCFEIVKRADAgFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE-------- 153
Cdd:cd14215   85 DYHGHMCISFELL--GLSTFDFLKENNY-LPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSDyeltynle 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 154 --------NSAPVKLGGFGVAIQLGESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER 225
Cdd:cd14215  162 kkrdersvKSTAIRVVDFGSATFDHEHHSTI---VSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNR 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 226 ----LFEGII------------KGKYKMNPR-QWS-------HISESAK-----------------DLVRRMLMLDPAER 264
Cdd:cd14215  239 ehlaMMERILgpipsrmirktrKQKYFYHGRlDWDentsagrYVRENCKplrryltseaeehhqlfDLIESMLEYEPSKR 318
                        330
                 ....*....|..
gi 548961101 265 ITVYEALNHPWL 276
Cdd:cd14215  319 LTLAAALKHPFF 330
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
484-562 1.39e-14

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: 69.49  E-value: 1.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 484 LVQFQKNTDEPMGITLK--MNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKI 561
Cdd:cd00136    1 TVTLEKDPGGGLGFSIRggKDGGGGIFVSRVEPGGPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELLKSAGGEVTLTV 80

                 .
gi 548961101 562 V 562
Cdd:cd00136   81 R 81
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1-230 1.53e-14

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: 75.86  E-value: 1.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   1 MADDDvlFEDVYELceviGKGPFSVVRRCINRETGQQFAVKIVdvaKFTSSPGLSTEdLKREASICHMLKHPHIVELLET 80
Cdd:cd06649    2 LKDDD--FERISEL----GAGNGGVVTKVQHKPSGLIMARKLI---HLEIKPAIRNQ-IIRELQVLHECNSPYIVGFYGA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  81 YSSDGMLYMVFEFMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHD-NNIIHRDVKPHCVLLASKensAPVK 159
Cdd:cd06649   72 FYSDGEISICMEHMDGGSLD-QVLKEAKR---IPEEILGKVSIAVLRGLAYLREkHQIMHRDVKPSNILVNSR---GEIK 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548961101 160 LGGFGVAIQLGESglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGI 230
Cdd:cd06649  145 LCDFGVSGQLIDS--MANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKELEAI 213
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
18-219 1.61e-14

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: 74.95  E-value: 1.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAkftsspgLSTEDLKR---EASICHMLKHPHIVELLET-----YSSDGMLYM 89
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKSCRLE-------LSVKNKDRwchEIQIMKKLNHPNVVKACDVpeemnFLVNDVPLL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLcFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQL 169
Cdd:cd14039   74 AMEYCSGGDL-RKLLNKPENCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVHKIIDLGYAKDL 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 gESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF 219
Cdd:cd14039  153 -DQGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
61-276 1.64e-14

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: 76.28  E-value: 1.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  61 REASICHMLKHPHIVELLETYSSDGML------YMVFEFMDgADLCFEIVKRADagfvysEAVASHYMRQILEALRYCHD 134
Cdd:cd07874   65 RELVLMKCVNHKNIISLLNVFTPQKSLeefqdvYLVMELMD-ANLCQVIQMELD------HERMSYLLYQMLCGIKHLHS 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 135 NNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVIL----- 209
Cdd:cd07874  138 AGIIHRDLKPSNIVVKS---DCTLKILDFGLARTAGTSFMMT-PYVVTRYYRAPEVILGMGYKENVDIWSVGCIMgemvr 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 210 -FILLSG-----------------CLPFYGTKERLFEGIIKGKYK-------------MNPRQWSH---ISESAKDLVRR 255
Cdd:cd07874  214 hKILFPGrdyidqwnkvieqlgtpCPEFMKKLQPTVRNYVENRPKyagltfpklfpdsLFPADSEHnklKASQARDLLSK 293
                        250       260
                 ....*....|....*....|.
gi 548961101 256 MLMLDPAERITVYEALNHPWL 276
Cdd:cd07874  294 MLVIDPAKRISVDEALQHPYI 314
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
3-292 1.76e-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: 75.47  E-value: 1.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   3 DDDVLFEDVYElcevIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTE---DLKREASICHMLKHPHIVELLE 79
Cdd:cd06635   22 DPEKLFSDLRE----IGHGSFGAVYFARDVRTSEVVAIK-----KMSYSGKQSNEkwqDIIKEVKFLQRIKHPNSIEYKG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  80 TYSSDGMLYMVFEFMDGA--DLcFEIVKRAdagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAP 157
Cdd:cd06635   93 CYLREHTAWLVMEYCLGSasDL-LEVHKKP-----LQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTE---PGQ 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 158 VKLGGFGVAIQLGEsglvAGGRVGTPHFMAPEVV---KREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEGIIK 232
Cdd:cd06635  164 VKLADFGSASIASP----ANSFVGTPYWMAPEVIlamDEGQYDGKVDVWSLGITCIELAERKPPLFNMNamSALYHIAQN 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548961101 233 GKYKMNPRQWshiSESAKDLVRRMLMLDPAERITVYEALNHPW-LKERdryaykihlPETV 292
Cdd:cd06635  240 ESPTLQSNEW---SDYFRNFVDSCLQKIPQDRPTSEELLKHMFvLRER---------PETV 288
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
16-209 2.91e-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: 73.92  E-value: 2.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCI-NRETGQ--QFAVKIV--DVAKFTSSPglstEDLKREASICHMLKHPHIVELLETYSSDGMLyMV 90
Cdd:cd05040    1 EKLGDGSFGVVRRGEwTTPSGKviQVAVKCLksDVLSQPNAM----DDFLKEVNAMHSLDHPNLIRLYGVVLSSPLM-MV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLcFEIVKRADAGFVYSeaVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLG 170
Cdd:cd05040   76 TELAPLGSL-LDRLRKDQGHFLIS--TLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDK---VKIGDFGLMRALP 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 548961101 171 EsglvagGR---VGTPH------FMAPEVVKREPYGKPVDVWGCGVIL 209
Cdd:cd05040  150 Q------NEdhyVMQEHrkvpfaWCAPESLKTRKFSHASDVWMFGVTL 191
L27 pfam02828
L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.
400-450 3.00e-14

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


Pssm-ID: 460717  Cd Length: 52  Bit Score: 67.84  E-value: 3.00e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 548961101  400 VQRAKEVLEEISCYPE-NNDAKELKRILTQPHFMALLQTHDVVAHEVYSDEA 450
Cdd:pfam02828   1 VELVLELLEDLQPLSEaSEDLAELQKLLQSPHLQALLEAHDKVAQKVYEPPS 52
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
61-276 4.91e-14

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: 74.70  E-value: 4.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  61 REASICHMLKHPHIVELLETYSSDGML------YMVFEFMDgADLCFEIVKRADagfvysEAVASHYMRQILEALRYCHD 134
Cdd:cd07875   72 RELVLMKCVNHKNIIGLLNVFTPQKSLeefqdvYIVMELMD-ANLCQVIQMELD------HERMSYLLYQMLCGIKHLHS 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 135 NNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLS 214
Cdd:cd07875  145 AGIIHRDLKPSNIVVKS---DCTLKILDFGLARTAGTSFMMT-PYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIK 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 215 GCLPFYGTK---------ERLFEGIIKGKYKMNPRQWSHI------------------------------SESAKDLVRR 255
Cdd:cd07875  221 GGVLFPGTDhidqwnkviEQLGTPCPEFMKKLQPTVRTYVenrpkyagysfeklfpdvlfpadsehnklkASQARDLLSK 300
                        250       260
                 ....*....|....*....|.
gi 548961101 256 MLMLDPAERITVYEALNHPWL 276
Cdd:cd07875  301 MLVIDASKRISVDEALQHPYI 321
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
58-223 6.56e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 74.50  E-value: 6.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  58 DLKREASICHMLKHPHIVELLETYSSDGMLYMVFEfmdgadlcfeiVKRADAgFVYSEAVASHYMRQI-------LEALR 130
Cdd:PHA03207 132 TPGREIDILKTISHRAIINLIHAYRWKSTVCMVMP-----------KYKCDL-FTYVDRSGPLPLEQAitiqrrlLEALA 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 131 YCHDNNIIHRDVKPHCVLLASKENSApvkLGGFGVAIQLGESGLVAG--GRVGTPHFMAPEVVKREPYGKPVDVWGCGVI 208
Cdd:PHA03207 200 YLHGRGIIHRDVKTENIFLDEPENAV---LGDFGAACKLDAHPDTPQcyGWSGTLETNSPELLALDPYCAKTDIWSAGLV 276
                        170
                 ....*....|....*
gi 548961101 209 LFILLSGCLPFYGTK 223
Cdd:PHA03207 277 LFEMSVKNVTLFGKQ 291
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
18-273 9.11e-14

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: 72.34  E-value: 9.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSS----DGMLYMVFEF 93
Cdd:cd14033    9 IGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKG---ERQRFSEEVEMLKGLQHPNIVRFYDSWKStvrgHKCIILVTEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  94 MDGADLCFEIVKRADAGFvyseAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLASKenSAPVKLGGFGVAIQlgE 171
Cdd:cd14033   86 MTSGTLKTYLKRFREMKL----KLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITGP--TGSVKIGDLGLATL--K 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKrEPYGKPVDVWGCGVILFILLSGCLPFYGTKE--RLFEGIIKGkykMNPRQWSHIS-ES 248
Cdd:cd14033  158 RASFAKSVIGTPEFMAPEMYE-EKYDEAVDVYAFGMCILEMATSEYPYSECQNaaQIYRKVTSG---IKPDSFYKVKvPE 233
                        250       260
                 ....*....|....*....|....*
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNH 273
Cdd:cd14033  234 LKEIIEGCIRTDKDERFTIQDLLEH 258
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
481-563 1.25e-13

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: 67.02  E-value: 1.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   481 RVRLVQFQKNTdEPMGITLKMN--ELNHCIVARIMHGGMIHRQGtLHVGDEIREINGISVANQTVEQLQKMLREMRGSIT 558
Cdd:smart00228   1 EPRLVELEKGG-GGLGFSLVGGkdEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVT 78

                   ....*
gi 548961101   559 FKIVP 563
Cdd:smart00228  79 LTVLR 83
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
9-269 1.50e-13

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: 71.68  E-value: 1.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVyELCEVIGKGPFSVVRRCI-NRETGQQFAVKiVDVAKFTSSPGLsTEDLKREASICHMLKHPHIVELLETYSSDGMl 87
Cdd:cd05056    6 EDI-TLGRCIGEGQFGDVYQGVyMSPENEKIAVA-VKTCKNCTSPSV-REKFLQEAYIMRQFDHPHIVKLIGVITENPV- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAI 167
Cdd:cd05056   82 WIVMELAPLGELRSYLQVNKYS---LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDC---VKLGDFGLSR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGESGLVAGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYGTKERLFEGII-KGKY-----KMNP 239
Cdd:cd05056  156 YMEDESYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWeILMLGVKPFQGVKNNDVIGRIeNGERlpmppNCPP 235
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 240 RQWShisesakdLVRRMLMLDPAERITVYE 269
Cdd:cd05056  236 TLYS--------LMTKCWAYDPSKRPRFTE 257
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
62-214 1.58e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 72.99  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  62 EASICHMLKHPHIVELLETYSSDGMLYMVFEFMDgADLCFEIVKR------ADAGFVyseavashyMRQILEALRYCHDN 135
Cdd:PHA03209 107 EAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYS-SDLYTYLTKRsrplpiDQALII---------EKQILEGLRYLHAQ 176
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 136 NIIHRDVKPHCVLLASKENsapVKLGGFGVAiQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLS 214
Cdd:PHA03209 177 RIIHRDVKTENIFINDVDQ---VCIGDLGAA-QFPVVAPAFLGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEMLA 251
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
9-278 1.68e-13

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: 72.07  E-value: 1.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   9 EDVYELCEvIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSpgLSTEDLKR---EASICHMLKH-PHIVELLETYSSD 84
Cdd:cd06617    1 DDLEVIEE-LGRGAYGVVDKMRHVPTGTIMAVK-----RIRAT--VNSQEQKRllmDLDISMRSVDcPYTVTFYGALFRE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  85 GMLYMVFEFMDGA-DLCFEIVKraDAGFVYSEAVASHYMRQILEALRYCHDN-NIIHRDVKPHCVLLASKENsapVKLGG 162
Cdd:cd06617   73 GDVWICMEVMDTSlDKFYKKVY--DKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQ---VKLCD 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 163 FGVAIQLGESgLVAGGRVGTPHFMAPEVV--KREPYGKPV--DVWGCGVILFILLSGCLPF--YGTKERLFEGIIKGKYK 236
Cdd:cd06617  148 FGISGYLVDS-VAKTIDAGCKPYMAPERInpELNQKGYDVksDVWSLGITMIELATGRFPYdsWKTPFQQLKQVVEEPSP 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 548961101 237 MNPRQwsHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd06617  227 QLPAE--KFSPEFQDFVNKCLKKNYKERPNYPELLQHPFFEL 266
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
18-280 1.77e-13

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: 72.02  E-value: 1.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKivdvakfTSSPGLSTEDLKR------EASICHmlKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd06618   23 IGSGTCGQVYKMRHKKTGHVMAVK-------QMRRSGNKEENKRilmdldVVLKSH--DCPYIVKCYGYFITDSDVFICM 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDgadLCFEIVKRADAGFVySEAVASHYMRQILEALRYCHDN-NIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLG 170
Cdd:cd06618   94 ELMS---TCLDKLLKRIQGPI-PEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILLDESGN---VKLCDFGISGRLV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 171 ESglVAGGR-VGTPHFMAPEVVKREPYGK---PVDVWGCGVILFILLSGCLPFYGTKERlFEGIIK----GKYKMNPRQw 242
Cdd:cd06618  167 DS--KAKTRsAGCAAYMAPERIDPPDNPKydiRADVWSLGISLVELATGQFPYRNCKTE-FEVLTKilneEPPSLPPNE- 242
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 548961101 243 sHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERD 280
Cdd:cd06618  243 -GFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRYE 279
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
16-274 1.86e-13

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear 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. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The 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: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 71.67  E-value: 1.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIvdvakfTSSP--GLSTEDLKREASICHML--KHPHIVELLETYSSDGMLYMVF 91
Cdd:cd14051    6 EKIGSGEFGSVYKCINRLDGCVYAIKK------SKKPvaGSVDEQNALNEVYAHAVlgKHPHVVRYYSAWAEDDHMIIQN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEN--SAPVKLGGFG----- 164
Cdd:cd14051   80 EYCNGGSLADAISENEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNpvSSEEEEEDFEgeedn 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 165 -----VAIQLGESGLVAggRVGTPH-------FMAPEVVkREPYGK--PVDVWGCGVILFILLSG-CLPFYGTKerlFEG 229
Cdd:cd14051  160 pesneVTYKIGDLGHVT--SISNPQveegdcrFLANEIL-QENYSHlpKADIFALALTVYEAAGGgPLPKNGDE---WHE 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 548961101 230 IIKGKYKMNPrqwsHISESAKDLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd14051  234 IRQGNLPPLP----QCSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
18-258 2.46e-13

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: 71.20  E-value: 2.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRciNRETGQqFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVeLLETYSSDGMLYMVFEFMDGA 97
Cdd:cd14150    8 IGTGSFGTVFR--GKWHGD-VAVKILKVTEPTPE---QLQAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQWCEGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLC---------FEIVKRADAGfvyseavashymRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVA-I 167
Cdd:cd14150   81 SLYrhlhvtetrFDTMQLIDVA------------RQTAQGMDYLHAKNIIHRDLKSNNIFL---HEGLTVKIGDFGLAtV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 QLGESGlvaGGRVGTPH----FMAPEVVKRE---PYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPr 240
Cdd:cd14150  146 KTRWSG---SQQVEQPSgsilWMAPEVIRMQdtnPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQIIFMVGRGYLSP- 221
                        250
                 ....*....|....*...
gi 548961101 241 QWSHISESAKDLVRRMLM 258
Cdd:cd14150  222 DLSKLSSNCPKAMKRLLI 239
SH3_DLG-like cd11861
Src Homology 3 domain of Disks large homolog proteins; The DLG-like proteins are scaffolding ...
610-668 2.94e-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: 65.04  E-value: 2.94e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548961101 610 YVRAQFEYDPAKDDLIPCKeaGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTA--GLIPS 668
Cdd:cd11861    1 YVRALFDYDPSRDSGLPSQ--GLSFKFGDILHVTNASDDEWWQARRVTPNGEEEevGVIPS 59
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
62-210 3.24e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 73.00  E-value: 3.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  62 EASICHMLKHPHIVELLETYSSDGMLYMVFEFMDgADLCFEIVKRADA-GFVYSEAVAshymRQILEALRYCHDNNIIHR 140
Cdd:PHA03211 210 EARLLRRLSHPAVLALLDVRVVGGLTCLVLPKYR-SDLYTYLGARLRPlGLAQVTAVA----RQLLSAIDYIHGEGIIHR 284
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 141 DVKPHCVLLASKENsapVKLGGFGVA--IQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILF 210
Cdd:PHA03211 285 DIKTENVLVNGPED---ICLGDFGAAcfARGSWSTPFHYGIAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIF 353
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
18-209 3.42e-13

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: 71.00  E-value: 3.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKivDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMK--ELIRFDEE---AQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLcFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESGLVAG 177
Cdd:cd14154   76 TL-KDVLKDMARPLPWAQRV--RFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKT---VVVADFGLARLIVEERLPSG 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 548961101 178 GR--------------------VGTPHFMAPEVVKREPYGKPVDVWGCGVIL 209
Cdd:cd14154  150 NMspsetlrhlkspdrkkrytvVGNPYWMAPEMLNGRSYDEKVDIFSFGIVL 201
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
16-274 3.67e-13

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. 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 Wee1b 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: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 70.73  E-value: 3.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKivdvAKFTSSPGLSTEDLKREASICHML--KHPHIVELLETYSSDGMLYMVFEF 93
Cdd:cd14139    6 EKIGVGEFGSVYKCIKRLDGCVYAIK----RSMRPFAGSSNEQLALHEVYAHAVlgHHPHVVRYYSAWAEDDHMIIQNEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  94 MDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASK-----------ENSAPVKLGG 162
Cdd:cd14139   82 CNGGSLQDAISENTKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFICHKmqsssgvgeevSNEEDEFLSA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 163 fGVAIQLGESGLVAG-----GRVGTPHFMAPEVVKREPYGKP-VDVWGCGVILfILLSGCLPFyGTKERLFEGIIKGKYK 236
Cdd:cd14139  162 -NVVYKIGDLGHVTSinkpqVEEGDSRFLANEILQEDYRHLPkADIFALGLTV-ALAAGAEPL-PTNGAAWHHIRKGNFP 238
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 548961101 237 MNPRQwshISESAKDLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd14139  239 DVPQE---LPESFSSLLKNMIQPDPEQRPSATALARHT 273
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
17-272 3.84e-13

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: 71.00  E-value: 3.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQFAVKIVdvakftsspgLSTEDLKREA---SICHMLK---HPHIVELLE--TYSSDGMLY 88
Cdd:cd14036    7 VIAEGGFAFVYEAQDVGTGKEYALKRL----------LSNEEEKNKAiiqEINFMKKlsgHPNIVQFCSaaSIGKEESDQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLC----FEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLAskeNSAPVKLGG 162
Cdd:cd14036   77 GQAEYLLLTELCkgqlVDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIG---NQGQIKLCD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 163 FGVAIQL----------GESGLVAG--GRVGTPHFMAPEVV---KREPYGKPVDVWGCGVILFILLSGCLPFY-GTKERl 226
Cdd:cd14036  154 FGSATTEahypdyswsaQKRSLVEDeiTRNTTPMYRTPEMIdlySNYPIGEKQDIWALGCILYLLCFRKHPFEdGAKLR- 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 548961101 227 fegIIKGKYKM--NPRQWSHISesakDLVRRMLMLDPAERITVYEALN 272
Cdd:cd14036  233 ---IINAKYTIppNDTQYTVFH----DLIRSTLKVNPEERLSITEIVE 273
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
18-278 4.46e-13

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: 70.49  E-value: 4.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspgLSTEDLKREASICHMLKHPHIVELLETYSSDGM----LYMVFEF 93
Cdd:cd14032    9 LGRGSFKTVYKGLDTETWVEVAWCELQDRKLTK---VERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrcIVLVTEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  94 MDGADLCfEIVKRADagfVYSEAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLASKENSapVKLGGFGVAIQLGE 171
Cdd:cd14032   86 MTSGTLK-TYLKRFK---VMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPTGS--VKIGDLGLATLKRA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SglVAGGRVGTPHFMAPEVVKrEPYGKPVDVWGCGVILFILLSGCLPFYGTKE--RLFEGIIKGkykMNPRQWSHISE-S 248
Cdd:cd14032  160 S--FAKSVIGTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPYSECQNaaQIYRKVTCG---IKPASFEKVTDpE 233
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd14032  234 IKEIIGECICKNKEERYEIKDLLSHAFFAE 263
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
18-278 5.12e-13

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: 70.46  E-value: 5.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSS----DGMLYMVFEF 93
Cdd:cd14030   33 IGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKS---ERQRFKEEAGMLKGLQHPNIVRFYDSWEStvkgKKCIVLVTEL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  94 MDGADLCfEIVKRADagfVYSEAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLASKENSapVKLGGFGVAIQLGE 171
Cdd:cd14030  110 MTSGTLK-TYLKRFK---VMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTGS--VKIGDLGLATLKRA 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SglVAGGRVGTPHFMAPEVVKrEPYGKPVDVWGCGVILFILLSGCLPFYGTKE--RLFEGIIKGkykMNPRQWSHIS-ES 248
Cdd:cd14030  184 S--FAKSVIGTPEFMAPEMYE-EKYDESVDVYAFGMCMLEMATSEYPYSECQNaaQIYRRVTSG---VKPASFDKVAiPE 257
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 249 AKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:cd14030  258 VKEIIEGCIRQNKDERYAIKDLLNHAFFQE 287
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
13-274 5.30e-13

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: 70.07  E-value: 5.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  13 ELCEVIGKGPFSVVRRCINRetGQQFAVKIV-DVAKFTSSpglstedLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd05039    9 KLGELIGKGEFGDVMLGDYR--GQKVAVKCLkDDSTAAQA-------FLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRADAgfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSApvKLGGFGVAiQLGE 171
Cdd:cd05039   80 EYMAKGSLVDYLRSRGRA--VITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLV-SEDNVA--KVSDFGLA-KEAS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLvAGGRVgtP-HFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPF--YGTKErLFEGIIKGkYKMNPrqwshiSE 247
Cdd:cd05039  154 SNQ-DGGKL--PiKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYprIPLKD-VVPHVEKG-YRMEA------PE 222
                        250       260       270
                 ....*....|....*....|....*....|....
gi 548961101 248 SAKDLVRRMLM----LDPAERIT---VYEALNHP 274
Cdd:cd05039  223 GCPPEVYKVMKncweLDPAKRPTfkqLREKLEHI 256
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
12-276 5.68e-13

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: 71.04  E-value: 5.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRE-TGQQFAVKIV-DVAKFtsspglstedlkREASICHMLKHPHI-----------VELL 78
Cdd:cd14213   14 YEIVDTLGEGAFGKVVECIDHKmGGMHVAVKIVkNVDRY------------REAARSEIQVLEHLnttdpnstfrcVQML 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  79 ETYSSDGMLYMVFEFMDGADLCFeIVKRADAGFVYSEAVASHYmrQILEALRYCHDNNIIHRDVKPHCVLLASKE----- 153
Cdd:cd14213   82 EWFDHHGHVCIVFELLGLSTYDF-IKENSFLPFPIDHIRNMAY--QICKSVNFLHHNKLTHTDLKPENILFVQSDyvvky 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 154 -----------NSAPVKLGGFGVAIQLGE--SGLVAggrvgTPHFMAPEVVKREPYGKPVDVW--GCGVILFILLSGCLP 218
Cdd:cd14213  159 npkmkrdertlKNPDIKVVDFGSATYDDEhhSTLVS-----TRHYRAPEVILALGWSQPCDVWsiGCILIEYYLGFTVFQ 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 219 FYGTKERL--FEGII------------KGKYKMNPR-QWSHISESAK------------------------DLVRRMLML 259
Cdd:cd14213  234 THDSKEHLamMERILgplpkhmiqktrKRKYFHHDQlDWDEHSSAGRyvrrrckplkefmlsqdvdheqlfDLIQKMLEY 313
                        330
                 ....*....|....*..
gi 548961101 260 DPAERITVYEALNHPWL 276
Cdd:cd14213  314 DPAKRITLDEALKHPFF 330
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
18-161 6.65e-13

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: 66.70  E-value: 6.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDvakftSSPGLSTEDLKREASICHMLK--HPHIVELLETYSSDGMLYMVFEFMD 95
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKIGD-----DVNNEEGEDLESEMDILRRLKglELNIPKVLVTEDVDGPNILLMELVK 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548961101  96 GADLCFEIVKRADagfvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLG 161
Cdd:cd13968   76 GGTLIAYTQEEEL-----DEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
10-274 7.08e-13

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. 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 Wee1a 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: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 70.05  E-value: 7.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  10 DVYELcEVIGKGPFSVVRRCINRETGQQFAVKivdVAKFTSSPGLSTEDLKREASICHML-KHPHIVELLETYSSDGMLY 88
Cdd:cd14138    6 EFHEL-EKIGSGEFGSVFKCVKRLDGCIYAIK---RSKKPLAGSVDEQNALREVYAHAVLgQHSHVVRYYSAWAEDDHML 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE--NSAPVK-----LG 161
Cdd:cd14138   82 IQNEYCNGGSLADAISENYRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSipNAASEEgdedeWA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 162 GFGVAIQLGESGLVAggRVGTPH-------FMAPEVVKrEPYG--KPVDVWGCGVILfILLSGCLPFYGTKERLFEgIIK 232
Cdd:cd14138  162 SNKVIFKIGDLGHVT--RVSSPQveegdsrFLANEVLQ-ENYThlPKADIFALALTV-VCAAGAEPLPTNGDQWHE-IRQ 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 548961101 233 GKYkmnPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHP 274
Cdd:cd14138  237 GKL---PRIPQVLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
18-219 1.27e-12

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: 69.45  E-value: 1.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINREtgqqfavKIVDVAKFTSSPGLSTEDLKR----EASICHMLKHPHIVELLeTYSSDG-MLYMVFE 92
Cdd:cd14158   23 LGEGGFGVVFKGYIND-------KNVAVKKLAAMVDISTEDLTKqfeqEIQVMAKCQHENLVELL-GYSCDGpQLCLVYT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  93 FMDGADL-----CFE----IVKRADAGFVYSEAVASHYMrqilealrycHDNNIIHRDVKPHCVLLasKENSAPvKLGGF 163
Cdd:cd14158   95 YMPNGSLldrlaCLNdtppLSWHMRCKIAQGTANGINYL----------HENNHIHRDIKSANILL--DETFVP-KISDF 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101 164 GVAIQLGESGLVAGGR--VGTPHFMAPEVVKREPYGKpVDVWGCGVILFILLSGCLPF 219
Cdd:cd14158  162 GLARASEKFSQTIMTEriVGTTAYMAPEALRGEITPK-SDIFSFGVVLLEIITGLPPV 218
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
401-449 2.78e-12

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


Pssm-ID: 197794  Cd Length: 53  Bit Score: 62.14  E-value: 2.78e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 548961101   401 QRAKEVLEEISCYPE-NNDAKELKRILTQPHFMALLQTHDVVAHEVYSDE 449
Cdd:smart00569   1 QRLLELLEELQSLLSpSEDLQELRRLLQSPHLQALLKIHDKVAETELDPP 50
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
12-166 2.97e-12

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: 67.87  E-value: 2.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIvdVAKFTSSPGlstedLKREASICHMLK-HPHIVELLETYSSDGMLYMV 90
Cdd:cd14016    2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKI--EKKDSKHPQ-----LEYEAKVYKLLQgGPGIPRLYWFGQEGDYNVMV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMdGADL--CFEIVKR----------ADagfvyseavashymrQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPV 158
Cdd:cd14016   75 MDLL-GPSLedLFNKCGRkfslktvlmlAD---------------QMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNKV 138

                 ....*...
gi 548961101 159 KLGGFGVA 166
Cdd:cd14016  139 YLIDFGLA 146
pknD PRK13184
serine/threonine-protein kinase PknD;
12-289 3.06e-12

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 70.57  E-value: 3.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIV--DVAKFtssPGLSTEDLkREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIreDLSEN---PLLKKRFL-REAKIAADLIHPGIVPVYSICSDGDPVYY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADL---------CfEIVKRADAgfvYSEAVAShYMR---QILEALRYCHDNNIIHRDVKPHCVLL-------- 149
Cdd:PRK13184  80 TMPYIEGYTLksllksvwqK-ESLSKELA---EKTSVGA-FLSifhKICATIEYVHSKGVLHRDLKPDNILLglfgevvi 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 150 ----------ASKENSAPVKLGGFGVaiqLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF 219
Cdd:PRK13184 155 ldwgaaifkkLEEEDLLDIDVDERNI---CYSSMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPY 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 548961101 220 YGTKER--LFEGIIKGKYKMNPrqWSHISESAKDLVRRMLMLDPAERITVYEALN---HPWLKERDRYAYKIHLP 289
Cdd:PRK13184 232 RRKKGRkiSYRDVILSPIEVAP--YREIPPFLSQIAMKALAVDPAERYSSVQELKqdlEPHLQGSPEWTVKATLM 304
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
32-221 3.24e-12

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: 68.07  E-value: 3.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  32 RETGQQFAVKIVDVAKFTSSPGLSTEDL----------------KREASICHMLKHPHIVELLEtyssdgmlymvfefMD 95
Cdd:cd14067   14 RYQGQPVAVKRFHIKKCKKRTDGSADTMlkhlraadamknfsefRQEASMLHSLQHPCIVYLIG--------------IS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLCF--EIVKRADAGFVYSE-AVASHYM-----------RQILEALRYCHDNNIIHRDVKPHCVLLASKE--NSAPVK 159
Cdd:cd14067   80 IHPLCFalELAPLGSLNTVLEEnHKGSSFMplghmltfkiaYQIAAGLAYLHKKNIIFCDLKSDNILVWSLDvqEHINIK 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 160 LGGFGVAIQLGESGLVagGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 221
Cdd:cd14067  160 LSDYGISRQSFHEGAL--GVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRPSLG 219
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
12-295 3.33e-12

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 69.68  E-value: 3.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTedlkREASICHMLKHPHIVELLETYSSDGM----- 86
Cdd:PTZ00036  68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIK-----KVLQDPQYKN----RELLIMKNLNHINIIFLKDYYYTECFkknek 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 ---LYMVFEFMDgadlcfEIVKRADAGFVYSEA-----VASHYMRQILEALRYCHDNNIIHRDVKPHCVLLasKENSAPV 158
Cdd:PTZ00036 139 nifLNVVMEFIP------QTVHKYMKHYARNNHalplfLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLI--DPNTHTL 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 159 KLGGFGVAiqlgeSGLVAGGR----VGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYG------------ 221
Cdd:PTZ00036 211 KLCDFGSA-----KNLLAGQRsvsyICSRFYRAPELmLGATNYTTHIDLWSLGCIIAEMILGYPIFSGqssvdqlvriiq 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 222 -----TKERLFEgiikgkykMNPrQWSHIS------------------ESAKDLVRRMLMLDPAERITVYEALNHPWLKE 278
Cdd:PTZ00036 286 vlgtpTEDQLKE--------MNP-NYADIKfpdvkpkdlkkvfpkgtpDDAINFISQFLKYEPLKRLNPIEALADPFFDD 356
                        330
                 ....*....|....*...
gi 548961101 279 -RDRYaykIHLPETVEQL 295
Cdd:PTZ00036 357 lRDPC---IKLPKYIDKL 371
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
18-225 4.05e-12

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: 67.42  E-value: 4.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCinRETGQqFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVeLLETYSSDGMLYMVFEFMDGA 97
Cdd:cd14062    1 IGSGSFGTVYKG--RWHGD-VAVKKLNVTDPTPS---QLQAFKNEVAVLRKTRHVNIL-LFMGYMTKPQLAIVTQWCEGS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLC---------FEIVKRADAGfvyseavashymRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAI- 167
Cdd:cd14062   74 SLYkhlhvletkFEMLQLIDIA------------RQTAQGMDYLHAKNIIHRDLKSNNIFLHE---DLTVKIGDFGLATv 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 168 -QLGESGLVAGGRVGTPHFMAPEVVK---REPYGKPVDVWGCGVILFILLSGCLPFYGTKER 225
Cdd:cd14062  139 kTRWSGSQQFEQPTGSILWMAPEVIRmqdENPYSFQSDVYAFGIVLYELLTGQLPYSHINNR 200
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
18-276 4.31e-12

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: 67.34  E-value: 4.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglsteDLKREASichmLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd13995   12 IPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPS------DVEIQAC----FRHENIAELYGALLWEETVHLFMEAGEGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 dlcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskenSAPVKLGGFGVAIQLGESGLVAG 177
Cdd:cd13995   82 ----SVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFM----STKAVLVDFGLSVQMTEDVYVPK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 178 GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNPrQWSHISESAKDLVRRM 256
Cdd:cd13995  154 DLRGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRsAYPSYLYIIHKQAP-PLEDIAQDCSPAMREL 232
                        250       260
                 ....*....|....*....|....
gi 548961101 257 ----LMLDPAERITVYEALNHPWL 276
Cdd:cd13995  233 leaaLERNPNHRSSAAELLKHEAL 256
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
18-220 5.82e-12

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: 67.41  E-value: 5.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRC----INRETGQQFAVKIVDvakfTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGM--LYMVF 91
Cdd:cd05038   12 LGEGHFGSVELCrydpLGDNTGEQVAVKSLQ----PSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPGRrsLRLIM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGAdlCFEIVKRADAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVA--IQL 169
Cdd:cd05038   88 EYLPSG--SLRDYLQRHRDQIDLKRLLL-FASQICKGMEYLGSQRYIHRDLAARNILVESEDL---VKISDFGLAkvLPE 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 548961101 170 GESGLVAGGRVGTPHF-MAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY 220
Cdd:cd05038  162 DKEYYYVKEPGESPIFwYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQ 213
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
4-264 7.11e-12

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. 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. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 67.33  E-value: 7.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   4 DDVLFEDVyelcevIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglSTEDLKREASI-CHMLKHPHIVELLETYS 82
Cdd:cd05089    2 EDIKFEDV------IGEGNFGQVIKAMIKKDGLKMNAAIKMLKEFASEN--DHRDFAGELEVlCKLGHHPNIINLLGACE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  83 SDGMLYMVFEFMDGADLcFEIVKRA-----DAGFVYSEAVASHYM-RQILE-------ALRYCHDNNIIHRDVKPHCVLL 149
Cdd:cd05089   74 NRGYLYIAIEYAPYGNL-LDFLRKSrvletDPAFAKEHGTASTLTsQQLLQfasdvakGMQYLSEKQFIHRDLAARNVLV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 150 AskENSApVKLGGFGVAiqLGESGLVAG--GRVGTpHFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYG-TKER 225
Cdd:cd05089  153 G--ENLV-SKIADFGLS--RGEEVYVKKtmGRLPV-RWMAIESLNYSVYTTKSDVWSFGVLLWEIVSlGGTPYCGmTCAE 226
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 548961101 226 LFEGIIKGKYKMNPRqwsHISESAKDLVRRMLMLDPAER 264
Cdd:cd05089  227 LYEKLPQGYRMEKPR---NCDDEVYELMRQCWRDRPYER 262
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
12-237 9.63e-12

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: 9.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETgQQFAVKIVdvakfTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd05148    8 FTLERKLGSGYFGEVWEGLWKNR-VRVAIKIL-----KSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIIT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskENSApVKLGGFGVAIQLGE 171
Cdd:cd05148   82 ELMEKGSL--LAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVG--EDLV-CKVADFGLARLIKE 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101 172 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYG-TKERLFEGIIKGkYKM 237
Cdd:cd05148  157 DVYLSSDKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGmNNHEVYDQITAG-YRM 223
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
18-266 1.03e-11

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily 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: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 66.60  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVV-----RRCINRETGQQFAVKIVDVAkftSSPGLSTEDLKrEASICHMLKHPHIVELLETYSSDGMLYMVFE 92
Cdd:cd05032   14 LGQGSFGMVyeglaKGVVKGEPETRVAIKTVNEN---ASMRERIEFLN-EASVMKEFNCHHVVRLLGVVSTGQPTLVVME 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  93 FMDGADLCFEIVKR---ADAGFVYSEAVASHYMR---QILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVA 166
Cdd:cd05032   90 LMAKGDLKSYLRSRrpeAENNPGLGPPTLQKFIQmaaEIADGMAYLAAKKFVHRDLAARNCMVAEDLT---VKIGDFGMT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 167 IQLGESGLV--AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYG-TKERLFEGIIKGKYkMN---- 238
Cdd:cd05032  167 RDIYETDYYrkGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWeMATLAEQPYQGlSNEEVLKFVIDGGH-LDlpen 245
                        250       260
                 ....*....|....*....|....*....
gi 548961101 239 -PRQWshisesaKDLVRRMLMLDPAERIT 266
Cdd:cd05032  246 cPDKL-------LELMRMCWQYNPKMRPT 267
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
13-273 1.12e-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: 66.16  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  13 ELCEVIGKGPFSVVRrcINRETGQQFAVKIVdvakftsSPGLSTEDLKREASICHMLKHPHIVELLETYSSD-GMLYMVF 91
Cdd:cd05082    9 KLLQTIGKGEFGDVM--LGDYRGNKVAVKCI-------KNDATAQAFLAEASVMTQLRHSNLVQLLGVIVEEkGGLYIVT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRADAgfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSApvKLGGFGVAIQLGE 171
Cdd:cd05082   80 EYMAKGSLVDYLRSRGRS--VLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLV-SEDNVA--KVSDFGLTKEASS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGLVAGGRVgtpHFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYGTKERLFEGIIKGKYKMNPRqwSHISESAK 250
Cdd:cd05082  155 TQDTGKLPV---KWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYPRIPLKDVVPRVEKGYKMDAP--DGCPPAVY 229
                        250       260
                 ....*....|....*....|....*.
gi 548961101 251 DLVRRMLMLDPAERIT---VYEALNH 273
Cdd:cd05082  230 DVMKNCWHLDAAMRPSflqLREQLEH 255
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
18-247 1.82e-11

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: 65.55  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRetGQqfavkiVDVA-KFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMdg 96
Cdd:cd05059   12 LGSGQFGVVHLGKWR--GK------IDVAiKMIKEGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYM-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  97 ADLCFEIVKRADAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKP-HCvlLASKENSapVKLGGFGVAIQLGESGLV 175
Cdd:cd05059   82 ANGCLLNYLRERRGKFQTEQLLE-MCKDVCEAMEYLESNGFIHRDLAArNC--LVGEQNV--VKVSDFGLARYVLDDEYT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 176 AGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYGTK-----ERLFEGIIKGKYKMNPRQ------- 241
Cdd:cd05059  157 SSVGTKFPvKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSnsevvEHISQGYRLYRPHLAPTEvytimys 236

                 ....*..
gi 548961101 242 -WSHISE 247
Cdd:cd05059  237 cWHEKPE 243
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
610-668 1.97e-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: 1.97e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101   610 YVRAQFEYDPAKDDlipckeaGIRFRVGDIIQIISKDDHNWWQGKLensKNGTAGLIPS 668
Cdd:smart00326   4 QVRALYDYTAQDPD-------ELSFKKGDIITVLEKSDDGWWKGRL---GRGKEGLFPS 52
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
56-276 2.02e-11

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: 65.81  E-value: 2.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  56 TEDLKREASicHM--LKHPHIVELLETY-SSDGMLYMVFEFMDgADLCFEIVKRAD--------AGFVYSEAVASHYMRQ 124
Cdd:cd14011   46 LELLKRGVK--QLtrLRHPRILTVQHPLeESRESLAFATEPVF-ASLANVLGERDNmpspppelQDYKLYDVEIKYGLLQ 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 125 ILEALRYCHDN-NIIHRDVKPHCVLLaskeNSAPV-KLGGFGVAIQL----GESGLVAGGRVGTPH-------FMAPEVV 191
Cdd:cd14011  123 ISEALSFLHNDvKLVHGNICPESVVI----NSNGEwKLAGFDFCISSeqatDQFPYFREYDPNLPPlaqpnlnYLAPEYI 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 192 KREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEgiikgkYKMNPRQWSHISESA--------KDLVRRMLMLDPAE 263
Cdd:cd14011  199 LSKTCDPASDMFSLGVLIYAIYNKGKPLFDCVNNLLS------YKKNSNQLRQLSLSLlekvpeelRDHVKTLLNVTPEV 272
                        250
                 ....*....|...
gi 548961101 264 RITVYEALNHPWL 276
Cdd:cd14011  273 RPDAEQLSKIPFF 285
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
18-227 2.12e-11

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: 65.35  E-value: 2.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQQFAVKivDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMK--ELIRCDEE---TQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLcfEIVKRADAGFVYSEAVAshYMRQILEALRYCHDNNIIHRDVKPHCVLlaskensapVKLGGFGVAIQLGESGLVAG 177
Cdd:cd14222   76 TL--KDFLRADDPFPWQQKVS--FAKGIASGMAYLHSMSIIHRDLNSHNCL---------IKLDKTVVVADFGLSRLIVE 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 178 GR--------------------------VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLS------GCLPF---YGT 222
Cdd:cd14222  143 EKkkpppdkpttkkrtlrkndrkkrytvVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEIIGqvyadpDCLPRtldFGL 222

                 ....*
gi 548961101 223 KERLF 227
Cdd:cd14222  223 NVRLF 227
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
13-266 2.16e-11

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR 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: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 65.97  E-value: 2.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  13 ELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLS-TEDLKREASI-CHMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd05055   38 SFGKTLGAGAFGKVVEATAYGLSKSDAVMKVAVKMLKPTAHSSeREALMSELKImSHLGNHENIVNLLGACTIGGPILVI 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLCFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQ-L 169
Cdd:cd05055  118 TEYCCYGDLLNFLRRKRESFLTLEDLL--SFSYQVAKGMAFLASKNCIHRDLAARNVLLT---HGKIVKICDFGLARDiM 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYGTK-ERLFEGIIKGKYKMNprQWSHIS 246
Cdd:cd05055  193 NDSNYVVKGNARLPvKWMAPESIFNCVYTFESDVWSYGILLWEIFSlGSNPYPGMPvDSKFYKLIKEGYRMA--QPEHAP 270
                        250       260
                 ....*....|....*....|
gi 548961101 247 ESAKDLVRRMLMLDPAERIT 266
Cdd:cd05055  271 AEIYDIMKTCWDADPLKRPT 290
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
12-247 2.46e-11

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: 64.97  E-value: 2.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKivdvakfTSSPGLSTEDLKREASIC-HMLKHPHIVELLETYSSDGMLYMV 90
Cdd:cd14017    2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMK-------VESKSQPKQVLKMEVAVLkKLQGKPHFCRLIGCGRTERYNYIV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMdGADLcFEIVKRADAGFvYSEAVASHYMRQILEALRYCHDNNIIHRDVKP-HCVLLASKENSAPVKLGGFGVAIQ- 168
Cdd:cd14017   75 MTLL-GPNL-AELRRSQPRGK-FSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPsNFAIGRGPSDERTVYILDFGLARQy 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLV------AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMN---- 238
Cdd:cd14017  152 TNKDGEVerpprnAAGFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKLKDKEEVGKMKEKIDHEellk 231
                        250
                 ....*....|....*
gi 548961101 239 --PRQ----WSHISE 247
Cdd:cd14017  232 glPKEffqiLKHIRS 246
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
13-221 3.35e-11

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: 65.09  E-value: 3.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  13 ELCEVIGKGPFSVVRR-----CINRETGQQFAVKIVdvaKFTSSPGLStEDLKREASICHMLKHPHIVELLETYSSDGML 87
Cdd:cd05048    8 RFLEELGEGAFGKVYKgellgPSSEESAISVAIKTL---KENASPKTQ-QDFRREAELMSDLQHPNIVCLLGVCTKEQPQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMDGADLCFEIVKRA---DAGFVYSEAVASHYMR---------QILEALRYCHDNNIIHRDVKPHCVLLASKENs 155
Cdd:cd05048   84 CMLFEYMAHGDLHEFLVRHSphsDVGVSSDDDGTASSLDqsdflhiaiQIAAGMEYLSSHHYVHRDLAARNCLVGDGLT- 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 548961101 156 apVKLGGFGVA--IQLGESGLVAGGRVGTPHFMAPEVVKrepYGK---PVDVWGCGVILFILLS-GCLPFYG 221
Cdd:cd05048  163 --VKISDFGLSrdIYSSDYYRVQSKSLLPVRWMPPEAIL---YGKfttESDVWSFGVVLWEIFSyGLQPYYG 229
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
16-264 5.16e-11

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. 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. Fer kinase is a member of the Fes subfamily of proteins which 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. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 63.87  E-value: 5.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETgqqfavkiVDVAKFTSSPGLSTEdLK----REASICHMLKHPHIVELLETYSSDGMLYMVF 91
Cdd:cd05085    2 ELLGKGNFGEVYKGTLKDK--------TPVAVKTCKEDLPQE-LKikflSEARILKQYDHPNIVKLIGVCTQRQPIYIVM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCFEIVKRADagfvysEAVASHYMRQILEA---LRYCHDNNIIHRDVKPHCVLLAskENSApVKLGGFGVAIQ 168
Cdd:cd05085   73 ELVPGGDFLSFLRKKKD------ELKTKQLVKFSLDAaagMAYLESKNCIHRDLAARNCLVG--ENNA-LKISDFGMSRQ 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 169 LGESGLVAGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYG-TKERLFEGIIKGkYKMNPRQwsHI 245
Cdd:cd05085  144 EDDGVYSSSGLKQIPiKWTAPEALNYGRYSSESDVWSFGILLWETFSlGVCPYPGmTNQQAREQVEKG-YRMSAPQ--RC 220
                        250
                 ....*....|....*....
gi 548961101 246 SESAKDLVRRMLMLDPAER 264
Cdd:cd05085  221 PEDIYKIMQRCWDYNPENR 239
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
4-239 6.01e-11

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: 64.17  E-value: 6.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   4 DDVLFEDVYELCEVIGKGPFSVVRRC---INRETGQQFAVKIVDVAKFTSSpglSTEDLKREASICHMLKHPHIVELLET 80
Cdd:cd05074    3 DVLIQEQQFTLGRMLGKGEFGSVREAqlkSEDGSFQKVAVKMLKADIFSSS---DIEEFLREAACMKEFDHPNVIKLIGV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  81 Y---SSDGML---YMVFEFMDGADL-CFEIVKR-ADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASK 152
Cdd:cd05074   80 SlrsRAKGRLpipMVILPFMKHGDLhTFLLMSRiGEEPFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNEN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 153 ENsapVKLGGFGVAIQLGESGLVAGGRVGT-P-HFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYGTKE-RLFE 228
Cdd:cd05074  160 MT---VCVADFGLSKKIYSGDYYRQGCASKlPvKWLALESLADNVYTTHSDVWAFGVTMWeIMTRGQTPYAGVENsEIYN 236
                        250
                 ....*....|.
gi 548961101 229 GIIKGKYKMNP 239
Cdd:cd05074  237 YLIKGNRLKQP 247
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
13-266 7.05e-11

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: 63.91  E-value: 7.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  13 ELCEVIGKGPFSVVRRciNRETGQqFAVKIVDVAkftsspGLSTEDL---KREASICHMLKHPHIVELLETYSSDGMLYM 89
Cdd:cd14063    3 EIKEVIGKGRFGRVHR--GRWHGD-VAIKLLNID------YLNEEQLeafKEEVAAYKNTRHDNLVLFMGACMDPPHLAI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLcFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVkLGGFGVaiqL 169
Cdd:cd14063   74 VTSLCKGRTL-YSLIHERKEKFDFNKTV--QIAQQICQGMGYLHAKGIIHKDLKSKNIFL---ENGRVV-ITDFGL---F 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAGGR----VGTPH----FMAPEVVK----------REPYGKPVDVWGCGVILFILLSGCLPFygtKERLFEGII 231
Cdd:cd14063  144 SLSGLLQPGRredtLVIPNgwlcYLAPEIIRalspdldfeeSLPFTKASDVYAFGTVWYELLAGRWPF---KEQPAESII 220
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 548961101 232 --KGKYKMNPRQWSHISESAKDLVRRMLMLDPAERIT 266
Cdd:cd14063  221 wqVGCGKKQSLSQLDIGREVKDILMQCWAYDPEKRPT 257
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
57-240 7.25e-11

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: 63.83  E-value: 7.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  57 EDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLC-FEIVKRADA-------GFVYSEAVASHYMR---QI 125
Cdd:cd05092   52 QDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMRHGDLNrFLRSHGPDAkildggeGQAPGQLTLGQMLQiasQI 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 126 LEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQLGESGLV-AGGRVGTP-HFMAPEVVKREPYGKPVDVW 203
Cdd:cd05092  132 ASGMVYLASLHFVHRDLATRNCLVG---QGLVVKIGDFGMSRDIYSTDYYrVGGRTMLPiRWMPPESILYRKFTTESDIW 208
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 548961101 204 GCGVILF-ILLSGCLPFYG-TKERLFEGIIKGKYKMNPR 240
Cdd:cd05092  209 SFGVVLWeIFTYGKQPWYQlSNTEAIECITQGRELERPR 247
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
16-264 9.37e-11

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie 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: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 63.52  E-value: 9.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglSTEDLKREASI-CHMLKHPHIVELLETYSSDGMLYMVFEFM 94
Cdd:cd05047    1 DVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKD--DHRDFAGELEVlCKLGHHPNIINLLGACEHRGYLYLAIEYA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  95 DGADLcFEIVKRA-----DAGFVYSEAVAS--------HYMRQILEALRYCHDNNIIHRDVKPHCVLLAskENSApVKLG 161
Cdd:cd05047   79 PHGNL-LDFLRKSrvletDPAFAIANSTAStlssqqllHFAADVARGMDYLSQKQFIHRDLAARNILVG--ENYV-AKIA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 162 GFGVAiqLGESGLVAG--GRVGTpHFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYG-TKERLFEGIIKGKYKM 237
Cdd:cd05047  155 DFGLS--RGQEVYVKKtmGRLPV-RWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGmTCAELYEKLPQGYRLE 231
                        250       260
                 ....*....|....*....|....*..
gi 548961101 238 NPRqwsHISESAKDLVRRMLMLDPAER 264
Cdd:cd05047  232 KPL---NCDDEVYDLMRQCWREKPYER 255
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
18-266 1.02e-10

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 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 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 Jak1 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: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 63.79  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCI----NRETGQQFAVKIVDvakfTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDG--MLYMVF 91
Cdd:cd05079   12 LGEGHFGKVELCRydpeGDNTGEQVAVKSLK----PESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGgnGIKLIM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  92 EFMDGADLCfEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGV--AIQL 169
Cdd:cd05079   88 EFLPSGSLK-EYLPRNKNKINLKQQL--KYAVQICKGMDYLGSRQYVHRDLAARNVLV---ESEHQVKIGDFGLtkAIET 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 170 GESGLVAGGRVGTPHF-MAPEVVKREPYGKPVDVWGCGVILFILLSGCL--------------PFYG--TKERLFEGIIK 232
Cdd:cd05079  162 DKEYYTVKDDLDSPVFwYAPECLIQSKFYIASDVWSFGVTLYELLTYCDsesspmtlflkmigPTHGqmTVTRLVRVLEE 241
                        250       260       270
                 ....*....|....*....|....*....|....
gi 548961101 233 GKYKMNPrqwSHISESAKDLVRRMLMLDPAERIT 266
Cdd:cd05079  242 GKRLPRP---PNCPEEVYQLMRKCWEFQPSKRTT 272
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
54-273 1.09e-10

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: 63.21  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  54 LSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLcFEIVKRADAGFVysEAVASHYM-RQILEALRYC 132
Cdd:cd05052   44 MEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNL-LDYLRECNREEL--NAVVLLYMaTQIASAMEYL 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 133 HDNNIIHRDVKPHCVLLAskENSApVKLGGFGVAIQLGESGLVAGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILF- 210
Cdd:cd05052  121 EKKNFIHRDLAARNCLVG--ENHL-VKVADFGLSRLMTGDTYTAHAGAKFPiKWTAPESLAYNKFSIKSDVWAFGVLLWe 197
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548961101 211 ILLSGCLPFYGTKERLFEGIIKGKYKMNprQWSHISESAKDLVRRMLMLDPAERIT---VYEALNH 273
Cdd:cd05052  198 IATYGMSPYPGIDLSQVYELLEKGYRME--RPEGCPPKVYELMRACWQWNPSDRPSfaeIHQALET 261
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
45-214 1.17e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 65.10  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  45 VAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDgadlcFEIVKradagFVYSEAV------- 117
Cdd:PHA03210 196 IAKRVKAGSRAAIQLENEILALGRLNHENILKIEEILRSEANTYMITQKYD-----FDLYS-----FMYDEAFdwkdrpl 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 118 ---ASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLgESGLVAG--GRVGTPHFMAPEVVK 192
Cdd:PHA03210 266 lkqTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFL---NCDGKIVLGDFGTAMPF-EKEREAFdyGWVGTVATNSPEILA 341
                        170       180
                 ....*....|....*....|..
gi 548961101 193 REPYGKPVDVWGCGVILFILLS 214
Cdd:PHA03210 342 GDGYCEITDIWSCGLILLDMLS 363
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
17-221 1.19e-10

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: 63.20  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRCINRETGQQfaVKI---VDVAKFTSSPGLSTEDLkREASICHMLKHPHIVELLETYSSDGMLyMVFEF 93
Cdd:cd05057   14 VLGSGAFGTVYKGVWIPEGEK--VKIpvaIKVLREETGPKANEEIL-DEAYVMASVDHPHLVRLLGICLSSQVQ-LITQL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  94 MDGADLcFEIVkRADAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLG--- 170
Cdd:cd05057   90 MPLGCL-LDYV-RNHRDNIGSQLLLN-WCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNH---VKITDFGLAKLLDvde 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 548961101 171 ESGLVAGGRVgtP-HFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYG 221
Cdd:cd05057  164 KEYHAEGGKV--PiKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYEG 214
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
610-668 1.20e-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: 57.47  E-value: 1.20e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 610 YVRAQFEYDPAKDDLIPckeagirFRVGDIIQIISKDDHNWWQGKLENSKngtAGLIPS 668
Cdd:cd00174    1 YARALYDYEAQDDDELS-------FKKGDIITVLEKDDDGWWEGELNGGR---EGLFPA 49
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
45-240 1.26e-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: 63.14  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  45 VAKFTSSPG-LSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLcFEIVKRADAGFVYSEAVAShYMR 123
Cdd:cd05072   34 VAVKTLKPGtMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGSL-LDFLKSDEGGKVLLPKLID-FSA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 124 QILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQLGESGLVAGGRVGTP-HFMAPEVVKREPYGKPVDV 202
Cdd:cd05072  112 QIAEGMAYIERKNYIHRDLRAANVLVS---ESLMCKIADFGLARVIEDNEYTAREGAKFPiKWTAPEAINFGSFTIKSDV 188
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 548961101 203 WGCGVILF-ILLSGCLPFYGTKERLFEGIIKGKYKMnPR 240
Cdd:cd05072  189 WSFGILLYeIVTYGKIPYPGMSNSDVMSALQRGYRM-PR 226
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
342-395 1.29e-10

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


Pssm-ID: 197794  Cd Length: 53  Bit Score: 57.52  E-value: 1.29e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 548961101   342 SQVLDSLEEIHALTDCSEkDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNP 395
Cdd:smart00569   1 QRLLELLEELQSLLSPSE-DLQELRRLLQSPHLQALLKIHDKVAETELDPPLPE 53
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
3-225 1.34e-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: 63.16  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   3 DDDVLFEDVYELCEVIGKGPFSVVRRciNRETGQqFAVKIVDVakfTSSPGLSTEDLKREASICHMLKHPHIVeLLETYS 82
Cdd:cd14151    1 DDWEIPDGQITVGQRIGSGSFGTVYK--GKWHGD-VAVKMLNV---TAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  83 SDGMLYMVFEFMDGADLC---------FEIVKRADAGfvyseavashymRQILEALRYCHDNNIIHRDVKPHCVLLaskE 153
Cdd:cd14151   74 TKPQLAIVTQWCEGSSLYhhlhiietkFEMIKLIDIA------------RQTAQGMDYLHAKSIIHRDLKSNNIFL---H 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548961101 154 NSAPVKLGGFGVA-IQLGESGLVAGGRV-GTPHFMAPEVVK---REPYGKPVDVWGCGVILFILLSGCLPFYGTKER 225
Cdd:cd14151  139 EDLTVKIGDFGLAtVKSRWSGSHQFEQLsGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNR 215
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
57-214 1.72e-10

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated 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. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK 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: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 63.19  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  57 EDLKREASICHMLKHPHIVELLE-TYSSDGMLYMVFEFMdGADLCFEIVKRADAGF-VYSEAVASHYMRQILEALRYCH- 133
Cdd:cd14001   50 ERLKEEAKILKSLNHPNIVGFRAfTKSEDGSLCLAMEYG-GKSLNDLIEERYEAGLgPFPAATILKVALSIARALEYLHn 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 134 DNNIIHRDVKPHCVLLASKENSapVKLGGFGVAIQLGESGLVA----GGRVGTPHFMAPEVVKRepyGKPV----DVWGC 205
Cdd:cd14001  129 EKKILHGDIKSGNVLIKGDFES--VKLCDFGVSLPLTENLEVDsdpkAQYVGTEPWKAKEALEE---GGVItdkaDIFAY 203

                 ....*....
gi 548961101 206 GVILFILLS 214
Cdd:cd14001  204 GLVLWEMMT 212
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
18-225 2.78e-10

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: 62.36  E-value: 2.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRcinretGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVeLLETYSSDGMLYMVFEFMDGA 97
Cdd:cd14149   20 IGSGSFGTVYK------GKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 DLcFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVA-IQLGESGLVA 176
Cdd:cd14149   93 SL-YKHLHVQETKFQMFQLI--DIARQTAQGMDYLHAKNIIHRDMKSNNIFL---HEGLTVKIGDFGLAtVKSRWSGSQQ 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 548961101 177 GGR-VGTPHFMAPEVVKRE---PYGKPVDVWGCGVILFILLSGCLPFYGTKER 225
Cdd:cd14149  167 VEQpTGSILWMAPEVIRMQdnnPFSFQSDVYSYGIVLYELMTGELPYSHINNR 219
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
16-219 3.08e-10

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: 63.11  E-value: 3.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSteDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 95
Cdd:cd05626    7 KTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVA--HVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAI-------- 167
Cdd:cd05626   85 GGDMMSLLIRME----VFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILI---DLDGHIKLTDFGLCTgfrwthns 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 168 ---QLGE----------------SGLVAGGR--------------------VGTPHFMAPEVVKREPYGKPVDVWGCGVI 208
Cdd:cd05626  158 kyyQKGShirqdsmepsdlwddvSNCRCGDRlktleqratkqhqrclahslVGTPNYIAPEVLLRKGYTQLCDWWSVGVI 237
                        250
                 ....*....|.
gi 548961101 209 LFILLSGCLPF 219
Cdd:cd05626  238 LFEMLVGQPPF 248
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
59-280 4.15e-10

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: 62.76  E-value: 4.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  59 LKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNII 138
Cdd:cd05625   48 VKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMG----VFPEDLARFYIAELTCAVESVHKMGFI 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 139 HRDVKPHCVLLaskENSAPVKLGGFGVAI-----------QLGE----------------SGLVAGGR------------ 179
Cdd:cd05625  124 HRDIKPDNILI---DRDGHIKLTDFGLCTgfrwthdskyyQSGDhlrqdsmdfsnewgdpENCRCGDRlkplerraarqh 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 180 --------VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISESAK 250
Cdd:cd05625  201 qrclahslVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAqTPLETQMKVINWQTSLHIPPQAKLSPEAS 280
                        250       260       270
                 ....*....|....*....|....*....|...
gi 548961101 251 DLVRRmLMLDPAERI---TVYEALNHPWLKERD 280
Cdd:cd05625  281 DLIIK-LCRGPEDRLgknGADEIKAHPFFKTID 312
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
483-561 4.90e-10

PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. 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 Dlg5-like 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: 467248 [Multi-domain]  Cd Length: 82  Bit Score: 56.57  E-value: 4.90e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 483 RLVQFQKnTDEPMGITLKMNELNHCIVARIMHGGMIHRQGtLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKI 561
Cdd:cd06767    4 RHVSIEK-GSEPLGISIVSGENGGIFVSSVTEGSLAHQAG-LEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLV 80
PDZ6_MUPP1-like cd06670
PDZ domain 6 of multi-PDZ-domain protein 1 (MUPP1) and related domains; PDZ (PSD-95 ...
489-551 5.34e-10

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: 56.88  E-value: 5.34e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548961101 489 KNTDEPMGITLKMN-ELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLR 551
Cdd:cd06670   10 VKGNSSLGITVSADkDGNGCIVKSIIHGGAVSRDGRISVGDFIVSINNESLRNVTNAQARAILR 73
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
41-273 5.50e-10

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: 60.76  E-value: 5.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  41 KIVDVAKFTSSPG-LSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFM-DGADLCFeivKRADAGFVYSEAVA 118
Cdd:cd05034   18 GTTKVAVKTLKPGtMSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMsKGSLLDY---LRTGEGRALRLPQL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 119 SHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskENSApVKLGGFGVAIQLGESGLVAggRVGT--P-HFMAPEVVKrep 195
Cdd:cd05034   95 IDMAAQIASGMAYLESRNYIHRDLAARNILVG--ENNV-CKVADFGLARLIEDDEYTA--REGAkfPiKWTAPEAAL--- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 196 YGK---PVDVWGCGVILF-ILLSGCLPFYG-TKERLFEGIIKGkYKMnPRQwSHISESAKDLVRRMLMLDPAERITvYEA 270
Cdd:cd05034  167 YGRftiKSDVWSFGILLYeIVTYGRVPYPGmTNREVLEQVERG-YRM-PKP-PGCPDELYDIMLQCWKKEPEERPT-FEY 242

                 ...
gi 548961101 271 LNH 273
Cdd:cd05034  243 LQS 245
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
19-271 5.66e-10

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. 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 MLTK 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: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 60.74  E-value: 5.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  19 GKGPFSVVRRCINRETGQQFAVKIVDvakftsspglsteDLKREASICHMLKHPHIVE------------LLETYSSDGM 86
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVKKLL-------------KIEKEAEILSVLSHRNIIQfygaileapnygIVTEYASYGS 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  87 LYmvfEFMDGADlcfeivkradagfvySEAV-ASHYM---RQILEALRYCHDN---NIIHRDVKPHCVLLASkenSAPVK 159
Cdd:cd14060   69 LF---DYLNSNE---------------SEEMdMDQIMtwaTDIAKGMHYLHMEapvKVIHRDLKSRNVVIAA---DGVLK 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 160 LGGFGVAIQLGESGLVAggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGtkerlFEG-------IIK 232
Cdd:cd14060  128 ICDFGASRFHSHTTHMS--LVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKG-----LEGlqvawlvVEK 200
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 548961101 233 GKYKMNPrqwSHISESAKDLVRRMLMLDPAERITVYEAL 271
Cdd:cd14060  201 NERPTIP---SSCPRSFAELMRRCWEADVKERPSFKQII 236
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
57-233 6.13e-10

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: 60.98  E-value: 6.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  57 EDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLcFEIVKRADAGFvyseAVASHYMRQILEALRYCHDNN 136
Cdd:cd14027   36 EALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNL-MHVLKKVSVPL----SVKGRIILEIIEGMAYLHGKG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 137 IIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGESGL-------------VAGGRVGTPHFMAPEVVkREPYGKPV--- 200
Cdd:cd14027  111 VIHKDLKPENILV---DNDFHIKIADLGLASFKMWSKLtkeehneqrevdgTAKKNAGTLYYMAPEHL-NDVNAKPTeks 186
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 548961101 201 DVWGCGVILFILLSGCLPFYG--TKERLFEGIIKG 233
Cdd:cd14027  187 DVYSFAIVLWAIFANKEPYENaiNEDQIIMCIKSG 221
SH3_DLG3 cd12029
Src Homology 3 domain of Disks Large homolog 3; DLG3, also called synapse-associated protein ...
607-673 6.36e-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: 55.86  E-value: 6.36e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 607 RQIYVRAQFEYDPAKDDLIPCKeaGIRFRVGDIIQIISKDDHNWWQGKL--ENSKNGTAGLIPSPELQE 673
Cdd:cd12029    1 RSLYVRALFDYDRTRDSCLPSQ--GLSFSYGDILHVINASDDEWWQARLvtPHGESEQIGVIPSKKRVE 67
SH3_DLG1 cd12031
Src Homology 3 domain of Disks Large homolog 1; DLG1, also called synapse-associated protein ...
607-668 6.60e-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: 55.85  E-value: 6.60e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548961101 607 RQIYVRAQFEYDPAKDDLIPCKeaGIRFRVGDIIQIISKDDHNWWQGK--LENSKNGTAGLIPS 668
Cdd:cd12031    1 RSLYVRALFDYDKTKDSGLPSQ--GLNFKFGDILHVVNASDDEWWQARqvTADGESEEIGVIPS 62
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
16-216 6.62e-10

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: 61.15  E-value: 6.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRC------------INRETGQQ--FAVKIV--DVAKftsspgLSTEDLKREASICHMLKHPHIVELLE 79
Cdd:cd05097   11 EKLGEGQFGEVHLCeaeglaeflgegAPEFDGQPvlVAVKMLraDVTK------TARNDFLKEIKIMSRLKNPNIIRLLG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  80 TYSSDGMLYMVFEFMDGADLCFEIVKRA-DAGFVYSEAVAS-------HYMRQILEALRYCHDNNIIHRDVKPHCVLLas 151
Cdd:cd05097   85 VCVSDDPLCMITEYMENGDLNQFLSQREiESTFTHANNIPSvsianllYMAVQIASGMKYLASLNFVHRDLATRNCLV-- 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 548961101 152 kENSAPVKLGGFGVAIQL--GESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGC 216
Cdd:cd05097  163 -GNHYTIKIADFGMSRNLysGDYYRIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLC 228
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
16-238 7.26e-10

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 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 tyr kinase catalytic 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 Tyk2 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: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 61.07  E-value: 7.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPF-SVVRRCI---NRETGQQFAVKIVdvaKFTSSPGLsTEDLKREASICHMLKHPHIVELLETYSSDG--MLYM 89
Cdd:cd05080   10 RDLGEGHFgKVSLYCYdptNDGTGEMVAVKAL---KADCGPQH-RSGWKQEIDILKTLYHENIVKYKGCCSEQGgkSLQL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLCFEIVKRAdagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQL 169
Cdd:cd05080   86 IMEYVPLGSLRDYLPKHS-----IGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLL---DNDRLVKIGDFGLAKAV 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548961101 170 GESGLVAggRVG----TPHF-MAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMN 238
Cdd:cd05080  158 PEGHEYY--RVRedgdSPVFwYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQSPPTKFLEMIGIAQGQMT 229
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
13-219 9.04e-10

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: 61.16  E-value: 9.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  13 ELCEVIGKGPFSVVRRCINR--ETGQQFAVKIVDVAKftsspgLSTEDLKR---EASICHMLKHPHIVELLETYSSDGML 87
Cdd:cd08216    1 ELLYEIGKCFKGGGVVHLAKhkPTNTLVAVKKINLES------DSKEDLKFlqqEILTSRQLQHPNILPYVTSFVVDNDL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  88 YMVFEFMD-GAdlCFEIVKRAdagFVY--SEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFG 164
Cdd:cd08216   75 YVVTPLMAyGS--CRDLLKTH---FPEglPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISG---DGKVVLSGLR 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101 165 VAIQLGESglvaGGRVGTPHF-----------MAPEVVKR--EPYGKPVDVWGCGVILFILLSGCLPF 219
Cdd:cd08216  147 YAYSMVKH----GKRQRVVHDfpksseknlpwLSPEVLQQnlLGYNEKSDIYSVGITACELANGVVPF 210
SH3_DLG2 cd12032
Src Homology 3 domain of Disks Large homolog 2; DLG2, also called postsynaptic density-93 ...
607-668 9.83e-10

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: 55.47  E-value: 9.83e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 548961101 607 RQIYVRAQFEYDPAKDDLIPCKeaGIRFRVGDIIQIISKDDHNWWQGK--LENSKNGTAGLIPS 668
Cdd:cd12032    4 RSLYVRAMFDYEKSKDSGLPSQ--GLSFRYGDILHVINASDDEWWQARrvTPDGDSEEMGVIPS 65
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
4-223 1.11e-09

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: 60.34  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   4 DDVLFEDVyELceviGKGPFSVVRRCINRETGQQFAVKIvDVAKFTSSPGLsTEDLKREASICHMLKHPHIVELLETYSS 83
Cdd:cd05115    3 DNLLIDEV-EL----GSGNFGCVKKGVYKMRKKQIDVAI-KVLKQGNEKAV-RDEMMREAQIMHQLDNPYIVRMIGVCEA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLyMVFEFMDGADLCFEIVKRADAgfVYSEAVAsHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGF 163
Cdd:cd05115   76 EALM-LVMEMASGGPLNKFLSGKKDE--ITVSNVV-ELMHQVSMGMKYLEEKNFVHRDLAARNVLLV---NQHYAKISDF 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548961101 164 GVAIQLGESGLVAGGRVGTP---HFMAPEVVKREPYGKPVDVWGCGVILFILLSgclpfYGTK 223
Cdd:cd05115  149 GLSKALGADDSYYKARSAGKwplKWYAPECINFRKFSSRSDVWSYGVTMWEAFS-----YGQK 206
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
18-223 1.12e-09

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: 60.06  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRETGQqfavKIVDVAKFTSSPGLS---TEDLKREASICHMLKHPHIVELLETYSSDGMLyMVFEFM 94
Cdd:cd05060    3 LGHGNFGSVRKGVYLMKSG----KEVEVAVKTLKQEHEkagKKEFLREASVMAQLDHPCIVRLIGVCKGEPLM-LVMELA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  95 DGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV--AIQLGES 172
Cdd:cd05060   78 PLGPLLKYLKKRRE----IPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQ---AKISDFGMsrALGAGSD 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 548961101 173 GLVA--GGRvgTP-HFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYGTK 223
Cdd:cd05060  151 YYRAttAGR--WPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGEMK 203
gmk PRK14738
guanylate kinase; Provisional
736-898 1.15e-09

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 58.97  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 736 LVLLGAHGVGRRHIKNTLITKHPDrFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLE 815
Cdd:PRK14738  16 VVISGPSGVGKDAVLARMRERKLP-FHFVVTATTRPKRPGEIDGVDYHFVTPEEFREMISQNELLEWAEVYGNYYGVPKA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 816 TIRKIHEQGLIAILDVEPQALKVLRtaEFAPFVVFI-AAPtitPGLNE------------DESL-QRLQKESDVLQRTYA 881
Cdd:PRK14738  95 PVRQALASGRDVIVKVDVQGAASIK--RLVPEAVFIfLAP---PSMDEltrrlelrrtesPEELeRRLATAPLELEQLPE 169
                        170
                 ....*....|....*....
gi 548961101 882 hyFDLTIIN--NEIDETIR 898
Cdd:PRK14738 170 --FDYVVVNpeDRLDEAVA 186
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
16-272 1.63e-09

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: 59.38  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQQFAVKivdVAKFTSSPGLSTEDLKrEASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 95
Cdd:cd05041    1 EKIGRGNFGDVYRGVLKPDNTEVAVK---TCRETLPPDLKRKFLQ-EARILKQYDHPNIVKLIGVCVQKQPIMIVMELVP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLCFEIVKRADAGFVyseavaSHYMRQILEA---LRYCHDNNIIHRDVKP-HCvlLASKENSapVKLGGFGVAIQlGE 171
Cdd:cd05041   77 GGSLLTFLRKKGARLTV------KQLLQMCLDAaagMEYLESKNCIHRDLAArNC--LVGENNV--LKISDFGMSRE-EE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 172 SGL--VAGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYG-TKERLFEGIIKGkYKMNPrqwshiS 246
Cdd:cd05041  146 DGEytVSDGLKQIPiKWTAPEALNYGRYTSESDVWSFGILLWeIFSLGATPYPGmSNQQTREQIESG-YRMPA------P 218
                        250       260       270
                 ....*....|....*....|....*....|
gi 548961101 247 ESAKDLVRRMLML----DPAERITVYEALN 272
Cdd:cd05041  219 ELCPEAVYRLMLQcwayDPENRPSFSEIYN 248
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
16-220 1.65e-09

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: 60.14  E-value: 1.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRciNRETGQQFAVKIVDVAKFTSspglstedLKREASICH--MLKHPHIVELL---ETYSSDGM-LYM 89
Cdd:cd13998    1 EVIGKGRFGEVWK--ASLKNEPVAVKIFSSRDKQS--------WFREKEIYRtpMLKHENILQFIaadERDTALRTeLWL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLCfEIVKRADAGFVYSEAVASHYMRqileALRYCHDN---------NIIHRDVKPHCVLLasKENSAPVkL 160
Cdd:cd13998   71 VTAFHPNGSL*-DYLSLHTIDWVSLCRLALSVAR----GLAHLHSEipgctqgkpAIAHRDLKSKNILV--KNDGTCC-I 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 161 GGFGVAIQL----GESGLVAGGRVGTPHFMAPEV------VKREPYGKPVDVWGCGVILFILLSGC-----------LPF 219
Cdd:cd13998  143 ADFGLAVRLspstGEEDNANNGQVGTKRYMAPEVlegainLRDFESFKRVDIYAMGLVLWEMASRCtdlfgiveeykPPF 222

                 .
gi 548961101 220 Y 220
Cdd:cd13998  223 Y 223
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
18-240 1.66e-09

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: 60.05  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVV--RRCINRETGQQFAVKIVDVAKFTSSPGlsTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMD 95
Cdd:cd05093   13 LGEGAFGKVflAECYNLCPEQDKILVAVKTLKDASDNA--RKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  96 GADLC-FEIVKRADAGFV--------YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskENSApVKLGGFGVA 166
Cdd:cd05093   91 HGDLNkFLRAHGPDAVLMaegnrpaeLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVG--ENLL-VKIGDFGMS 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101 167 IQLGESGLV-AGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYG-TKERLFEGIIKGKYKMNPR 240
Cdd:cd05093  168 RDVYSTDYYrVGGHTMLPiRWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQlSNNEVIECITQGRVLQRPR 245
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
14-264 2.28e-09

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET 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: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 59.59  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  14 LCEVIGKGPF-SVVRRCINRETGQ----QFAVKIVdvaKFTSSPgLSTEDLKREASICHMLKHPHIVELLETYSSDGMLY 88
Cdd:cd05045    4 LGKTLGEGEFgKVVKATAFRLKGRagytTVAVKML---KENASS-SELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  89 MVFEFMDGADL--CFEIVKRADAGFVYSEAVASH------------------YMRQILEALRYCHDNNIIHRDVKPHCVL 148
Cdd:cd05045   80 LIVEYAKYGSLrsFLRESRKVGPSYLGSDGNRNSsyldnpderaltmgdlisFAWQISRGMQYLAEMKLVHRDLAARNVL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 149 LASKENsapVKLGGFGVAIQLGESGLV---AGGRVGTpHFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYG-TK 223
Cdd:cd05045  160 VAEGRK---MKISDFGLSRDVYEEDSYvkrSKGRIPV-KWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGiAP 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 548961101 224 ERLFEgIIKGKYKMNprQWSHISESAKDLVRRMLMLDPAER 264
Cdd:cd05045  236 ERLFN-LLKTGYRME--RPENCSEEMYNLMLTCWKQEPDKR 273
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
45-266 2.39e-09

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: 58.77  E-value: 2.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  45 VAKFTSSPG-LSTEDLKREASICHMLKHPHIVELLETYSSDGmLYMVFEFMDGADLcFEIVKRADAGFVYSEAVAShYMR 123
Cdd:cd14203   22 VAIKTLKPGtMSPEAFLEEAQIMKKLRHDKLVQLYAVVSEEP-IYIVTEFMSKGSL-LDFLKDGEGKYLKLPQLVD-MAA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 124 QILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQLGESGLVAGGRVGTP-HFMAPEVVKREPYGKPVDV 202
Cdd:cd14203   99 QIASGMAYIERMNYIHRDLRAANILVG---DNLVCKIADFGLARLIEDNEYTARQGAKFPiKWTAPEAALYGRFTIKSDV 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548961101 203 WGCGVILFILLS-GCLPFYGTKER-LFEGIIKGkYKMNPRQWShiSESAKDLVRRMLMLDPAERIT 266
Cdd:cd14203  176 WSFGILLTELVTkGRVPYPGMNNReVLEQVERG-YRMPCPPGC--PESLHELMCQCWRKDPEERPT 238
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
16-216 2.50e-09

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes 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 region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 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: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 59.65  E-value: 2.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVV--RRCINRETgqqfAVKIVDVAKFTSspgLSTEdlKREASICHMlKHPHIVELL----ETYSSDGMLYM 89
Cdd:cd14053    1 EIKARGRFGAVwkAQYLNRLV----AVKIFPLQEKQS---WLTE--REIYSLPGM-KHENILQFIgaekHGESLEAEYWL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLCfEIVKradaGFVYSEAVASHYMRQILEALRYCHDN----------NIIHRDVKPHCVLLasKENSAPVk 159
Cdd:cd14053   71 ITEFHERGSLC-DYLK----GNVISWNELCKIAESMARGLAYLHEDipatngghkpSIAHRDFKSKNVLL--KSDLTAC- 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548961101 160 LGGFGVAIQLgESGLVAG---GRVGTPHFMAPEVV------KREPYgKPVDVWGCGVILFILLSGC 216
Cdd:cd14053  143 IADFGLALKF-EPGKSCGdthGQVGTRRYMAPEVLegainfTRDAF-LRIDMYAMGLVLWELLSRC 206
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
16-214 2.54e-09

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: 59.26  E-value: 2.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRC----INRETGQQFAVKivdvaKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGM--LYM 89
Cdd:cd14205   10 QQLGKGNFGSVEMCrydpLQDNTGEVVAVK-----KLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRrnLRL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  90 VFEFMDGADLCFEIVKRADAgFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQL 169
Cdd:cd14205   85 IMEYLPYGSLRDYLQKHKER-IDHIKLL--QYTSQICKGMEYLGTKRYIHRDLATRNILV---ENENRVKIGDFGLTKVL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 548961101 170 ------------GESglvaggrvgtPHF-MAPEVVKREPYGKPVDVWGCGVILFILLS 214
Cdd:cd14205  159 pqdkeyykvkepGES----------PIFwYAPESLTESKFSVASDVWSFGVVLYELFT 206
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
8-216 2.87e-09

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 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 DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 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: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 59.56  E-value: 2.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101   8 FEDVYeLCEVIGKGPFSVVRRCINRETGQQF--AVKIV--DVAKFTSSpglsteDLKREASICHMLKHPHIVELLETYSS 83
Cdd:cd05096   18 FGEVH-LCEVVNPQDLPTLQFPFNVRKGRPLlvAVKILrpDANKNARN------DFLKEVKILSRLKDPNIIRLLGVCVD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  84 DGMLYMVFEFMDGADL---------------CFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVL 148
Cdd:cd05096   91 EDPLCMITEYMENGDLnqflsshhlddkeenGNDAVPPAHCLPAISYSSLLHVALQIASGMKYLSSLNFVHRDLATRNCL 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 149 LASKENsapVKLGGFGVAIQL--GESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGC 216
Cdd:cd05096  171 VGENLT---IKIADFGMSRNLyaGDYYRIQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEILMLC 237
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
18-244 2.95e-09

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: 59.59  E-value: 2.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRC----INRETGQQFAVKIVDVAKFTSSPGlSTEDLKREASICHML-KHPHIVELLETYSSDGMLYMVFE 92
Cdd:cd05099   20 LGEGCFGQVVRAeaygIDKSRPDQTVTVAVKMLKDNATDK-DLADLISEMELMKLIgKHKNIINLLGVCTQEGPLYVIVE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  93 FMD--------------GADLCFEIVKRADAGFVYSEAVASHYmrQILEALRYCHDNNIIHRDVKPHCVLLASKEnsaPV 158
Cdd:cd05099   99 YAAkgnlreflrarrppGPDYTFDITKVPEEQLSFKDLVSCAY--QVARGMEYLESRRCIHRDLAARNVLVTEDN---VM 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 159 KLGGFGVAI---QLGESGLVAGGRVGTpHFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYGTK-ERLFEGIIKG 233
Cdd:cd05099  174 KIADFGLARgvhDIDYYKKTSNGRLPV-KWMAPEALFDRVYTHQSDVWSFGILMWeIFTLGGSPYPGIPvEELFKLLREG 252
                        250
                 ....*....|.
gi 548961101 234 KYKMNPRQWSH 244
Cdd:cd05099  253 HRMDKPSNCTH 263
L27 pfam02828
L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.
341-388 3.76e-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: 53.20  E-value: 3.76e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 548961101  341 VSQVLDSLEEIHALTDCSEkDLDFLHSVFQDQHLHTLLDLYDKINTKS 388
Cdd:pfam02828   1 VELVLELLEDLQPLSEASE-DLAELQKLLQSPHLQALLEAHDKVAQKV 47
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
18-219 4.28e-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: 58.33  E-value: 4.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVVRRCINRetgQQFAVKIvdvaKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGA 97
Cdd:cd05114   12 LGSGLFGVVRLGKWR---AQYKVAI----KAIREGAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  98 dlCFEIVKRADAGfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGESGLVAG 177
Cdd:cd05114   85 --CLLNYLRQRRG-KLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVND---TGVVKVSDFGMTRYVLDDQYTSS 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 548961101 178 GRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPF 219
Cdd:cd05114  159 SGAKFPvKWSPPEVFNYSKFSSKSDVWSFGVLMWeVFTEGKMPF 202
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
17-216 4.56e-09

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: 58.75  E-value: 4.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  17 VIGKGPFSVVRRC----INRETGQQFAVKivdvaKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGM--LYMV 90
Cdd:cd05081   11 QLGKGNFGSVELCrydpLGDNTGALVAVK-----QLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGRrsLRLV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  91 FEFMDGADLcFEIVKRADAGFVYSEAVAshYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVA--IQ 168
Cdd:cd05081   86 MEYLPSGCL-RDFLQRHRARLDASRLLL--YSSQICKGMEYLGSRRCVHRDLAARNILVESEAH---VKIADFGLAklLP 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 548961101 169 LGESGLVAGGRVGTPHF-MAPEVVKREPYGKPVDVWGCGVILFILLSGC 216
Cdd:cd05081  160 LDKDYYVVREPGQSPIFwYAPESLSDNIFSRQSDVWSFGVVLYELFTYC 208
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
125-264 4.79e-09

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty 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: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 58.27  E-value: 4.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 125 ILEALRYCHDNNIIHRDVKPHCVLLaSKENSApvKLGGFGVAIqlgESGLVAGGRVGTPHFMAPEVVKREpYGKPVDVWG 204
Cdd:cd13975  111 VVEGIRFLHSQGLVHRDIKLKNVLL-DKKNRA--KITDLGFCK---PEAMMSGSIVGTPIHMAPELFSGK-YDNSVDVYA 183
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548961101 205 CGVILFILLSGC--LPF----YGTKERLFEGIIKGkykMNPRQWSHISESAKDLVRRMLMLDPAER 264
Cdd:cd13975  184 FGILFWYLCAGHvkLPEafeqCASKDHLWNNVRKG---VRPERLPVFDEECWNLMEACWSGDPSQR 246
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
16-214 4.90e-09

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: 58.15  E-value: 4.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  16 EVIGKGPFSVVRRCINRETGQqfavKIVDVAKFTSSPGLSTE---DLKREASICHMLKHPHIVELLETYSSDGMLYMVFE 92
Cdd:cd05033   10 KVIGGGEFGEVCSGSLKLPGK----KEIDVAIKTLKSGYSDKqrlDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  93 FMDGADLcFEIVKRADAGFVYSEAVAshYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGES 172
Cdd:cd05033   86 YMENGSL-DKFLRENDGKFTVTQLVG--MLRGIASGMKYLSEMNYVHRDLAARNILVNSDLV---CKVSDFGLSRRLEDS 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 548961101 173 G---LVAGGRVGTpHFMAPEVVKREPYGKPVDVWGCGVILFILLS 214
Cdd:cd05033  160 EatyTTKGGKIPI-RWTAPEAIAYRKFTSASDVWSFGIVMWEVMS 203
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
124-272 6.05e-09

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: 58.66  E-value: 6.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 124 QILEALRYCHDNNIIHRDVKPHCVLLASKENSAPV-KLGGFGVAIQLGESGL--------VAGGrvGTPHFMAPEVVKRE 194
Cdd:cd14018  146 QLLEGVDHLVRHGIAHRDLKSDNILLELDFDGCPWlVIADFGCCLADDSIGLqlpfsswyVDRG--GNACLMAPEVSTAV 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 195 P-------YGKpVDVWGCGVILFILLSGCLPFYGTKERLFEgiiKGKYKMN--PRQWSHISESAKDLVRRMLMLDPAERI 265
Cdd:cd14018  224 PgpgvvinYSK-ADAWAVGAIAYEIFGLSNPFYGLGDTMLE---SRSYQESqlPALPSAVPPDVRQVVKDLLQRDPNKRV 299

                 ....*..
gi 548961101 266 TVYEALN 272
Cdd:cd14018  300 SARVAAN 306
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
58-238 7.02e-09

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: 58.49  E-value: 7.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  58 DLKREASICHML-KHPHIVELLETYSSDGMLYMVFEFMD--------------GADLCFEIVKRADAGFVYSEAVASHYm 122
Cdd:cd05101   75 DLVSEMEMMKMIgKHKNIINLLGACTQDGPLYVIVEYASkgnlreylrarrppGMEYSYDINRVPEEQMTFKDLVSCTY- 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 123 rQILEALRYCHDNNIIHRDVKPHCVLLAskENSApVKLGGFGVAIQLGESGL---VAGGRVGTpHFMAPEVVKREPYGKP 199
Cdd:cd05101  154 -QLARGMEYLASQKCIHRDLAARNVLVT--ENNV-MKIADFGLARDINNIDYykkTTNGRLPV-KWMAPEALFDRVYTHQ 228
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 548961101 200 VDVWGCGVILF-ILLSGCLPFYGTK-ERLFEgIIKGKYKMN 238
Cdd:cd05101  229 SDVWSFGVLMWeIFTLGGSPYPGIPvEELFK-LLKEGHRMD 268
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
14-247 7.19e-09

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: 57.78  E-value: 7.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  14 LCEVIGKGPFSVVR----RCINRETGQ-QFAVKIVdvakftssPGLSTE----DLKREASICHMLKHPHIVELLETYSSD 84
Cdd:cd05036   10 LIRALGQGAFGEVYegtvSGMPGDPSPlQVAVKTL--------PELCSEqdemDFLMEALIMSKFNHPNIVRCIGVCFQR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  85 GMLYMVFEFMDGADL-CF--EIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLG 161
Cdd:cd05036   82 LPRFILLELMAGGDLkSFlrENRPRPEQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPGRVAKIG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 162 GFGVAIQLGESGLV-AGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYG-TKERLFEGIIKGKyKM 237
Cdd:cd05036  162 DFGMARDIYRADYYrKGGKAMLPvKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSlGYMPYPGkSNQEVMEFVTSGG-RM 240
                        250       260
                 ....*....|....*....|...
gi 548961101 238 NPRQ-------------WSHISE 247
Cdd:cd05036  241 DPPKncpgpvyrimtqcWQHIPE 263
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
45-266 7.36e-09

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. 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 Yes 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 (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 57.77  E-value: 7.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  45 VAKFTSSPG-LSTEDLKREASICHMLKHPHIVELLETYSSDGmLYMVFEFMDGADLcFEIVKRADAGFVYSEAVAShYMR 123
Cdd:cd05069   39 VAIKTLKPGtMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEP-IYIVTEFMGKGSL-LDFLKEGDGKYLKLPQLVD-MAA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 124 QILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQLGESGLVAGGRVGTP-HFMAPEVVKREPYGKPVDV 202
Cdd:cd05069  116 QIADGMAYIERMNYIHRDLRAANILVG---DNLVCKIADFGLARLIEDNEYTARQGAKFPiKWTAPEAALYGRFTIKSDV 192
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548961101 203 WGCGVILFILLS-GCLPFYGTKER-LFEGIIKGkYKMNPRQwsHISESAKDLVRRMLMLDPAERIT 266
Cdd:cd05069  193 WSFGILLTELVTkGRVPYPGMVNReVLEQVERG-YRMPCPQ--GCPESLHELMKLCWKKDPDERPT 255
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
122-276 7.46e-09

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: 58.22  E-value: 7.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 122 MRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLGGFGVAIQLgesglvaggRVGT----------PHFMAPEV- 190
Cdd:cd14013  126 MRQILVALRKLHSTGIVHRDVKPQNIIVSEGDGQ--FKIIDLGAAADL---------RIGInyipkeflldPRYAPPEQy 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 191 -----VKREP--------------YGKP--VDVWGCGVilfILLSGCLPfygtKERLFEGIIKGKYKMNPRQW------- 242
Cdd:cd14013  195 imstqTPSAPpapvaaalspvlwqMNLPdrFDMYSAGV---ILLQMAFP----NLRSDSNLIAFNRQLKQCDYdlnawrm 267
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 548961101 243 ---SHISESAK--------------DLVRRMLMLDPAERITVYEALNHPWL 276
Cdd:cd14013  268 lvePRASADLRegfeildlddgagwDLVTKLIRYKPRGRLSASAALAHPYF 318
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
18-240 7.67e-09

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: 58.10  E-value: 7.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  18 IGKGPFSVV--RRCINRETGQQfavKIVDVAKFTSSPGLST-EDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFM 94
Cdd:cd05094   13 LGEGAFGKVflAECYNLSPTKD---KMLVAVKTLKDPTLAArKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEYM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  95 DGADLC-FEIVKRADAG-FVYSEAVAS----------HYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGG 162
Cdd:cd05094   90 KHGDLNkFLRAHGPDAMiLVDGQPRQAkgelglsqmlHIATQIASGMVYLASQHFVHRDLATRNCLVG---ANLLVKIGD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 163 FGVAIQLGESGLV-AGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYG-TKERLFEGIIKGKYKMN 238
Cdd:cd05094  167 FGMSRDVYSTDYYrVGGHTMLPiRWMPPESIMYRKFTTESDVWSFGVILWeIFTYGKQPWFQlSNTEVIECITQGRVLER 246

                 ..
gi 548961101 239 PR 240
Cdd:cd05094  247 PR 248
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
57-221 8.21e-09

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. 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. The Ror2 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: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 57.72  E-value: 8.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  57 EDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYS----EAVAS--------HYMRQ 124
Cdd:cd05091   54 EEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIFSYCSHGDLHEFLVMRSPHSDVGStdddKTVKStlepadflHIVTQ 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 125 ILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGvAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWG 204
Cdd:cd05091  134 IAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKISDLGLFR-EVYAADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWS 212
                        170
                 ....*....|....*...
gi 548961101 205 CGVILFILLS-GCLPFYG 221
Cdd:cd05091  213 YGVVLWEVFSyGLQPYCG 230
SH3_GRB2_C cd11949
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical ...
610-668 1.63e-08

C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. It is ubiquitously expressed in all tissues throughout development and is important in cell cycle progression, motility, morphogenesis, and angiogenesis. In lymphocytes, GRB2 is associated with antigen receptor signaling components. GRB2 contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRB2 binds to Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, as well as to the proline-rich C-terminus of FGRF2. 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: 212882 [Multi-domain]  Cd Length: 53  Bit Score: 51.38  E-value: 1.63e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 548961101 610 YVRAQFEYDPAKDDlipckEAGirFRVGDIIQIISKDDHNWWQGKLenskNGTAGLIPS 668
Cdd:cd11949    1 YVQALFDFDPQEDG-----ELG--FRRGDFIEVMDNSDPNWWKGAC----HGQTGMFPR 48
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
33-221 2.20e-08

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. 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. The Ror1 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: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 56.56  E-value: 2.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101  33 ETGQQFAVKIVdvaKFTSSPGLSTEdLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKR---ADA 109
Cdd:cd05090   32 DHAQLVAIKTL---KDYNNPQQWNE-FQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLHEFLIMRsphSDV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548961101 110 GFVYSE--AVAS--------HYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESGL--VAG 177
Cdd:cd05090  108 GCSSDEdgTVKSsldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLH---VKISDLGLSREIYSSDYyrVQN 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 548961101 178 GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYG 221
Cdd:cd05090  185 KSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYG 229
 
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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