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Conserved domains on  [gi|1039796143|ref|XP_017173859|]
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peripheral plasma membrane protein CASK isoform X22 [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 ...
8-313 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: 609.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEgkrwisNLKREASICHMLKHPHIVELLETY 87
Cdd:cd14094     1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTE------DLKREASICHMLKHPHIVELLETY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLG 167
Cdd:cd14094    75 SSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQ 247
Cdd:cd14094   155 GFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQ 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796143 248 WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGA 313
Cdd:cd14094   235 WSHISESAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRIHLPETVEQLRKFNARRKLKGA 300
Guanylate_kin pfam00625
Guanylate kinase;
716-889 4.80e-74

Guanylate kinase;


:

Pssm-ID: 395500  Cd Length: 182  Bit Score: 240.36  E-value: 4.80e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 716 KRKTLVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYG 795
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 796 TKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTItPGLNE------DESLQRLQKESDVLQRTYAHY-F 868
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSL-KVLQRrlkgrgKEQEEKINKRMAAAEQEFQHYeF 159
                         170       180
                  ....*....|....*....|.
gi 1039796143 869 DLTIINNEIDETIRHLEEAVE 889
Cdd:pfam00625 160 DVIIVNDDLEEAYKKLKEALE 180
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
495-575 1.34e-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: 1.34e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 495 RLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIV 574
Cdd:cd10831     1 RLVQFQKNTDEPMGITLKMNEDGRCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREARGSITFKIV 80

                  .
gi 1039796143 575 P 575
Cdd:cd10831    81 P 81
SH3_CASK cd12081
Src Homology 3 domain of Calcium/calmodulin-dependent Serine protein Kinase; CASK is a ...
599-660 1.53e-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: 1.53e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 599 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPEL 660
Cdd:cd12081     1 YVRAQFEYDPLKDDLIPCKQAGIRFRVGDILQIISKDDHNWWQAKLENSKNGTAGLIPSPEL 62
L27 pfam02828
L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.
412-462 2.47e-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: 2.47e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 412 VQRAKEVLEEISCYPE-NNDAKELKRILTQPHFMALLQTHDVVAHEVYSDEA 462
Cdd:pfam02828   1 VELVLELLEDLQPLSEaSEDLAELQKLLQSPHLQALLEAHDKVAQKVYEPPS 52
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
354-407 1.23e-10

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


:

Pssm-ID: 197794  Cd Length: 53  Bit Score: 57.52  E-value: 1.23e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039796143  354 SQVLDSLEEIHALTDCSEkDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNP 407
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 ...
8-313 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: 609.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEgkrwisNLKREASICHMLKHPHIVELLETY 87
Cdd:cd14094     1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTE------DLKREASICHMLKHPHIVELLETY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLG 167
Cdd:cd14094    75 SSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQ 247
Cdd:cd14094   155 GFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQ 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796143 248 WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGA 313
Cdd:cd14094   235 WSHISESAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRIHLPETVEQLRKFNARRKLKGA 300
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-282 1.02e-94

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 298.29  E-value: 1.02e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglstegkrwiSNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDR----------ERILREIKILKKLKHPNIVRLYDVFEDED 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   92 MLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:smart00220  71 KLYLVMEYCEGGDLFDLLKKRG----RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH---VKLADFGL 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  172 AIQLGESGLvAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG--TKERLFEGIIKGKYKMNPRQWS 249
Cdd:smart00220 144 ARQLDPGEK-LTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGddQLLELFKKIGKPKPPFPPPEWD 222
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1039796143  250 hISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:smart00220 223 -ISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
Guanylate_kin pfam00625
Guanylate kinase;
716-889 4.80e-74

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 240.36  E-value: 4.80e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 716 KRKTLVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYG 795
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 796 TKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTItPGLNE------DESLQRLQKESDVLQRTYAHY-F 868
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSL-KVLQRrlkgrgKEQEEKINKRMAAAEQEFQHYeF 159
                         170       180
                  ....*....|....*....|.
gi 1039796143 869 DLTIINNEIDETIRHLEEAVE 889
Cdd:pfam00625 160 DVIIVNDDLEEAYKKLKEALE 180
Pkinase pfam00069
Protein kinase domain;
12-282 2.77e-64

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 215.19  E-value: 2.77e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglstEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEK---------IKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcFEIVKRadaGFVYSEAVASHYMRQILEALRYCHDNNIihrdvkphcvllaskensapvklggfgv 171
Cdd:pfam00069  72 NLYLVLEYVEGGSL-FDLLSE---KGAFSEREAKFIMKQILEGLESGSSLTT---------------------------- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 aiqlgesglvaggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYkMNPRQWSH 250
Cdd:pfam00069 120 -------------FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNeIYELIIDQPY-AFPELPSN 185
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1039796143 251 ISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:pfam00069 186 LSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
726-892 2.32e-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: 2.32e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  726 HGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLETIRKIH 805
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  806 EQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTITPGLNE-----DESLQRLQKESDVLQRTYAHY--FDLTIINNEID 878
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRlrqrgTETSERIQKRLAAAQKEAQEYhlFDYVIVNDDLE 160
                          170
                   ....*....|....
gi 1039796143  879 ETIRHLEEAVELVC 892
Cdd:smart00072 161 DAYEELKEILEAEQ 174
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
495-575 1.34e-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: 1.34e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 495 RLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIV 574
Cdd:cd10831     1 RLVQFQKNTDEPMGITLKMNEDGRCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREARGSITFKIV 80

                  .
gi 1039796143 575 P 575
Cdd:cd10831    81 P 81
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
12-270 2.64e-52

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 190.61  E-value: 2.64e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvAKFTSSPglstegkRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLR-PELAADP-------EARERFRREARALARLNHPNIVRVYDVGEEDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:COG0515    81 RPYLVMEYVEGESLA-DLLRRRGP---LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGR---VKLIDFGI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGL-VAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWS 249
Cdd:COG0515   154 ARALGGATLtQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGdSPAELLRAHLREPPPPPSELRP 233
                         250       260
                  ....*....|....*....|.
gi 1039796143 250 HISESAKDLVRRMLMLDPAER 270
Cdd:COG0515   234 DLPPALDAIVLRALAKDPEER 254
SH3_CASK cd12081
Src Homology 3 domain of Calcium/calmodulin-dependent Serine protein Kinase; CASK is a ...
599-660 1.53e-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: 1.53e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 599 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPEL 660
Cdd:cd12081     1 YVRAQFEYDPLKDDLIPCKQAGIRFRVGDILQIISKDDHNWWQAKLENSKNGTAGLIPSPEL 62
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
12-300 3.22e-37

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 142.65  E-value: 3.22e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglstegKRWISNLKR------EASICHMLKHPHIVELLE 85
Cdd:PTZ00263   20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLK--------------KREILKMKQvqhvaqEKSILMELSHPFIVNMMC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  86 TYSSDGMLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVK 165
Cdd:PTZ00263   86 SFQDENRVYFLLEFVVGGEL-FTHLRKAGR---FPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGH---VK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 166 LGGFGVAIQLGESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMn 244
Cdd:PTZ00263  159 VTDFGFAKKVPDRTFTL---CGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDdTPFRIYEKILAGRLKF- 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 245 PRqWshISESAKDLVRRMLMLDPAERI-----TVYEALNHPWLKERD---RYAYKIHLPETVEQ 300
Cdd:PTZ00263  235 PN-W--FDGRARDLVKGLLQTDHTKRLgtlkgGVADVKNHPYFHGANwdkLYARYYPAPIPVRV 295
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
720-888 1.06e-29

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: 116.05  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 720 LVLLGAHGVGRRHIKNTLITKHPDrFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLE 799
Cdd:TIGR03263   3 IVISGPSGAGKSTLVKALLEEDPN-LKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTPKS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 800 TIRKIHEQGLIAILDVEPQ-ALKVLRTAEFAPFvVFIAAPTItpglneDESLQRLQK-----ESDVLQR--------TYA 865
Cdd:TIGR03263  82 PVEEALAAGKDVLLEIDVQgARQVKKKFPDAVS-IFILPPSL------EELERRLRKrgtdsEEVIERRlakakkeiAHA 154
                         170       180
                  ....*....|....*....|...
gi 1039796143 866 HYFDLTIINNEIDETIRHLEEAV 888
Cdd:TIGR03263 155 DEFDYVIVNDDLEKAVEELKSII 177
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
720-885 5.57e-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: 5.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 720 LVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLE 799
Cdd:cd00071     2 IVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSKA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 800 TIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPtitpglnedeslqrlqkesdvlqrtyahyfDLTIINNEIDE 879
Cdd:cd00071    82 AVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP------------------------------DYVIVNDDLEK 131

                  ....*.
gi 1039796143 880 TIRHLE 885
Cdd:cd00071   132 AYEELK 137
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
720-889 2.09e-27

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 110.16  E-value: 2.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 720 LVLLGAHGVGRRHIKNTLITKHPDrFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLE 799
Cdd:COG0194     5 IVLSGPSGAGKTTLVKALLERDPD-LRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGTPKA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 800 TIRKIHEQGLIAILDVEPQ-ALKVLRTAEFAPFvVFIAAPTItpglneDESLQRL----QKESDVLQR---------TYA 865
Cdd:COG0194    84 EVEEALAAGKDVLLEIDVQgARQVKKKFPDAVS-IFILPPSL------EELERRLrgrgTDSEEVIERrlakareelAHA 156
                         170       180
                  ....*....|....*....|....
gi 1039796143 866 HYFDLTIINNEIDETIRHLEEAVE 889
Cdd:COG0194   157 DEFDYVVVNDDLDRAVEELKAIIR 180
gmk PRK00300
guanylate kinase; Provisional
720-885 5.60e-24

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 100.55  E-value: 5.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 720 LVLLGAHGVGrrhiKNTLIT---KHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGT 796
Cdd:PRK00300    8 IVLSGPSGAG----KSTLVKallERDPNLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYYGT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 797 KLETIRKIHEQGLIAILDVEPQ-ALKVLRTAEFAPFvVFIAAPTItpglneDESLQRLQK---ES-DVLQR--------- 862
Cdd:PRK00300   84 PRSPVEEALAAGKDVLLEIDWQgARQVKKKMPDAVS-IFILPPSL------EELERRLRGrgtDSeEVIARrlakareei 156
                         170       180
                  ....*....|....*....|...
gi 1039796143 863 TYAHYFDLTIINNEIDETIRHLE 885
Cdd:PRK00300  157 AHASEYDYVIVNDDLDTALEELK 179
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
12-227 9.89e-24

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 106.42  E-value: 9.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRR--CI--NRETgqqfAVKIVD---------VAKFtsspglstegkrwisnlKREA----Sichm 74
Cdd:NF033483    9 YEIGERIGRGGMAEVYLakDTrlDRDV----AVKVLRpdlardpefVARF-----------------RREAqsaaS---- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  75 LKHPHIVELLETYSSDGMLYMVFEFMDGADLcFEIVkRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVL 154
Cdd:NF033483   64 LSHPNIVSVYDVGEDGGIPYIVMEYVDGRTL-KDYI-REHGPLSPEEAV--EIMIQILSALEHAHRNGIVHRDIKPQNIL 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 155 LAskeNSAPVKLGGFGVAIQLGESGLVAGGRV-GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 227
Cdd:NF033483  140 IT---KDGRVKVTDFGIARALSSTTMTQTNSVlGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDG 210
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
33-302 1.96e-22

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: 104.16  E-value: 1.96e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   33 ETGQQFAVKIVDVakftsspgLSTEGKRWISNLKREASICHMLKHPHIVELLET-YSSDGMLYMVFEFMDGADLcfeiVK 111
Cdd:TIGR03903    1 MTGHEVAIKLLRT--------DAPEEEHQRARFRRETALCARLYHPNIVALLDSgEAPPGLLFAVFEYVPGRTL----RE 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  112 RADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGR------ 185
Cdd:TIGR03903   69 VLAADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIGTLLPGVRDADVATltrtte 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  186 -VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG--TKERLFEGIIKGKYKMNPRQWSHiseSAKDLVRRM 262
Cdd:TIGR03903  149 vLGTPTYCAPEQLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGasVAEILYQQLSPVDVSLPPWIAGH---PLGQVLRKA 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1039796143  263 LMLDPAERitvyeALNHPWLKERDRyayKIHLPETVEQLR 302
Cdd:TIGR03903  226 LNKDPRQR-----AASAPALAERFR---ALELCALVGILR 257
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
496-573 3.17e-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: 3.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 496 LVQFQKNTDEPMGITLKMNELNH---CIVARIMHGGMIHRQGtLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFK 572
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGdpgIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                  .
gi 1039796143 573 I 573
Cdd:pfam00595  80 I 80
L27 pfam02828
L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.
412-462 2.47e-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: 2.47e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 412 VQRAKEVLEEISCYPE-NNDAKELKRILTQPHFMALLQTHDVVAHEVYSDEA 462
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 ...
493-575 1.46e-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: 66.63  E-value: 1.46e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  493 RVRLVQFQKNTdEPMGITLKMN--ELNHCIVARIMHGGMIHRQGtLHVGDEIREINGISVANQTVEQLQKMLREMRGSIT 570
Cdd:smart00228   1 EPRLVELEKGG-GGLGFSLVGGkdEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVT 78

                   ....*
gi 1039796143  571 FKIVP 575
Cdd:smart00228  79 LTVLR 83
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
413-461 2.47e-12

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


Pssm-ID: 197794  Cd Length: 53  Bit Score: 62.14  E-value: 2.47e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039796143  413 QRAKEVLEEISCYPE-NNDAKELKRILTQPHFMALLQTHDVVAHEVYSDE 461
Cdd:smart00569   1 QRLLELLEELQSLLSpSEDLQELRRLLQSPHLQALLKIHDKVAETELDPP 50
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
599-657 1.94e-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: 1.94e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143  599 YVRAQFEYDPAKDDlipckeaGIRFRVGDIIQIISKDDHNWWQGKLensKNGTAGLIPS 657
Cdd:smart00326   4 QVRALYDYTAQDPD-------ELSFKKGDIITVLEKSDDGWWKGRL---GRGKEGLFPS 52
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
354-407 1.23e-10

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


Pssm-ID: 197794  Cd Length: 53  Bit Score: 57.52  E-value: 1.23e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039796143  354 SQVLDSLEEIHALTDCSEkDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNP 407
Cdd:smart00569   1 QRLLELLEELQSLLSPSE-DLQELRRLLQSPHLQALLKIHDKVAETELDPPLPE 53
L27 pfam02828
L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.
353-400 3.22e-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: 3.22e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1039796143 353 VSQVLDSLEEIHALTDCSEkDLDFLHSVFQDQHLHTLLDLYDKINTKS 400
Cdd:pfam02828   1 VELVLELLEDLQPLSEASE-DLAELQKLLQSPHLQALLEAHDKVAQKV 47
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
601-657 2.30e-08

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


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 50.66  E-value: 2.30e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 601 RAQFEYDPAKDDLIPckeagirFRVGDIIQIISKDDHNWWQGKLensKNGTAGLIPS 657
Cdd:pfam00018   1 VALYDYTAQEPDELS-------FKKGDIIIVLEKSEDGWWKGRN---KGGKEGLIPS 47
 
Name Accession Description Interval E-value
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
8-313 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: 609.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEgkrwisNLKREASICHMLKHPHIVELLETY 87
Cdd:cd14094     1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTE------DLKREASICHMLKHPHIVELLETY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLG 167
Cdd:cd14094    75 SSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQ 247
Cdd:cd14094   155 GFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQ 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796143 248 WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGA 313
Cdd:cd14094   235 WSHISESAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRIHLPETVEQLRKFNARRKLKGA 300
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
11-281 2.25e-120

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: 365.65  E-value: 2.25e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglstegkrwISNLKREASICHMLKHPHIVELLETYSSD 90
Cdd:cd05117     1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSED---------EEMLRREIEILKRLDHPNIVKLYEVFEDD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLCFEIVKRadagFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFG 170
Cdd:cd05117    72 KNLYLVMELCTGGELFDRIVKK----GSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSPIKIIDFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLGEsGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWS 249
Cdd:cd05117   148 LAKIFEE-GEKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGeTEQELFEKILKGKYSFDSPEWK 226
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1039796143 250 HISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd05117   227 NVSEEAKDLIKRLLVVDPKKRLTAAEALNHPW 258
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-313 5.81e-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: 358.27  E-value: 5.81e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstegkRWISNLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSA---------RDHQKLEREARICRLLKHPNIVRLHDSISE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGF 169
Cdd:cd14086    72 EGFHYLVFDLVTGGELFEDIVARE----FYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT-KERLFEGIIKGKYKMNPRQW 248
Cdd:cd14086   148 GLAIEVQGDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEdQHRLYAQIKAGAYDYPSPEW 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039796143 249 SHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGA 313
Cdd:cd14086   228 DTVTPEAKDLINQMLTVNPAKRITAAEALKHPWICQRDRVASMVHRQETVDCLKKFNARRKLKGA 292
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-282 1.02e-94

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 298.29  E-value: 1.02e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglstegkrwiSNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDR----------ERILREIKILKKLKHPNIVRLYDVFEDED 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   92 MLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:smart00220  71 KLYLVMEYCEGGDLFDLLKKRG----RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH---VKLADFGL 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  172 AIQLGESGLvAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG--TKERLFEGIIKGKYKMNPRQWS 249
Cdd:smart00220 144 ARQLDPGEK-LTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGddQLLELFKKIGKPKPPFPPPEWD 222
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1039796143  250 hISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:smart00220 223 -ISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
12-281 3.48e-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: 257.06  E-value: 3.48e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTsspglstegKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14003     2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLK---------EEIEEKIKREIEIMKLLNHPNIIKLYEVIETEN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd14003    73 KIYLVMEYASGGEL-FDYIVNNGR---LSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGN---LKIIDFGL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLgESGLVAGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMnprqWS 249
Cdd:cd14003   146 SNEF-RGGSLLKTFCGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSkLFRKILKGKYPI----PS 220
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1039796143 250 HISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14003   221 HLSPDARDLIRRMLVVDPSKRITIEEILNHPW 252
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
8-282 1.06e-74

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: 245.73  E-value: 1.06e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglsTEGKRWISNLKREASICHML-KHPHIVELLET 86
Cdd:cd14093     1 FYAKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSE---NEAEELREATRREIEILRQVsGHPNIIELHDV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYMVFEFMDGADLcF----EIVKradagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsa 162
Cdd:cd14093    78 FESPTFIFLVFELCRKGEL-FdyltEVVT-------LSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLN-- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 163 pVKLGGFGVAIQLGEsGLVAGGRVGTPHFMAPEVVKR------EPYGKPVDVWGCGVILFILLSGCLPFYGTKERL-FEG 235
Cdd:cd14093   148 -VKISDFGFATRLDE-GEKLRELCGTPGYLAPEVLKCsmydnaPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVmLRN 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1039796143 236 IIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14093   226 IMEGKYEFGSPEWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
Guanylate_kin pfam00625
Guanylate kinase;
716-889 4.80e-74

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 240.36  E-value: 4.80e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 716 KRKTLVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYG 795
Cdd:pfam00625   1 SRRPVVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 796 TKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTItPGLNE------DESLQRLQKESDVLQRTYAHY-F 868
Cdd:pfam00625  81 TSVETIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSL-KVLQRrlkgrgKEQEEKINKRMAAAEQEFQHYeF 159
                         170       180
                  ....*....|....*....|.
gi 1039796143 869 DLTIINNEIDETIRHLEEAVE 889
Cdd:pfam00625 160 DVIIVNDDLEEAYKKLKEALE 180
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
9-281 1.02e-69

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: 231.88  E-value: 1.02e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkftsspglSTEGKRwiSNLKREASICHMLKHPHIVELLETYS 88
Cdd:cd14083     2 RDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKK--------ALKGKE--DSLENEIAVLRKIKHPNIVQLLDIYE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGG 168
Cdd:cd14083    72 SKSHLYLVMELVTGGELFDRIVEKG----SYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSKIMISD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAiQLGESGLVAGGrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQ 247
Cdd:cd14083   148 FGLS-KMEDSGVMSTA-CGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDsKLFAQILKAEYEFDSPY 225
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796143 248 WSHISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14083   226 WDDISDSAKDFIRHLMEKDPNKRYTCEQALEHPW 259
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
12-316 9.01e-69

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: 230.21  E-value: 9.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstegkrwisnlkREASIchMLK---HPHIVELLETYS 88
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPS---------------EEIEI--LLRygqHPNIITLRDVYD 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAP-VKLG 167
Cdd:cd14091    65 DGNSVYLVTELLRGGELLDRILRQKF----FSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDPEsLRIC 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVAIQL-GESGLVAggrvgTPH----FMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF-YG---TKERLFEGIIK 238
Cdd:cd14091   141 DFGFAKQLrAENGLLM-----TPCytanFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFaSGpndTPEVILARIGS 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796143 239 GKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDryaykiHLPETveQLRKFNARRKLKGAVLA 316
Cdd:cd14091   216 GKIDLSGGNWDHVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRNRD------SLPQR--QLTDPQDAALVKGAVAA 285
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
8-282 3.00e-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: 228.43  E-value: 3.00e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEGKRWISNLKREASICHMLKHPHIVELLETY 87
Cdd:cd14084     4 LRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIG---SRREINKPRNIETEIEILKKLSHPCIIKIEDFF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLG 167
Cdd:cd14084    81 DAEDDYYIVLELMEGGELFDRVVSNK----RLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEECLIKIT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVAIQLGESGLVAGgRVGTPHFMAPEVVK---REPYGKPVDVWGCGVILFILLSGCLPFYG--TKERLFEGIIKGKYK 242
Cdd:cd14084   157 DFGLSKILGETSLMKT-LCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEeyTQMSLKEQILSGKYT 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039796143 243 MNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14084   236 FIPKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
8-319 1.68e-65

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: 221.62  E-value: 1.68e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglSTEGKRWIsnlKREASICHMLKHPHIVELLETY 87
Cdd:cd14085     1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLK----------KTVDKKIV---RTEIGVLLRLSHPNIIKLKEIF 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLG 167
Cdd:cd14085    68 ETPTEISLVLELVTGGELFDRIVEKG----YYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIA 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVAiQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG--TKERLFEGIIKGKYKMNP 245
Cdd:cd14085   144 DFGLS-KIVDQQVTMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDerGDQYMFKRILNCDYDFVS 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 246 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDryAYKIHLPETVEQLRKFNARRKLKGAVLAAVS 319
Cdd:cd14085   223 PWWDDVSLNAKDLVKKLIVLDPKKRLTTQQALQHPWVTGKA--ANFAHMDTAQKKLQEFNARRKLKAAVKAVVA 294
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
12-281 1.79e-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: 220.27  E-value: 1.79e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglsTEGKRWIsnLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14095     2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAK--------CKGKEHM--IENEVAILRRVKHPNIVQLIEEYDTDT 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEN-SAPVKLGGFG 170
Cdd:cd14095    72 ELYLVMELVKGGDL-FDAITSSTK---FTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDgSKSLKLADFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLGESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY---GTKERLFEGIIKGKYKMNPRQ 247
Cdd:cd14095   148 LATEVKEPLFTV---CGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRspdRDQEELFDLILAGEFEFLSPY 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796143 248 WSHISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14095   225 WDNISDSAKDLISRMLVVDPEKRYSAGQVLDHPW 258
Pkinase pfam00069
Protein kinase domain;
12-282 2.77e-64

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 215.19  E-value: 2.77e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglstEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEK---------IKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcFEIVKRadaGFVYSEAVASHYMRQILEALRYCHDNNIihrdvkphcvllaskensapvklggfgv 171
Cdd:pfam00069  72 NLYLVLEYVEGGSL-FDLLSE---KGAFSEREAKFIMKQILEGLESGSSLTT---------------------------- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 aiqlgesglvaggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYkMNPRQWSH 250
Cdd:pfam00069 120 -------------FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNeIYELIIDQPY-AFPELPSN 185
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1039796143 251 ISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:pfam00069 186 LSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
18-282 3.45e-64

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: 217.04  E-value: 3.45e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVD---VAKFTSSPGLSTEGKRWISNLKREASICHMLKHPHIVELLETYSSDGM-- 92
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFNksrLRKRREGKNDRGKIKNALDDVRREIAIMKKLDHPNIVRLYEVIDDPESdk 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  93 LYMVFEFMDGADLcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVA 172
Cdd:cd14008    81 LYLVLEYCEGGPV--MELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGT---VKISDFGVS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 173 IQLGESGLVAGGRVGTPHFMAPEV--VKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNPRqw 248
Cdd:cd14008   156 EMFEDGNDTLQKTAGTPAFLAPELcdGDSKTYsGKAADIWALGVTLYCLVFGRLPFNGDNILeLYEAIQNQNDEFPIP-- 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796143 249 SHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14008   234 PELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
18-281 1.79e-63

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: 214.05  E-value: 1.79e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglstEGKRwisNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIPKRD---------KKKE---AVLREISILNQLQHPRIIQLHEAYESPTELVLIL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLCFEIVKRadagFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGFGVAIQLGE 177
Cdd:cd14006    69 ELCSGGELLDRLAER----GSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQ-IKIIDFGLARKLNP 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 sGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISESAK 256
Cdd:cd14006   144 -GEELKEIFGTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGeDDQETLANISACRVDFSEEYFSSVSQEAK 222
                         250       260
                  ....*....|....*....|....*
gi 1039796143 257 DLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14006   223 DFIRKLLVKEPRKRPTAQEALQHPW 247
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
11-282 7.33e-63

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: 212.88  E-value: 7.33e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKF-TSSPGLSTEgkrwisnlkREASICHMLKHPHIVELLETYSS 89
Cdd:cd14081     2 PYRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLsKESVLMKVE---------REIAIMKLIEHPNVLKLYDVYEN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGF 169
Cdd:cd14081    73 KKYLYLVLEYVSGGELFDYLVKKG----RLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNN---IKIADF 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVA-IQLGESGLVAGgrVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMnPr 246
Cdd:cd14081   146 GMAsLQPEGSLLETS--CGSPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRqLLEKVKRGVFHI-P- 221
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039796143 247 qwSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14081   222 --HFISPDAQDLLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
12-280 3.37e-62

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: 211.17  E-value: 3.37e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspgLSTEGKRwisNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd08215     2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSN------MSEKERE---EALNEVKLLSKLKHPNIVKYYESFEENG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd08215    73 KLCIVMEYADGGDLAQKIKKQKKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGV---VKLGDFGI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNPrqwSH 250
Cdd:cd08215   150 SKVLESTTDLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPaLVYKIVKGQYPPIP---SQ 226
                         250       260       270
                  ....*....|....*....|....*....|
gi 1039796143 251 ISESAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd08215   227 YSSELRDLVNSMLQKDPEKRPSANEILSSP 256
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-309 5.76e-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: 211.39  E-value: 5.76e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstegkrwiSNLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd14166     3 ETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRD-----------SSLENEIAVLKRIKHENIVTLEDIYES 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGF 169
Cdd:cd14166    72 TTHYYLVMQLVSGGELFDRILERG----VYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSKIMITDF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAiQLGESGLVAGGrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQW 248
Cdd:cd14166   148 GLS-KMEQNGIMSTA-CGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEeTESRLFEKIKEGYYEFESPFW 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796143 249 SHISESAKDLVRRMLMLDPAERITVYEALNHPWLK-----ERDRYaykihlPETVEQLRKFNARRK 309
Cdd:cd14166   226 DDISESAKDFIRHLLEKNPSKRYTCEKALSHPWIIgntalHRDIY------PSVSEQIQKNFAKSK 285
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
8-282 7.07e-62

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: 210.98  E-value: 7.07e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEGKrwiSNLKREASICHMLK-HPHIVELLET 86
Cdd:cd14181     8 FYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTAERLSPEQLEEVR---SSTLKEIHILRQVSgHPSIITLIDS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKL 166
Cdd:cd14181    85 YESSTFIFLVFDLMRRGELFDYLTEKV----TLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILL---DDQLHIKL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAIQLgESGLVAGGRVGTPHFMAPEVVK------REPYGKPVDVWGCGVILFILLSGCLPFYGTKERL-FEGIIKG 239
Cdd:cd14181   158 SDFGFSCHL-EPGEKLRELCGTPGYLAPEILKcsmdetHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLmLRMIMEG 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1039796143 240 KYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14181   237 RYQFSSPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPFF 279
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-282 4.37e-61

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: 208.34  E-value: 4.37e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftssPGLSTEGKRwiSNLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd14167     3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCI--------AKKALEGKE--TSIENEIAVLHKIKHPNIVALDDIYES 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLCFEIVKRadaGFvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGF 169
Cdd:cd14167    73 GGHLYLIMQLVSGGELFDRIVEK---GF-YTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEDSKIMISDF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAiQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQW 248
Cdd:cd14167   149 GLS-KIEGSGSVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDaKLFEQILKAEYEFDSPYW 227
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796143 249 SHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14167   228 DDISDSAKDFIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
10-281 3.83e-60

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: 206.50  E-value: 3.83e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELC-EVIGKGPFSVVRRCINRETGQQFAVKIVDvakftSSPGLSTegkrwiSNLKREASICHMLK-HPHIVELLETY 87
Cdd:cd14090     1 DLYKLTgELLGEGAYASVQTCINLYTGKEYAVKIIE-----KHPGHSR------SRVFREVETLHQCQgHPNILQLIEYF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLG 167
Cdd:cd14090    70 EDDERFYLVFEKMRGGPLLSHIEKRVH----FTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVSPVKIC 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVAiqlgeSGLVAGGR-------------VGTPHFMAPEVV-----KREPYGKPVDVWGCGVILFILLSGCLPFYGT- 228
Cdd:cd14090   146 DFDLG-----SGIKLSSTsmtpvttpelltpVGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGRc 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796143 229 ---------------KERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14090   221 gedcgwdrgeacqdcQELLFHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
16-281 8.07e-60

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: 204.83  E-value: 8.07e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIV-DVAKftsspglstegkrwisnLKREASIcHML--KHPHIVELLE----TYS 88
Cdd:cd14089     7 QVLGLGINGKVLECFHKKTGEKFALKVLrDNPK-----------------ARREVEL-HWRasGCPHIVRIIDvyenTYQ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAvaSHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGG 168
Cdd:cd14089    69 GRKCLLVVMECMEGGELFSRIQERADSAFTEREA--AEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAILKLTD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLVAGGRVgTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY---------GTKERlfegIIKG 239
Cdd:cd14089   147 FGFAKETTTKKSLQTPCY-TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYsnhglaispGMKKR----IRNG 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1039796143 240 KYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14089   222 QYEFPNPEWSNVSEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
16-282 1.40e-59

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: 203.91  E-value: 1.40e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglstegkrwISNLKREASICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd06606     6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEE---------LEALEREIRILSSLKHPNIVRYLGTERTENTLNI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQL 175
Cdd:cd06606    77 FLEYVPGGSLA-SLLKKFGK---LPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGV---VKLADFGCAKRL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GESGLVAGGR--VGTPHFMAPEVVKREPYGKPVDVW--GCGVILfiLLSGCLPFYGTKER---LFEgIIKGKYKmnPRQW 248
Cdd:cd06606   150 AEIATGEGTKslRGTPYWMAPEVIRGEGYGRAADIWslGCTVIE--MATGKPPWSELGNPvaaLFK-IGSSGEP--PPIP 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796143 249 SHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd06606   225 EHLSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
726-892 2.32e-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: 2.32e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  726 HGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLETIRKIH 805
Cdd:smart00072   1 SGVGKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  806 EQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTITPGLNE-----DESLQRLQKESDVLQRTYAHY--FDLTIINNEID 878
Cdd:smart00072  81 EKGKHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRlrqrgTETSERIQKRLAAAQKEAQEYhlFDYVIVNDDLE 160
                          170
                   ....*....|....
gi 1039796143  879 ETIRHLEEAVELVC 892
Cdd:smart00072 161 DAYEELKEILEAEQ 174
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
9-282 3.67e-59

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: 203.10  E-value: 3.67e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSP-GLSTEgkrwisNLKREASICHMLKHPHIVELLETY 87
Cdd:cd14105     4 EDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASRrGVSRE------DIEREVSILRQVLHPNIITLHDVF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAP-VKL 166
Cdd:cd14105    78 ENKTDVVLILELVAGGEL-FDFLAEKES---LSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPIPrIKL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAIQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNP 245
Cdd:cd14105   154 IDFGLAHKI-EDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGdTKQETLANITAVNYDFDD 232
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1039796143 246 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14105   233 EYFSNTSELAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
12-281 1.06e-58

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: 201.48  E-value: 1.06e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstegkRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14663     2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVARE--------GMVEQIKREIAIMKLLRHPNIVELHEVMATKT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKradaGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd14663    74 KIFFVMELVTGGELFSKIAK----NGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGN---LKISDFGL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIqLGESGLVAG---GRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnPR 246
Cdd:cd14663   147 SA-LSEQFRQDGllhTTCGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFDDENlMALYRKIMKGEFEY-PR 224
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1039796143 247 qwsHISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14663   225 ---WFSPGAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
18-282 1.87e-58

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: 200.53  E-value: 1.87e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglstEGKRwiSNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRK---------AKDR--EDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVM 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLcFEIVkrADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKeNSAPVKLGGFGVAIQLGE 177
Cdd:cd14103    70 EYVAGGEL-FERV--VDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSR-TGNQIKIIDFGLARKYDP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 SGLVaggRV--GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISES 254
Cdd:cd14103   146 DKKL---KVlfGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGdNDAETLANVTRAKWDFDDEAFDDISDE 222
                         250       260
                  ....*....|....*....|....*...
gi 1039796143 255 AKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14103   223 AKDFISKLLVKDPRKRMSAAQCLQHPWL 250
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
12-283 2.45e-58

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: 200.39  E-value: 2.45e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpGLSTegkrwisNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14007     2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKS-GLEH-------QLRREIEIQSHLRHPNILRLYGYFEDKK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcFEIVKRADagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd14007    74 RIYLILEYAPNGEL-YKELKKQK---RFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGE---LKLADFGW 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnprqWSH 250
Cdd:cd14007   147 SVHAPSNRRKT--FCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESkSHQETYKRIQNVDIKF----PSS 220
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1039796143 251 ISESAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd14007   221 VSPEAKDLISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
8-287 4.49e-57

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


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 198.68  E-value: 4.49e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYEL---CEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglstegKRWisNLKREASICHMLK-HPHIVEL 83
Cdd:cd14092     1 FFQNYELdlrEEALGDGSFSVCRKCVHKKTGQEFAVKIVS--------------RRL--DTSREVQLLRLCQgHPNIVKL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  84 LETYSSDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAP 163
Cdd:cd14092    65 HEVFQDELHTYLVMELLRGGELLERIRKKKR----FTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAE 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 164 VKLGGFGVAIQLGESGLVAggrvgTP----HFMAPEVVKREP----YGKPVDVWGCGVILFILLSGCLPFYGTKER---- 231
Cdd:cd14092   141 IKIVDFGFARLKPENQPLK-----TPcftlPYAAPEVLKQALstqgYDESCDLWSLGVILYTMLSGQVPFQSPSRNesaa 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 232 -LFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDR 287
Cdd:cd14092   216 eIMKRIKSGDFSFDGEEWKNVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSS 272
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
18-281 9.84e-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: 195.90  E-value: 9.84e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTsspglstegKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLN---------KKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLCFEIVKRadagFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGE 177
Cdd:cd14009    72 EYCAGGDLSQYIRKR----GRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVLKIADFGFARSLQP 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 SGLvAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNPRQWSHISESAK 256
Cdd:cd14009   148 ASM-AETLCGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVqLLRNIERSDAVIPFPIAAQLSPDCK 226
                         250       260
                  ....*....|....*....|....*
gi 1039796143 257 DLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14009   227 DLLRRLLRRDPAERISFEEFFAHPF 251
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
12-281 2.21e-56

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: 195.17  E-value: 2.21e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFtsspglstEGKRWIsnLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKL--------KGKEDM--IESEILIIKSLSHPNIVKLFEVYETEK 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEN-SAPVKLGGFG 170
Cdd:cd14185    72 EIYLILEYVRGGDLFDAIIESVK----FTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDkSTTLKLADFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLGESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG---TKERLFEGIIKGKYKMNPRQ 247
Cdd:cd14185   148 LAKYVTGPIFTV---CGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSperDQEELFQIIQLGHYEFLPPY 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796143 248 WSHISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14185   225 WDNISEAAKDLISRLLVVDPEKRYTAKQVLQHPW 258
PDZ_CASK-like cd10831
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ...
495-575 1.34e-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: 1.34e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 495 RLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIV 574
Cdd:cd10831     1 RLVQFQKNTDEPMGITLKMNEDGRCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREARGSITFKIV 80

                  .
gi 1039796143 575 P 575
Cdd:cd10831    81 P 81
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
10-282 1.85e-55

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: 192.41  E-value: 1.85e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAvkivdvAKFTSSPGLSTEgkrwiSNLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd14114     2 DHYDILEELGTGAFGVVHRCTERATGNNFA------AKFIMTPHESDK-----ETVRKEIQIMNQLHHPKLINLHDAFED 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLcFEivKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnSAPVKLGGF 169
Cdd:cd14114    71 DNEMVLILEFLSGGEL-FE--RIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKR-SNEVKLIDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQW 248
Cdd:cd14114   147 GLATHLDPKESVK-VTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDdETLRNVKSCDWNFDDSAF 225
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796143 249 SHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14114   226 SGISEEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
12-281 4.08e-55

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: 191.92  E-value: 4.08e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGlSTEGkrwisnLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14098     2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDK-NLQL------FQREINILKSLEHPGIVRLIDWYEDDQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIvkrADAGFVySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSAPVKLGGFGV 171
Cdd:cd14098    75 HIYLVMEYVEGGDLMDFI---MAWGAI-PEQHARELTKQILEAMAYTHSMGITHRDLKPENILI-TQDDPVIVKISDFGL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 A-IQLGESGLVAggRVGTPHFMAPEVVK----REP--YGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKM 243
Cdd:cd14098   150 AkVIHTGTFLVT--FCGTMAYLAPEILMskeqNLQggYSNLVDMWSVGCLVYVMLTGALPFDGsSQLPVEKRIRKGRYTQ 227
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039796143 244 NPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14098   228 PPLVDFNISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
12-282 8.75e-55

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: 190.62  E-value: 8.75e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTsspglstegKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14069     3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAP---------GDCPENIKKEVCIQKMLSHKNVVRFYGHRREGE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcFEIVKrADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd14069    74 FQYLFLEYASGGEL-FDKIE-PDVGM--PEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDN---LKISDFGL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQL---GESGLVaGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKER--LFEGIIKGKyKMNP 245
Cdd:cd14069   147 ATVFrykGKERLL-NKMCGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELPWDQPSDScqEYSDWKENK-KTYL 224
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1039796143 246 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14069   225 TPWKKIDTAALSLLRKILTENPNKRITIEDIKKHPWY 261
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
12-282 2.53e-54

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: 189.02  E-value: 2.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspgLSTEGKrwisnLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14079     4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKS---LDMEEK-----IRREIQILKLFRHPHIIRLYEVIETPT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd14079    76 DIFMVMEYVSGGELFDYIVQKGR----LSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMN---VKIADFGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 aiqlgeSGLVAGGR-----VGTPHFMAPEVVKREPYGKP-VDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMn 244
Cdd:cd14079   149 ------SNIMRDGEflktsCGSPNYAAPEVISGKLYAGPeVDVWSCGVILYALLCGSLPFDDEHiPNLFKKIKSGIYTI- 221
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039796143 245 PrqwSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14079   222 P---SHLSPGARDLIKRMLVVDPLKRITIPEIRQHPWF 256
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
12-282 4.62e-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: 189.96  E-value: 4.62e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCI-NRETGQQFAVKIVDVAKFTSSPGLSTEgkrwISNLKREASICHMLKHPHIVELLETYSSD 90
Cdd:cd14096     3 YRLINKIGEGAFSNVYKAVpLRNTGKPVAIKVVRKADLSSDNLKGSS----RANILKEVQIMKRLSHPNIVKLLDFQESD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAS--------KENSA 162
Cdd:cd14096    79 EYYYIVLELADGGEIFHQIVRLT----YFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivKLRKA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 163 P----------------------VKLGGFGVAIQLGESGLVAggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLS 220
Cdd:cd14096   155 DddetkvdegefipgvggggigiVKLADFGLSKQVWDSNTKT--PCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLC 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039796143 221 GCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14096   233 GFPPFYDeSIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
18-280 6.19e-54

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: 186.71  E-value: 6.19e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFtsspglstegKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKL----------KKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVM 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLcFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 177
Cdd:cd00180    71 EYCEGGSL-KDLLKENKGPL--SEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGT---VKLADFGLAKDLDS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 SG--LVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILlsgclpfygtkerlfegiikgkykmnprqwshisESA 255
Cdd:cd00180   145 DDslLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL----------------------------------EEL 190
                         250       260
                  ....*....|....*....|....*
gi 1039796143 256 KDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd00180   191 KDLIRRMLQYDPKKRPSAKELLEHL 215
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
10-281 1.53e-53

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: 187.16  E-value: 1.53e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLstegkrwisnLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd14184     1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHL----------IENEVSILRRVKHPNIIMLIEEMDT 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEN-SAPVKLGG 168
Cdd:cd14184    71 PAELYLVMELVKGGDL-FDAITSSTK---YTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDgTKSLKLGD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLgESGLVAggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT---KERLFEGIIKGKYKMNP 245
Cdd:cd14184   147 FGLATVV-EGPLYT--VCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSEnnlQEDLFDQILLGKLEFPS 223
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039796143 246 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14184   224 PYWDNITDSAKELISHMLQVNVEARYTAEQILSHPW 259
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
10-320 2.19e-53

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: 187.93  E-value: 2.19e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglsTEGKRWISNLKREAsichmlKHPHIVELLETYSS 89
Cdd:cd14175     1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSK--------RDPSEEIEILLRYG------QHPNIITLKDVYDD 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE-NSAPVKLGG 168
Cdd:cd14175    67 GKHVYLVTELMRGGELLDKILRQK----FFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESgNPESLRICD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQL-GESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG----TKERLFEGIIKGKYKM 243
Cdd:cd14175   143 FGFAKQLrAENGLLMT-PCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANgpsdTPEEILTRIGSGKFTL 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 244 NPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRyaykihLPETveQLRKFNARRkLKGAVLAAVSS 320
Cdd:cd14175   222 SGGNWNTVSDAAKDLVSKMLHVDPHQRLTAKQVLQHPWITQKDK------LPQS--QLNHQDVQL-VKGAMAATYSA 289
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-282 2.50e-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: 187.02  E-value: 2.50e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftssPGLSTEGKRwiSNLKREASICHMLKHPHIVELLETYSSD 90
Cdd:cd14169     4 VYELKEKLGEGAFSEVVLAQERGSQRLVALKCI--------PKKALRGKE--AMVENEIAVLRRINHENIVSLEDIYESP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFG 170
Cdd:cd14169    74 THLYLAMELVTGGELFDRIIERGS----YTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFEDSKIMISDFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAiQLGESGLVAGGrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQWS 249
Cdd:cd14169   150 LS-KIEAQGMLSTA-CGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDsELFNQILKAEYEFDSPYWD 227
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1039796143 250 HISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14169   228 DISESAKDFIRHLLERDPEKRFTCEQALQHPWI 260
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
9-282 2.62e-53

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: 186.70  E-value: 2.62e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSP-GLSTEgkrwisNLKREASICHMLKHPHIVELLETY 87
Cdd:cd14196     4 EDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRrGVSRE------EIEREVSILRQVLHPNIITLHDVY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAP-VKL 166
Cdd:cd14196    78 ENRTDVVLILELVSGGEL-FDFLAQKES---LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPhIKL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAIQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNP 245
Cdd:cd14196   154 IDFGLAHEI-EDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGdTKQETLANITAVSYDFDE 232
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1039796143 246 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14196   233 EFFSHTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
12-282 2.95e-53

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: 186.20  E-value: 2.95e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglstEGKRWISNlkrEASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14087     3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKC---------RGREVCES---ELNVLRRVRHTNIIQLIEVFETKE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGV 171
Cdd:cd14087    71 RVYMVMELATGGELFDRIIAKGS----FTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDSKIMITDFGL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQL--GESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQW 248
Cdd:cd14087   147 ASTRkkGPNCLMKT-TCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDdNRTRLYRQILRAKYSYSGEPW 225
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796143 249 SHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14087   226 PSVSNLAKDFIDRLLTVNPGERLSATQALKHPWI 259
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
9-282 4.06e-53

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: 186.38  E-value: 4.06e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSP-GLSTEgkrwisNLKREASICHMLKHPHIVELLETY 87
Cdd:cd14194     4 DDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRrGVSRE------DIEREVSILKEIQHPNVITLHEVY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAP-VKL 166
Cdd:cd14194    78 ENKTDVILILELVAGGEL-FDFLAEKES---LTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPrIKI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAIQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNP 245
Cdd:cd14194   154 IDFGLAHKI-DFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGdTKQETLANVSAVNYEFED 232
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1039796143 246 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14194   233 EYFSNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
12-277 6.33e-53

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: 185.48  E-value: 6.33e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvAKFTSSPGLstegkrwISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14014     2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLR-PELAEDEEF-------RERFLREARALARLSHPNIVRVYDVGEDDG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd14014    74 RPYIVMEYVEGGSL-ADLLRERGP---LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGR---VKLTDFGI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGL-VAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWS 249
Cdd:cd14014   147 ARALGDSGLtQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGdSPAAVLAKHLQEAPPPPSPLNP 226
                         250       260
                  ....*....|....*....|....*...
gi 1039796143 250 HISESAKDLVRRMLMLDPAERITVYEAL 277
Cdd:cd14014   227 DVPPALDAIILRALAKDPEERPQSAAEL 254
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
9-283 1.35e-52

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: 184.82  E-value: 1.35e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSP-GLSTEgkrwisNLKREASICHMLKHPHIVELLETY 87
Cdd:cd14195     4 EDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRrGVSRE------EIEREVNILREIQHPNIITLHDIF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAP-VKL 166
Cdd:cd14195    78 ENKTDVVLILELVSGGEL-FDFLAEKES---LTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPrIKL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAIQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNP 245
Cdd:cd14195   154 IDFGIAHKI-EAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGeTKQETLTNISAVNYDFDE 232
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039796143 246 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd14195   233 EYFSNTSELAKDFIRRLLVKDPKKRMTIAQSLEHSWIK 270
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
8-282 2.20e-52

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: 184.09  E-value: 2.20e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYEL-CEVIGKGPFSVVRRCINRETGQQFAvkivdvAKFTSspgLSTEGKRWISNLKREASICHMLK-HPHIVELLE 85
Cdd:cd14106     5 INEVYTVeSTPLGRGKFAVVRKCIHKETGKEYA------AKFLR---KRRRGQDCRNEILHEIAVLELCKdCPRVVNLHE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  86 TYSSDGMLYMVFEFMDGAdlcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVK 165
Cdd:cd14106    76 VYETRSELILILELAAGG----ELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGDIK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 166 LGGFGVAIQLGESGLVaggR--VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYK 242
Cdd:cd14106   152 LCDFGISRVIGEGEEI---ReiLGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGdDKQETFLNISQCNLD 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039796143 243 MNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14106   229 FPEELFKDVSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
12-270 2.64e-52

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 190.61  E-value: 2.64e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvAKFTSSPglstegkRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLR-PELAADP-------EARERFRREARALARLNHPNIVRVYDVGEEDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:COG0515    81 RPYLVMEYVEGESLA-DLLRRRGP---LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGR---VKLIDFGI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGL-VAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWS 249
Cdd:COG0515   154 ARALGGATLtQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGdSPAELLRAHLREPPPPPSELRP 233
                         250       260
                  ....*....|....*....|.
gi 1039796143 250 HISESAKDLVRRMLMLDPAER 270
Cdd:COG0515   234 DLPPALDAIVLRALAKDPEER 254
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
9-313 3.07e-52

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: 184.87  E-value: 3.07e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftssPGLSTEGKRwiSNLKREASICHMLKHPHIVELLETYS 88
Cdd:cd14168     9 KKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCI--------PKKALKGKE--SSIENEIAVLRKIKHENIVALEDIYE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRadaGFvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGG 168
Cdd:cd14168    79 SPNHLYLVMQLVSGGELFDRIVEK---GF-YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEESKIMISD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGeSGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQ 247
Cdd:cd14168   155 FGLSKMEG-KGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDsKLFEQILKADYEFDSPY 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 248 WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHlpETVE-QLRKFNARRKLKGA 313
Cdd:cd14168   234 WDDISDSAKDFIRNLMEKDPNKRYTCEQALRHPWIAGDTALCKNIH--ESVSaQIRKNFAKSKWRQA 298
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
8-284 4.82e-52

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: 183.58  E-value: 4.82e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakfTSSPGLSTEGkrwISNLkREASI--CHMLK----HPHIV 81
Cdd:cd14182     1 FYEKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDI---TGGGSFSPEE---VQEL-REATLkeIDILRkvsgHPNII 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  82 ELLETYSSDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENs 161
Cdd:cd14182    74 QLKDTYETNTFFFLVFDLMKKGELFDYLTEKV----TLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMN- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 162 apVKLGGFGVAIQLGEsGLVAGGRVGTPHFMAPEVVK------REPYGKPVDVWGCGVILFILLSGCLPFYGTKERL-FE 234
Cdd:cd14182   149 --IKLTDFGFSCQLDP-GEKLREVCGTPGYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLmLR 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039796143 235 GIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd14182   226 MIMSGNYQFGSPEWDDRSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQQ 275
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
18-281 9.41e-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: 181.56  E-value: 9.41e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstegKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIK--------RKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLCFEIVKRadagFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 177
Cdd:cd05123    73 DYVPGGELFSHLSKE----GRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGH---IKLTDFGLAKELSS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnPrqwSHISESAK 256
Cdd:cd05123   146 DGDRTYTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAeNRKEIYEKILKSPLKF-P---EYVSPEAK 221
                         250       260
                  ....*....|....*....|....*...
gi 1039796143 257 DLVRRMLMLDPAERIT---VYEALNHPW 281
Cdd:cd05123   222 SLISGLLQKDPTKRLGsggAEEIKAHPF 249
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
11-283 1.79e-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: 181.25  E-value: 1.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglstegKRwISNLKREASICHMLKHPHIVELLETYSSD 90
Cdd:cd06614     1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRK-----------QN-KELIINEILIMKECKHPNIVDYYDSYLVG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLCfEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFG 170
Cdd:cd06614    69 DELWVVMEYMDGGSLT-DIITQNPVRM--NESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGS---VKLADFG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEGIIKGKYKM-NPRQ 247
Cdd:cd06614   143 FAAQLTKEKSKRNSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPplRALFLITTKGIPPLkNPEK 222
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039796143 248 WSHiseSAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd06614   223 WSP---EFKDFLNKCLVKDPEKRPSAEELLQHPFLK 255
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
11-282 8.45e-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: 179.32  E-value: 8.45e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsspglstEGKRWISNLKREASICHMLKHPHIVELLETYSSD 90
Cdd:cd05122     1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINL-----------ESKEKKESILNEIAILKKCKHPNIVKYYGSYLKK 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLCfEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFG 170
Cdd:cd05122    70 DELWIVMEFCSGGSLK-DLLKNTNKTL--TEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSD---GEVKLIDFG 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY--GTKERLFEGIIKGKYKM-NPRQ 247
Cdd:cd05122   144 LSAQL-SDGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSelPPMKALFLIATNGPPGLrNPKK 222
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1039796143 248 WshiSESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd05122   223 W---SKEFKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
12-281 1.59e-50

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: 179.33  E-value: 1.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvAKFtsspgLSTEGKrwISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd05581     3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLD-KRH-----IIKEKK--VKYVTIEKEVLSRLAHPGIVKLYYTFQDES 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd05581    75 KLYFVLEYAPNGDLLEYIRKYGS----LDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMH---IKITDFGT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGR-----------------VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERL-F 233
Cdd:cd05581   148 AKVLGPDSSPESTKgdadsqiaynqaraasfVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLtF 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 234 EGIIKGKYKMNPrqwsHISESAKDLVRRMLMLDPAERITV-----YEAL-NHPW 281
Cdd:cd05581   228 QKIVKLEYEFPE----NFPPDAKDLIQKLLVLDPSKRLGVnenggYDELkAHPF 277
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
8-356 2.00e-50

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: 180.99  E-value: 2.00e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglsTEGKRWISNLKREAsichmlKHPHIVELLETY 87
Cdd:cd14176    17 FTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK--------RDPTEEIEILLRYG------QHPNIITLKDVY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE-NSAPVKL 166
Cdd:cd14176    83 DDGKYVYVVTELMKGGELLDKILRQK----FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgNPESIRI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAIQL-GESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG----TKERLFEGIIKGKY 241
Cdd:cd14176   159 CDFGFAKQLrAENGLLMT-PCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANgpddTPEEILARIGSGKF 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 242 KMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRyaykihLPETveQLRKFNARRKLKGAVLAAVSSH 321
Cdd:cd14176   238 SLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQ------LPQY--QLNRQDAPHLVKGAMAATYSAL 309
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1039796143 322 KFNsfygdppeelPDFSEDPTSSGLLAAERAVSQV 356
Cdd:cd14176   310 NRN----------QSPVLEPVGRSTLAQRRGIKKI 334
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
8-320 4.15e-50

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: 178.67  E-value: 4.15e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstegkRWISNLKREAsichmlKHPHIVELLETY 87
Cdd:cd14177     2 FTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPS--------EEIEILMRYG------QHPNIITLKDVY 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSA-PVKL 166
Cdd:cd14177    68 DDGRYVYLVTELMKGGELLDRILRQK----FFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANAdSIRI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAIQL-GESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG----TKERLFEGIIKGKY 241
Cdd:cd14177   144 CDFGFAKQLrGENGLLL-TPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANgpndTPEEILLRIGSGKF 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 242 KMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRyaykihLPEtvEQLRKFNARRKLKGAVLAAVSS 320
Cdd:cd14177   223 SLSGGNWDTVSDAAKDLLSHMLHVDPHQRYTAEQVLKHSWIACRDQ------LPH--YQLNRQDAPHLVKGAMAATYSA 293
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
8-286 7.86e-50

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: 177.90  E-value: 7.86e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstegkRWISNLKREAsichmlKHPHIVELLETY 87
Cdd:cd14178     1 FTDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPS--------EEIEILLRYG------QHPNIITLKDVY 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE-NSAPVKL 166
Cdd:cd14178    67 DDGKFVYLVMELMRGGELLDRILRQK----CFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESgNPESIRI 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAIQL-GESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG----TKERLFEGIIKGKY 241
Cdd:cd14178   143 CDFGFAKQLrAENGLLMT-PCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANgpddTPEEILARIGSGKY 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039796143 242 KMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERD 286
Cdd:cd14178   222 ALSGGNWDSISDAAKDIVSKMLHVDPHQRLTAPQVLRHPWIVNRE 266
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
12-282 4.14e-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: 174.35  E-value: 4.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdVAKFTsspgLSTEGKRWISNLKReasICHMLKHPHIVELLE--TYSS 89
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKI-KNDFR----HPKAALREIKLLKH---LNDVEGHPNIVKLLDvfEHRG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMdGADLCfEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLasKENSAPVKLGGF 169
Cdd:cd05118    73 GNHLCLVFELM-GMNLY-ELIKDYPRGL--PLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILI--NLELGQLKLADF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGLVagGRVGTPHFMAPEVVKR-EPYGKPVDVWGCGVILFILLSGclpfygtkERLFEGiikgkyKMNPRQW 248
Cdd:cd05118   147 GLARSFTSPPYT--PYVATRWYRAPEVLLGaKPYGSSIDIWSLGCILAELLTG--------RPLFPG------DSEVDQL 210
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1039796143 249 SHI-----SESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd05118   211 AKIvrllgTPEALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
18-286 1.75e-48

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: 173.17  E-value: 1.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAkftsspglSTEGKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd05579     1 ISRGAYGRVYLAKKKSTGDLYAIKVIKKR--------DMIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADL--------CFEivkradagfvysEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGF 169
Cdd:cd05579    73 EYLPGGDLysllenvgALD------------EDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDA---NGHLKLTDF 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GvaiqLGESGLVAGGR-------------------VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TK 229
Cdd:cd05579   138 G----LSKVGLVRRQIklsiqkksngapekedrriVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAeTP 213
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 230 ERLFEGIIKGKYkmNPRQWSHISESAKDLVRRMLMLDPAERI---TVYEALNHPWLKERD 286
Cdd:cd05579   214 EEIFQNILNGKI--EWPEDPEVSDEAKDLISKLLTPDPEKRLgakGIEEIKNHPFFKGID 271
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
10-282 2.33e-48

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: 173.67  E-value: 2.33e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELC-EVIGKGPFSVVRRCINRETGQQFAVKIVDvakftSSPGLSTegkrwiSNLKREASICHMLK-HPHIVELLETY 87
Cdd:cd14173     1 DVYQLQeEVLGEGAYARVQTCINLITNKEYAVKIIE-----KRPGHSR------SRVFREVEMLYQCQgHRNVLELIEFF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLG 167
Cdd:cd14173    70 EEEDKFYLVFEKMRGGSILSHIHRRRH----FNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKIC 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GF--GVAIQL-GESGLVAGGRVGTP----HFMAPEVVKR-----EPYGKPVDVWGCGVILFILLSGCLPFYG-------- 227
Cdd:cd14173   146 DFdlGSGIKLnSDCSPISTPELLTPcgsaEYMAPEVVEAfneeaSIYDKRCDLWSLGVILYIMLSGYPPFVGrcgsdcgw 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039796143 228 --------TKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14173   226 drgeacpaCQNMLFESIQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
10-282 4.17e-48

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: 172.13  E-value: 4.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKivdvaKFtsspgLSTEGKRWISNLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd14088     1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCK-----KF-----LKRDGRKVRKAAKNEINILKMVKHPNILQLVDVFET 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLcFEIVkrADAGFvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGF 169
Cdd:cd14088    71 RKEYFIFLELATGREV-FDWI--LDQGY-YSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSKIVISDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQlgESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE---------RLFEGIIKGK 240
Cdd:cd14088   147 HLAKL--ENGLIKE-PCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEeddyenhdkNLFRKILAGD 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1039796143 241 YKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14088   224 YEFDSPYWDDISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
10-282 5.72e-48

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: 171.71  E-value: 5.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELC-EVIGKGPFSVVRRCINRETGQQFAVKIVdvakfTSSPGLSTEgkrwiSNLKREASIChmlkhPHIVELLETYS 88
Cdd:cd14172     3 DDYKLSkQVLGLGVNGKVLECFHRRTGQKCALKLL-----YDSPKARRE-----VEHHWRASGG-----PHIVHILDVYE 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 ----SDGMLYMVFEFMDGADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPV 164
Cdd:cd14172    68 nmhhGKRCLLIIMECMEGGELFSRIQERGDQAF--TEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 165 KLGGFGVAIQLGESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY---------GTKERlfeg 235
Cdd:cd14172   146 KLTDFGFAKETTVQNALQ-TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYsntgqaispGMKRR---- 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1039796143 236 IIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14172   221 IRMGQYGFPNPEWAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
12-282 1.19e-47

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: 170.29  E-value: 1.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspgLSTEGKrwiSNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14074     5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTK------LDDVSK---AHLFQEVRCMKLVQHPNVVRLYEVIDTQT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLGGFGV 171
Cdd:cd14074    76 KLYLILELGDGGDM-YDYIMKHENGL--NEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGL--VKLTDFGF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLgESGLVAGGRVGTPHFMAPEVVKREPYGKP-VDVWGCGVILFILLSGCLPFY--GTKERLFEgIIKGKYKMNPrqw 248
Cdd:cd14074   151 SNKF-QPGEKLETSCGSLAYSAPEILLGDEYDAPaVDIWSLGVILYMLVCGQPPFQeaNDSETLTM-IMDCKYTVPA--- 225
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796143 249 sHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14074   226 -HVSPECKDLIRRMLIRDPKKRASLEEIENHPWL 258
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
10-284 1.51e-47

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: 170.56  E-value: 1.51e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglsTEGKRWIsnLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd14183     6 ERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSK--------CRGKEHM--IQNEVSILRRVKHPNIVLLIEEMDM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLL-ASKENSAPVKLGG 168
Cdd:cd14183    76 PTELYLVMELVKGGDL-FDAITSTNK---YTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyEHQDGSKSLKLGD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIqlgesglVAGGRV----GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT---KERLFEGIIKGKY 241
Cdd:cd14183   152 FGLAT-------VVDGPLytvcGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSgddQEVLFDQILMGQV 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1039796143 242 KMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd14183   225 DFPSPYWDNVSDSAKELITMMLQVDVDQRYSALQVLEHPWVND 267
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
10-283 1.60e-47

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: 171.37  E-value: 1.60e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELC-EVIGKGPFSVVRRCINRETGQQFAVKIVDvakftSSPGLSTegkrwiSNLKREASICHMLK-HPHIVELLETY 87
Cdd:cd14174     1 DLYRLTdELLGEGAYAKVQGCVSLQNGKEYAVKIIE-----KNAGHSR------SRVFREVETLYQCQgNKNILELIEFF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLG 167
Cdd:cd14174    70 EDDTRFYLVFEKLRGGSILAHIQKRKH----FNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSPVKIC 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GF--GVAIQLGESGL-VAGGRVGTP----HFMAPEVV-----KREPYGKPVDVWGCGVILFILLSGCLPFYGT------- 228
Cdd:cd14174   146 DFdlGSGVKLNSACTpITTPELTTPcgsaEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgw 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 229 ---------KERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd14174   226 drgevcrvcQNKLFESIQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
12-282 1.80e-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: 170.32  E-value: 1.80e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIV-----DVAKFTSSPGLSTEGKRWISNLkREASICHMLKHPHIVELLET 86
Cdd:cd14077     3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIprasnAGLKKEREKRLEKEISRDIRTI-REAALSSLLNHPHICRLRDF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKL 166
Cdd:cd14077    82 LRTPNHYYMLFEYVDGGQLLDYIISHGK----LKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGN---IKI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 ggfgvaIQLGESGLVAGGRV-----GTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKG 239
Cdd:cd14077   155 ------IDFGLSNLYDPRRLlrtfcGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENmPALHAKIKKG 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1039796143 240 KYKMNprqwSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14077   229 KVEYP----SYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
12-282 2.88e-47

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: 169.29  E-value: 2.88e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRC--INRETGQQFAVKIVDVAKftsSPglstegKRWISN-LKREASICHMLKHPHIVELLETYS 88
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKKK---AP------KDFLEKfLPRELEILRKLRHPNIIQVYSIFE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLcFEIVKRAdaGFVySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGG 168
Cdd:cd14080    73 RGSKVFIFMEYAEHGDL-LEYIQKR--GAL-SESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNN---VKLSD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGEsglvAGGRV------GTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGK 240
Cdd:cd14080   146 FGFARLCPD----DDGDVlsktfcGSAAYAAPEILQGIPYdPKKYDIWSLGVILYIMLCGSMPFDDSNiKKMLKDQQNRK 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1039796143 241 YKMNPRQWsHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14080   222 VRFPSSVK-KLSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
8-283 4.23e-47

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: 170.82  E-value: 4.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELC---EVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglstegKRWISNLKREAS---ICHmlKHPHIV 81
Cdd:cd14180     1 FFQCYELDleePALGEGSFSVCRKCRHRQSGQEYAVKIIS--------------RRMEANTQREVAalrLCQ--SHPNIV 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  82 ELLETYSSDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENS 161
Cdd:cd14180    65 ALHEVLHDQYHTYLVMELLRGGELLDRIKKKA----RFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDG 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 162 APVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEG------ 235
Cdd:cd14180   141 AVLKVIDFGFARLRPQGSRPLQTPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKMFHNhaadim 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039796143 236 --IIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd14180   221 hkIKEGDFSLEGEAWKGVSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQ 270
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
18-282 4.87e-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: 169.95  E-value: 4.87e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVdvakfTSSPGLSTEgkrwiSNLKREASichmlKHPHIVELLETYSSD------- 90
Cdd:cd14171    14 LGTGISGPVRVCVKKSTGERFALKIL-----LDRPKARTE-----VRLHMMCS-----GHPNIVQIYDVYANSvqfpges 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 ---GMLYMVFEFMDGADLCFEIVKRAdaGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLG 167
Cdd:cd14171    79 sprARLLIVMELMEGGELFDRISQHR--HF--TEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAPIKLC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVAiqlgesgLVAGGRVGTPHF----MAPEVV------KRE-----------PYGKPVDVWGCGVILFILLSGCLPFY 226
Cdd:cd14171   155 DFGFA-------KVDQGDLMTPQFtpyyVAPQVLeaqrrhRKErsgiptsptpyTYDKSCDMWSLGVIIYIMLCGYPPFY 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 227 GT------KERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14171   228 SEhpsrtiTKDMKRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
12-282 6.53e-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: 169.20  E-value: 6.53e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvaKFTSSpglsTEGkrwI-SNLKREASICHMLKHPHIVELLETYSSD 90
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKI---RLDNE----EEG---IpSTALREISLLKELKHPNIVKLLDVIHTE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDgADLcFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFG 170
Cdd:cd07829    71 NKLYLVFEYCD-QDL-KKYLDKRPGPL--PPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGV---LKLADFG 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLGESGLVAGGRVGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFE---------- 234
Cdd:cd07829   144 LARAFGIPLRTYTHEVVTLWYRAPEILLGSKhYSTAVDIWSVGCIFAELITGKPLFPGDSEidqlfKIFQilgtpteesw 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 235 -GIIK-GKYKMNPRQWSH---------ISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd07829   224 pGVTKlPDYKPTFPKWPKndlekvlprLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
12-282 3.30e-46

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: 166.19  E-value: 3.30e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEGKrwisnLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14099     3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKP---KQREK-----LKSEIKIHRSLKHPNIVKFHDCFEDEE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEfmdgadLC-----FEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKL 166
Cdd:cd14099    75 NVYILLE------LCsngslMELLKRRKA---LTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMN---VKI 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAIQLGESGLVAGGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMN 244
Cdd:cd14099   143 GDFGLAARLEYDGERKKTLCGTPNYIAPEVLeKKKGHSFEVDIWSLGVILYTLLVGKPPFETsDVKETYKRIKKNEYSFP 222
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039796143 245 PRqwSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14099   223 SH--LSISDEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
11-282 5.44e-46

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: 166.18  E-value: 5.44e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglstegkrwISNLKREASICHMLKHPHIVELLETYSSD 90
Cdd:cd14097     2 IYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSA---------VKLLEREVDILKHVNHAHIIHLEEVFETP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLCfEIVKRADagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASK--ENSAP--VKL 166
Cdd:cd14097    73 KRMYLVMELCEDGELK-ELLLRKG---FFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSiiDNNDKlnIKV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAIQ---LGESGLVAggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYK 242
Cdd:cd14097   149 TDFGLSVQkygLGEDMLQE--TCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAkSEEKLFEEIRKGDLT 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039796143 243 MNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14097   227 FTQSVWQSVSDAAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
16-281 1.16e-45

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: 164.89  E-value: 1.16e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFtsspglSTEGKrwiSNLKREASICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd14082     9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRF------PTKQE---SQLRNEVAILQQLSHPGVVNLECMFETPERVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLcfEIVKRADAGFVySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQL 175
Cdd:cd14082    80 VMEKLHGDML--EMILSSEKGRL-PERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQVKLCDFGFARII 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GESGLvaggR---VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFyGTKERLFEGIIKGKYKMNPRQWSHIS 252
Cdd:cd14082   157 GEKSF----RrsvVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-NEDEDINDQIQNAAFMYPPNPWKEIS 231
                         250       260
                  ....*....|....*....|....*....
gi 1039796143 253 ESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14082   232 PDAIDLINNLLQVKMRKRYSVDKSLSHPW 260
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
12-282 2.30e-45

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: 163.72  E-value: 2.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstegkrwisNLK---REASICHMLKHPHIVELLETYS 88
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEE------------NLKkiyREVQIMKMLNHPHIIKLYQVME 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGG 168
Cdd:cd14071    70 TKDMLYLVTEYASNGEIFDYLAQHGR----MSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMN---IKIAD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAiQLGESGLVAGGRVGTPHFMAPEVVKREPYGKP-VDVWGCGVILFILLSGCLPFYGT-----KERLFEGIIKGKYK 242
Cdd:cd14071   143 FGFS-NFFKPGELLKTWCGSPPYAAPEVFEGKEYEGPqLDIWSLGVVLYVLVCGALPFDGStlqtlRDRVLSGRFRIPFF 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039796143 243 MnprqwshiSESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14071   222 M--------STDCEHLIRRMLVLDPSKRLTIEQIKKHKWM 253
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
11-282 2.41e-45

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: 163.55  E-value: 2.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglstegkrwISNLKREASICHMLKHPHIVELLETYSSD 90
Cdd:cd06627     1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSD---------LKSVMGEIDLLKKLNHPNIVKYIGSVKTK 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFG 170
Cdd:cd06627    72 DSLYIILEYVENGSLA-SIIKKFGK---FPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGL---VKLADFG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVW--GCGVILfiLLSGCLPFYGTK--ERLFEgIIKGKYkmnPR 246
Cdd:cd06627   145 VATKLNEVEKDENSVVGTPYWMAPEVIEMSGVTTASDIWsvGCTVIE--LLTGNPPYYDLQpmAALFR-IVQDDH---PP 218
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039796143 247 QWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd06627   219 LPENISPELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
12-282 2.44e-45

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: 163.71  E-value: 2.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstegKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14073     3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIED--------EQDMVRIRREIEIMSSLNHPHIIRIYEVFENKD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd14073    75 KIVIVMEYASGGELYDYISERR----RLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGN---AKIADFGL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AiQLGESGLVAGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYkmnpRQWS 249
Cdd:cd14073   148 S-NLYSKDKLLQTFCGSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDfKRLVKQISSGDY----REPT 222
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1039796143 250 HISEsAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14073   223 QPSD-ASGLIRWMLTVNPKRRATIEDIANHWWV 254
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
11-284 3.16e-45

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


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 164.26  E-value: 3.16e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkfTSSPGLstegkrwisnLKREASICHMLKHPHIVELLETYSSD 90
Cdd:cd14104     1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVK--GADQVL----------VKKEISILNIARHRNILRLHESFESH 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLcFEIVkrADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGFG 170
Cdd:cd14104    69 EELVMIFEFISGVDI-FERI--TTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSY-IKIIEFG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWS 249
Cdd:cd14104   145 QSRQL-KPGDKFRLQYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAeTNQQTIENIRNAEYAFDDEAFK 223
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1039796143 250 HISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd14104   224 NISIEALDFVDRLLVKERKSRMTAQEALNHPWLKQ 258
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
18-282 6.41e-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: 162.43  E-value: 6.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGlsteGKrwiSNLKREASICHMLKHPHIVELLETYSSD--GMLYM 95
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRIPN----GE---ANVKREIQILRRLNHRNVIKLVDVLYNEekQKLYM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGAdLCFEIVKRADAGFVYSEAvaSHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQL 175
Cdd:cd14119    74 VMEYCVGG-LQEMLDSAPDKRLPIWQA--HGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGT---LKISDFGVAEAL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 geSGLVAGGRV----GTPHFMAPEVVKREPY--GKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPrqw 248
Cdd:cd14119   148 --DLFAEDDTCttsqGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIyKLFENIGKGEYTIPD--- 222
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796143 249 sHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14119   223 -DVDPDLQDLLRGMLEKDPEKRFTIEQIRQHPWF 255
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
17-286 1.30e-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: 161.99  E-value: 1.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKIVdvakftssPGLSTEGKRwiSNLKREASICHMLKHPHIVELLETYSSDGMLYMV 96
Cdd:cd06623     8 VLGQGSSGVVYKVRHKPTGKIYALKKI--------HVDGDEEFR--KQLLRELKTLRSCESPYVVKCYGAFYKEGEISIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCH-DNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQL 175
Cdd:cd06623    78 LEYMDGGSLA-DLLKKVGK---IPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLLINSKGE---VKIADFGISKVL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER----LFEGIIKG-KYKMNPRQWsh 250
Cdd:cd06623   151 ENTLDQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPsffeLMQAICDGpPPSLPAEEF-- 228
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039796143 251 iSESAKDLVRRMLMLDPAERITVYEALNHPWLKERD 286
Cdd:cd06623   229 -SPEFRDFISACLQKDPKKRPSAAELLQHPFIKKAD 263
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
12-282 2.49e-44

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: 160.88  E-value: 2.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstegKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd05578     2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIE--------KDSVRNVLNELEILQELEHPFLVNLWYSFQDEE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGV 171
Cdd:cd05578    74 DMYMVVDLLLGGDLRYHLQQKV----KFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILL---DEQGHVHITDFNI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHI 251
Cdd:cd05578   147 ATKL-TDGTLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRAKFETASVLYPAGW 225
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1039796143 252 SESAKDLVRRMLMLDPAERITVYEAL-NHPWL 282
Cdd:cd05578   226 SEEAIDLINKLLERDPQKRLGDLSDLkNHPYF 257
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
16-284 3.15e-44

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: 162.52  E-value: 3.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglstegKRWISNLKREASICHMLK-HPHIVELLETYSSDGMLY 94
Cdd:cd14179    13 KPLGEGSFSICRKCLHKKTNQEYAVKIVS--------------KRMEANTQREIAALKLCEgHPNIVKLHEVYHDQLHTF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  95 MVFEFMDGADLcFEIVKRADagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQ 174
Cdd:cd14179    79 LVMELLKGGEL-LERIKKKQ---HFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSEIKIIDFGFARL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 175 LGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF--------YGTKERLFEGIIKGKYKMNPR 246
Cdd:cd14179   155 KPPDNQPLKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFqchdksltCTSAEEIMKKIKQGDFSFEGE 234
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039796143 247 QWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd14179   235 AWKNVSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQD 272
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
9-282 5.52e-44

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: 159.86  E-value: 5.52e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSS-PGLSTEgkrwISNLKReasichmLKHPHIVELLETY 87
Cdd:cd14078     2 LKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALGDDlPRVKTE----IEALKN-------LSHQHICRLYHVI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLG 167
Cdd:cd14078    71 ETDNKIFMVLEYCPGGELFDYIVAKDR----LSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQN---LKLI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGvaiqlgesgLVA---GGR-------VGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEG 235
Cdd:cd14078   144 DFG---------LCAkpkGGMdhhletcCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNvMALYRK 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1039796143 236 IIKGKYKmNPRqWshISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14078   215 IQSGKYE-EPE-W--LSPSSKLLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
10-282 1.38e-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: 158.57  E-value: 1.38e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKivdvakFTSSPGLStegKRWISNLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd14002     1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALK------FIPKRGKS---EKELRNLRQEIEILRKLNHPNIIEMLDSFET 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGaDLcFEIVkrADAGfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGF 169
Cdd:cd14002    72 KKEFVVVTEYAQG-EL-FQIL--EDDG-TLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKG---GVVKLCDF 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKgkykmNPRQW 248
Cdd:cd14002   144 GFARAMSCNTLVLTSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSiYQLVQMIVK-----DPVKW 218
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1039796143 249 -SHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14002   219 pSNMSPEFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
PDZ_MPP1-like cd10830
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 ...
495-575 1.40e-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: 1.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 495 RLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIV 574
Cdd:cd10830     1 RLVQFEKNTEEPMGITLKLNEKQSCIVARILHGGMIHRQGSLHVGDEILEINGKSVTNHSVDQLQKMLKETKGMVSLKVI 80

                  .
gi 1039796143 575 P 575
Cdd:cd10830    81 P 81
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
12-282 1.76e-43

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: 158.45  E-value: 1.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglstegkrwISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14072     2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSS---------LQKLFREVRIMKILNHPNIVKLFEVIETEK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRADAgfvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd14072    73 TLYLVMEYASGGEVFDYLVAHGRM----KEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMN---IKIADFGF 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQlgesgLVAGGRV----GTPHFMAPEVVKREPYGKP-VDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnP 245
Cdd:cd14072   146 SNE-----FTPGNKLdtfcGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGqNLKELRERVLRGKYRI-P 219
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1039796143 246 rqwSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14072   220 ---FYMSTDCENLLKKFLVLNPSKRGTLEQIMKDRWM 253
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
16-284 1.96e-43

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: 159.81  E-value: 1.96e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIV-DVAKftsspglsteGKRWISnLKREASIChmlkhPHIVELLETY----SSD 90
Cdd:cd14170     8 QVLGLGINGKVLQIFNKRTQEKFALKMLqDCPK----------ARREVE-LHWRASQC-----PHIVRIVDVYenlyAGR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFG 170
Cdd:cd14170    72 KCLLIVMECLDGGELFSRIQDRGDQAF--TEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLGESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY---------GTKERlfegIIKGKY 241
Cdd:cd14170   150 FAKETTSHNSLTT-PCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYsnhglaispGMKTR----IRMGQY 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1039796143 242 KMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd14170   225 EFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQ 267
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
12-282 4.20e-43

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: 157.50  E-value: 4.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspgLSTEGKRWISnlkREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14075     4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTK------LDQKTQRLLS---REISSMEKLHHPNIIRLYEVVETLS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGV 171
Cdd:cd14075    75 KLHLVMEYASGGELYTKISTEGK----LSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASN---NCVKVGDFGF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLgESGLVAGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnPrqwS 249
Cdd:cd14075   148 STHA-KRGETLNTFCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRAeTVAKLKKCILEGTYTI-P---S 222
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1039796143 250 HISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14075   223 YVSEPCQELIRGILQPVPSDRYSIDEIKNSEWL 255
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-280 5.70e-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: 157.32  E-value: 5.70e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglsTEGKRWIS--NLKREasichmLKHPHIVELLETY-- 87
Cdd:cd08217     2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSE-----KEKQQLVSevNILRE------LKHPNIVRYYDRIvd 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCfEIVKRADAGFVY-SEAVASHYMRQILEALRYCHDNN-----IIHRDVKPHCVLLASKENs 161
Cdd:cd08217    71 RANTTLYIVMEYCEGGDLA-QLIKKCKKENQYiPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNN- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 162 apVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGK 240
Cdd:cd08217   149 --VKLGDFGLARVLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANqLELAKKIKEGK 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039796143 241 YkmnPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd08217   227 F---PRIPSRYSSELNEVIKSMLNVDPDKRPSVEELLQLP 263
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
12-286 2.41e-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: 2.41e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstegKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd05580     3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIK--------LKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd05580    75 NLYMVMEYVPGGEL-FSLLRRSGR---FPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGH---IKITDFGF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGEsglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnPRqwsH 250
Cdd:cd05580   148 AKRVKD---RTYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDeNPMKIYEKILEGKIRF-PS---F 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1039796143 251 ISESAKDLVRRMLMLDPAERI-----TVYEALNHPWLKERD 286
Cdd:cd05580   221 FDPDAKDLIKRLLVVDLTKRLgnlknGVEDIKNHPWFAGID 261
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
12-282 2.57e-42

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: 156.32  E-value: 2.57e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGlSTEGKRWISnlkREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd07833     3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIK-----KFKESED-DEDVKKTAL---REVKVLRQLRHENIVNLKEAFRRKG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcfEIVKRADAGFVYsEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLasKENSApVKLGGFGV 171
Cdd:cd07833    74 RLYLVFEYVERTLL--ELLEASPGGLPP-DAVRS-YIWQLLQAIAYCHSHNIIHRDIKPENILV--SESGV-LKLCDFGF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVA-GGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE--RLFEgIIKGKYKMNPRQ 247
Cdd:cd07833   147 ARALTARPASPlTDYVATRWYRAPELlVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDidQLYL-IQKCLGPLPPSH 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039796143 248 W-----------------SHI-----------SESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd07833   226 QelfssnprfagvafpepSQPeslerrypgkvSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
16-282 7.63e-42

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: 154.10  E-value: 7.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIVdvaKFTSSPGLSTEGkrwISNLKREASICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd06632     6 QLLGSGSFGSVYEGFNGDTGDFFAVKEV---SLVDDDKKSRES---VKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQL 175
Cdd:cd06632    80 FLEYVPGGSI-HKLLQRYGA---FEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILV---DTNGVVKLADFGMAKHV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GESGLvAGGRVGTPHFMAPEVVKRE--PYGKPVDVW--GCGVILfiLLSGCLPFYGtkerlFEG---IIK-GKYKMNPRQ 247
Cdd:cd06632   153 EAFSF-AKSFKGSPYWMAPEVIMQKnsGYGLAVDIWslGCTVLE--MATGKPPWSQ-----YEGvaaIFKiGNSGELPPI 224
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1039796143 248 WSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd06632   225 PDHLSPDAKDFIRLCLQRDPEDRPTASQLLEHPFV 259
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
8-282 2.57e-41

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: 152.28  E-value: 2.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELCE-VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFtsspglstegkrwisnLKREASICHMLKHPHIVELLET 86
Cdd:cd14109     1 VRELYEIGEeDEKRAAQGAPFHVTERSTGRNFLAQLRYGDPF----------------LMREVDIHNSLDHPNIVQMHDA 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYMVFEFMD-GADLCFEIVKRADAgfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnsapVK 165
Cdd:cd14109    65 YDDEKLAVTVIDNLAsTIELVRDNLLPGKD--YYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDDK----LK 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 166 LGGFGVAIQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMN 244
Cdd:cd14109   139 LADFGQSRRL-LRGKLTTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDReTLTNVRSGKWSFD 217
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039796143 245 PRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14109   218 SSPLGNISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
18-281 3.34e-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: 152.51  E-value: 3.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAK------FTSSP---GLSTEGKRWISNLKR---EASICHMLKHPHIVELLE 85
Cdd:cd14118     2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKllkqagFFRRPpprRKPGALGKPLDPLDRvyrEIAILKKLDHPNVVKLVE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  86 TYS--SDGMLYMVFEFMDGADlcfeiVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSap 163
Cdd:cd14118    82 VLDdpNEDNLYMVFELVDKGA-----VMEVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLL-GDDGH-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 164 VKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVK--REPY-GKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGK 240
Cdd:cd14118   154 VKIADFGVSNEFEGDDALLSSTAGTPAFMAPEALSesRKKFsGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTD 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1039796143 241 YKMNPRQWShISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14118   234 PVVFPDDPV-VSEQLKDLILRMLDKNPSERITLPEIKEHPW 273
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
7-282 3.63e-41

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: 152.40  E-value: 3.63e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   7 LFEDVYELC--EVIGKGPFSVVRRCINRETGQQFAvkivdvAKFTSSpglSTEGKRWISNLKREASICHMLK-HPHIVEL 83
Cdd:cd14197     4 PFQERYSLSpgRELGRGKFAVVRKCVEKDSGKEFA------AKFMRK---RRKGQDCRMEIIHEIAVLELAQaNPWVINL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  84 LETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAP 163
Cdd:cd14197    75 HEVYETASEMILVLEYAAGGEIFNQCVADREEAF--KEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 164 VKLGGFGVAIQLGESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT-KERLFEGIIKGKYK 242
Cdd:cd14197   153 IKIVDFGLSRILKNSEELR-EIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDdKQETFLNISQMNVS 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039796143 243 MNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14197   232 YSEEEFEHLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
PDZ_MPP-like cd06726
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ...
495-575 4.50e-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: 145.10  E-value: 4.50e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 495 RLVQFQKNTDEPMGITLKMNElNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIV 574
Cdd:cd06726     1 RLVEFEKARDEPLGATIKMEE-DSVIVARILHGGMAHRSGLLHVGDEILEINGIPVSGKTVDELQKLLSSLSGSVTFKLI 79

                  .
gi 1039796143 575 P 575
Cdd:cd06726    80 P 80
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
12-304 5.33e-41

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: 152.01  E-value: 5.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsspglsTEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd06609     3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDL----------EEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADlCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGV 171
Cdd:cd06609    73 KLWIIMEYCGGGS-VLDLLKPG----PLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLS---EEGDVKLADFGV 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGcLPFYGTKER---LFEgIIKGKYKMNPRqw 248
Cdd:cd06609   145 SGQLTSTMSKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKG-EPPLSDLHPmrvLFL-IPKNNPPSLEG-- 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796143 249 SHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYkihLPETVEQLRKF 304
Cdd:cd06609   221 NKFSKPFKDFVELCLNKDPKERPSAKELLKHKFIKKAKKTSY---LTLLIERIKKW 273
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
18-282 6.30e-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: 6.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglstEGKRWISNLKREASICHMLK-HPHIVELLETYSSDGMLYMV 96
Cdd:cd14198    16 LGRGKFAVVRQCISKSTGQEYAAKFLKKRR---------RGQDCRAEILHEIAVLELAKsNPRVVNLHEVYETTSEIILI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMDGAD---LCFeivkrADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAI 173
Cdd:cd14198    87 LEYAAGGEifnLCV-----PDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFGMSR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 174 QLGESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT-KERLFEGIIKGKYKMNPRQWSHIS 252
Cdd:cd14198   162 KIGHACELR-EIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEdNQETFLNISQVNVDYSEETFSSVS 240
                         250       260       270
                  ....*....|....*....|....*....|
gi 1039796143 253 ESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14198   241 QLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
9-282 6.95e-41

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: 151.31  E-value: 6.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspGLSTEGKRwisNLKREASICHMLKHPHIVELLETYS 88
Cdd:cd14191     1 SDFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFK--------AYSAKEKE---NIRQEISIMNCLHHPKLVQCVDAFE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVkraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGG 168
Cdd:cd14191    70 EKANIVMVLEMVSGGELFERII---DEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTK-IKLID 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQ 247
Cdd:cd14191   146 FGLARRLENAGSLKV-LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDnETLANVTSATWDFDDEA 224
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1039796143 248 WSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14191   225 FDEISDDAKDFISNLLKKDMKARLTCTQCLQHPWL 259
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
18-281 9.50e-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: 150.84  E-value: 9.50e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVdvakftsspglsteGKRWISN------LKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCV--------------KKRHIVQtrqqehIFSEKEILEECNSPFIVKLYRTFKDKK 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGV 171
Cdd:cd05572    67 YLYMLMEYCLGGELWTILRDRG----LFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLL---DSNGYVKLVDFGF 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGeSGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE---RLFEGIIKGKYKMN-PRq 247
Cdd:cd05572   140 AKKLG-SGRKTWTFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEdpmKIYNIILKGIDKIEfPK- 217
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1039796143 248 wsHISESAKDLVRRMLMLDPAERITV----YEAL-NHPW 281
Cdd:cd05572   218 --YIDKNAKNLIKQLLRRNPEERLGYlkggIRDIkKHKW 254
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
12-282 1.05e-40

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: 150.74  E-value: 1.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspgLSTEGKRWISnlkREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14111     5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIVP---------YQAEEKQGVL---QEYEILKSLHHERIMALHEAYITPR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRadagFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGV 171
Cdd:cd14111    73 YLVLIAEFCSGKELLHSLIDR----FRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVT---NLNAIKIVDFGS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVA-GGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEG-IIKGKY---KMNPR 246
Cdd:cd14111   146 AQSFNPLSLRQlGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAkILVAKFdafKLYPN 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039796143 247 qwshISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14111   226 ----VSQSASLFLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
17-281 4.90e-40

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: 148.66  E-value: 4.90e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspgLSTEGKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYMV 96
Cdd:cd06625     7 LLGQGAFGQVYLCYDADTGRELAVKQVEIDP------INTEASKEVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLG 176
Cdd:cd06625    81 MEYMPGGSVKDEIKAYG----ALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGN---VKLGDFGASKRLQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 177 ESGLVAGGR--VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGtkerlFE---GIIK-GKYKMNPRQWSH 250
Cdd:cd06625   154 TICSSTGMKsvTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAE-----FEpmaAIFKiATQPTNPQLPPH 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1039796143 251 ISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd06625   229 VSEDARDFLSLIFVRNKKQRPSAEELLSHSF 259
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
12-280 1.64e-39

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: 147.15  E-value: 1.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTegkrwISNLKREASIchmlKHPHIVELLETYSSDG 91
Cdd:cd08530     2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKEREDS-----VNEIRLLASV----NHPNIIRYKEAFLDGN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd08530    73 RLCIVMEYAPFGDLSKLISKRKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDL---VKIGDLGI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AiQLGESGLvAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYkmnPRQWSH 250
Cdd:cd08530   150 S-KVLKKNL-AKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEArTMQELRYKVCRGKF---PPIPPV 224
                         250       260       270
                  ....*....|....*....|....*....|
gi 1039796143 251 ISESAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd08530   225 YSQDLQQIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
12-282 2.72e-39

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: 146.64  E-value: 2.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINReTGQQFAVKIVDVAKFTSSPGLStegkrwisNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14161     5 YEFLETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRIKDEQDLL--------HIRREIEIMSSLNHPHIISVYEVFENSS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd14161    76 KIVIVMEYASRGDLYDYISERQR----LSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGN---IKIADFGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AiQLGESGLVAGGRVGTPHFMAPEVVKREPYGKP-VDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYkmnpRQWS 249
Cdd:cd14161   149 S-NLYNQDKFLQTYCGSPLYASPEIVNGRPYIGPeVDSWSLGVLLYILVHGTMPFDGHDYKiLVKQISSGAY----REPT 223
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1039796143 250 HISEsAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14161   224 KPSD-ACGLIRWLLMVNPERRATLEDVASHWWV 255
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
16-282 5.17e-39

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: 145.83  E-value: 5.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIVdvakftsspglSTEGKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd14193    10 EILGGGRFGQVHKCEEKSSGLKLAAKII-----------KARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLCFEIVkraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnSAPVKLGGFGVAIQL 175
Cdd:cd14193    79 VMEYVDGGELFDRII---DENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSRE-ANQVKIIDFGLARRY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GESGLVaggRV--GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQWSHIS 252
Cdd:cd14193   155 KPREKL---RVnfGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDnETLNNILACQWDFEDEEFADIS 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 1039796143 253 ESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14193   232 EEAKDFISKLLIKEKSWRMSASEALKHPWL 261
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
16-281 8.51e-39

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: 144.74  E-value: 8.51e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVV----RRCINRETgqqFAVKIVDVAKFTSSpglSTEgkrwisNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14121     1 EKLGSGTYATVykayRKSGAREV---VAVKCVSKSSLNKA---STE------NLLTEIELLKKLKHPHIVELKDFQWDEE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsaPV-KLGGFG 170
Cdd:cd14121    69 HIYLIMEYCSGGDLSRFIRSRR----TLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYN--PVlKLADFG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLGESGLVAGGRvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQwS 249
Cdd:cd14121   143 FAQHLKPNDEAHSLR-GSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASrSFEELEEKIRSSKPIEIPTR-P 220
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1039796143 250 HISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14121   221 ELSADCRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
12-285 1.14e-38

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: 146.18  E-value: 1.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSP-GLStegkrwISNLkREASICHMLKHPHIVELLETYSSD 90
Cdd:cd07841     2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAKdGIN------FTAL-REIKLLQELKHPNIIGLLDVFGHK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGaDLcfEIVKRaDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFG 170
Cdd:cd07841    75 SNINLVFEFMET-DL--EKVIK-DKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASD---GVLKLADFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLGESGLVAGGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFE---------- 234
Cdd:cd07841   148 LARSFGSPNRKMTHQVVTRWYRAPELLfGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDidqlgKIFEalgtpteenw 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796143 235 -GIIKGKY-----KMNPRQWSHI----SESAKDLVRRMLMLDPAERITVYEALNHPWLKER 285
Cdd:cd07841   228 pGVTSLPDyvefkPFPPTPLKQIfpaaSDDALDLLQRLLTLNPNKRITARQALEHPYFSND 288
SH3_CASK cd12081
Src Homology 3 domain of Calcium/calmodulin-dependent Serine protein Kinase; CASK is a ...
599-660 1.53e-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: 1.53e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 599 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPEL 660
Cdd:cd12081     1 YVRAQFEYDPLKDDLIPCKQAGIRFRVGDILQIISKDDHNWWQAKLENSKNGTAGLIPSPEL 62
SH3_MPP1-like cd12035
Src Homology 3 domain of Membrane Protein, Palmitoylated 1 (or MAGUK p55 subfamily member 1) ...
599-660 1.71e-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: 1.71e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 599 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPEL 660
Cdd:cd12035     1 YVRAQFDYDPSKDDLIPCQQAGIAFKTGDILQIISKDDHNWWQARKPGASKEPAGLIPSPEL 62
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
12-278 4.33e-38

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: 143.18  E-value: 4.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspgLSTEGKRwiSNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd08224     2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFE------MMDAKAR--QDCLKEIDLLQQLNHPNIIKYLASFIENN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGV 171
Cdd:cd08224    74 ELNIVLELADAGDLSRLIKHFKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITA---NGVVKLGDLGL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE---RLFEGIIKGKYKmnPRQW 248
Cdd:cd08224   151 GRFFSSKTTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMnlySLCKKIEKCEYP--PLPA 228
                         250       260       270
                  ....*....|....*....|....*....|
gi 1039796143 249 SHISESAKDLVRRMLMLDPAERITVYEALN 278
Cdd:cd08224   229 DLYSQELRDLVAACIQPDPEKRPDISYVLD 258
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
11-282 4.53e-38

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: 143.11  E-value: 4.53e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLstegkrwisnlkREASICHMLKHPHIVELLETYSSD 90
Cdd:cd14107     3 VYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAF------------QERDILARLSHRRLTCLLDQFETR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSaPVKLGGFG 170
Cdd:cd14107    71 KTLILILELCSSEELLDRLFLKG----VVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRE-DIKICDFG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLGESGLvAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNPRQWS 249
Cdd:cd14107   146 FAQEITPSEH-QFSKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRaTLLNVAEGVVSWDTPEIT 224
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1039796143 250 HISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14107   225 HLSEDAKDFIKRVLQPDPEKRPSASECLSHEWF 257
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
9-282 7.62e-38

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: 142.40  E-value: 7.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsspglstegKRWISNLKREASICHMLKHPHIVELLETYS 88
Cdd:cd06612     2 EEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPV-------------EEDLQEIIKEISILKQCDSPYIVKYYGSYF 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCfEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGG 168
Cdd:cd06612    69 KNTDLWIVMEYCGAGSVS-DIMKITNKTL--TEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQ---AKLAD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEgiIKGK----YK 242
Cdd:cd06612   143 FGVSGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHpmRAIFM--IPNKppptLS 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039796143 243 mNPRQWshiSESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd06612   221 -DPEKW---SPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
9-282 8.02e-38

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: 142.31  E-value: 8.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDvYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvAKFTSSPGLstegkrwISNLKREASICHMLKHPHIVELLETYS 88
Cdd:cd14186     1 ED-FKVLNLLGKGSFACVYRARSLHTGLEVAIKMID-KKAMQKAGM-------VQRVRNEVEIHCQLKHPSILELYNYFE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGG 168
Cdd:cd14186    72 DSNYVYLVLEMCHNGEMSRYLKNRKKP---FTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMN---IKIAD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF-YGTKERLFEGIIKGKYKMNprq 247
Cdd:cd14186   146 FGLATQLKMPHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFdTDTVKNTLNKVVLADYEMP--- 222
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1039796143 248 wSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14186   223 -AFLSREAQDLIHQLLRKNPADRLSLSSVLDHPFM 256
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
5-282 1.13e-37

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: 142.04  E-value: 1.13e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   5 DVLFEDVYELceviGKGPFSVVRRCINRETGQQFAVKIVDvAKFTsspglstegKRwiSNLKREASICHMLKHPHIVELL 84
Cdd:cd14113     6 DSFYSEVAEL----GRGRFSVVKKCDQRGTKRAVATKFVN-KKLM---------KR--DQVTHELGVLQSLQHPQLVGLL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  85 ETYSSDGMLYMVFEFMDGADLCFEIVKradAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPV 164
Cdd:cd14113    70 DTFETPTSYILVLEMADQGRLLDYVVR---WGNLTEEKIRF-YLREILEALQYLHNCRIAHLDLKPENILVDQSLSKPTI 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 165 KLGGFGVAIQLGESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKM 243
Cdd:cd14113   146 KLADFGDAVQLNTTYYIH-QLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDeSVEETCLNICRLDFSF 224
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1039796143 244 NPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14113   225 PDDYFKGVSQKAKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
12-282 1.27e-37

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: 141.88  E-value: 1.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglSTEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14070     4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKK-------AKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETEN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd14070    77 SYYLVMELCPGGNLMHRIYDKKR----LEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDN---IKLIDFGL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAG--GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFygTKE-----RLFEGIIKGkyKMN 244
Cdd:cd14070   150 SNCAGILGYSDPfsTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPF--TVEpfslrALHQKMVDK--EMN 225
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039796143 245 PRQwSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14070   226 PLP-TDLSPGAISFLRSLLEPDPLKRPNIKQALANRWL 262
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
12-281 1.57e-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: 141.66  E-value: 1.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglstEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14665     2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIE------------RGEKIDENVQREIINHRSLRHPNIVRFKEVILTPT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcFEIVkrADAGfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkeNSAP-VKLGGFG 170
Cdd:cd14665    70 HLAIVMEYAAGGEL-FERI--CNAG-RFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDG--SPAPrLKICDFG 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAiqlgESGLVAG---GRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFEGIIKGKY 241
Cdd:cd14665   144 YS----KSSVLHSqpkSTVGTPAYIAPEVLLKKEYdGKIADVWSCGVTLYVMLVGAYPFEDPEEprnfrKTIQRILSVQY 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039796143 242 KMNprQWSHISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14665   220 SIP--DYVHISPECRHLISRIFVADPATRITIPEIRNHEW 257
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
12-282 1.75e-37

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: 141.39  E-value: 1.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEGKRWIsnlkREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRK-----MREEAI----DEARVLSKLNSPYVIKYYDSFVDKG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcFEIVKRaDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd08529    73 KLNIVMEYAENGDL-HSLIKS-QRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDN---VKIGDLGV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQWsh 250
Cdd:cd08529   148 AKILSDTTNFAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQgALILKIVRGKYPPISASY-- 225
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1039796143 251 iSESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd08529   226 -SQDLSQLIDSCLTKDYRQRPDTTELLRNPSL 256
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
18-282 2.15e-37

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: 141.29  E-value: 2.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRC--INRETGQQFAVKIvdvakFTSSPGLSTEgKRWISNLKREASICHMLKHPHIVELLE-TYSSDGMLY 94
Cdd:cd13994     1 IGKGATSVVRIVtkKNPRSGVLYAVKE-----YRRRDDESKR-KDYVKRLTSEYIISSKLHHPNIVKVLDlCQDLHGKWC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  95 MVFEFMDGADLCFEIVKRADAGFvysEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQ 174
Cdd:cd13994    75 LVMEYCPGGDLFTLIEKADSLSL---EEKDC-FFKQILRGVAYLHSHGIAHRDLKPENILLDEDGV---LKLTDFGTAEV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 175 LGESG----LVAGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFEGIIKGKYKMN 244
Cdd:cd13994   148 FGMPAekesPMSAGLCGSEPYMAPEVFTSGSYdGRAVDVWSCGIVLFALFTGRFPWRSAKKsdsayKAYEKSGDFTNGPY 227
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039796143 245 PRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd13994   228 EPIENLLPSECRRLIYRMLHPDPEKRITIDEALNDPWV 265
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
12-300 3.22e-37

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 142.65  E-value: 3.22e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglstegKRWISNLKR------EASICHMLKHPHIVELLE 85
Cdd:PTZ00263   20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLK--------------KREILKMKQvqhvaqEKSILMELSHPFIVNMMC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  86 TYSSDGMLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVK 165
Cdd:PTZ00263   86 SFQDENRVYFLLEFVVGGEL-FTHLRKAGR---FPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGH---VK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 166 LGGFGVAIQLGESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMn 244
Cdd:PTZ00263  159 VTDFGFAKKVPDRTFTL---CGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDdTPFRIYEKILAGRLKF- 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 245 PRqWshISESAKDLVRRMLMLDPAERI-----TVYEALNHPWLKERD---RYAYKIHLPETVEQ 300
Cdd:PTZ00263  235 PN-W--FDGRARDLVKGLLQTDHTKRLgtlkgGVADVKNHPYFHGANwdkLYARYYPAPIPVRV 295
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
12-282 3.90e-37

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: 140.48  E-value: 3.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELC--EVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsspglstEGKRWISNLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd14192     4 YAVCphEVLGGGRFGQVHKCTELSTGLTLAAKIIKV-----------KGAKEREEVKNEINIMNQLNHVNLIQLYDAFES 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLCFEIVkraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGF 169
Cdd:cd14192    73 KTNLTLIMEYVDGGELFDRIT---DESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQ-IKIIDF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLG--ESGLVaggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPR 246
Cdd:cd14192   149 GLARRYKprEKLKV---NFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGeTDAETMNNIVNCKWDFDAE 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039796143 247 QWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14192   226 AFENLSEEAKDFISRLLVKEKSCRMSATQCLKHEWL 261
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
17-271 6.84e-37

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: 141.77  E-value: 6.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFS---VVRRCINRETGQQFAVKIVDVAKFTSSpglstegKRWISNLKREASICHMLKHPHIVELLETYSSDGML 93
Cdd:cd05584     3 VLGKGGYGkvfQVRKTTGSDKGKIFAMKVLKKASIVRN-------QKDTAHTKAERNILEAVKHPFIVDLHYAFQTGGKL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  94 YMVFEFMDGADLcFEIVKRADagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAI 173
Cdd:cd05584    76 YLILEYLSGGEL-FMHLEREG---IFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGH---VKLTDFGLCK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 174 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPrqwsHIS 252
Cdd:cd05584   149 ESIHDGTVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAeNRKKTIDKILKGKLNLPP----YLT 224
                         250
                  ....*....|....*....
gi 1039796143 253 ESAKDLVRRMLMLDPAERI 271
Cdd:cd05584   225 NEARDLLKKLLKRNVSSRL 243
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
12-282 7.75e-37

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: 139.53  E-value: 7.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVD--------VAKFtsspglstegkrwisnLKREASICHMLKHPHIVEL 83
Cdd:cd14165     3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDkkkapddfVEKF----------------LPRELEILARLNHKSIIKT 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  84 LETY-SSDGMLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSA 162
Cdd:cd14165    67 YEIFeTSDGKVYIVMELGVQGDL-LEFIKLRGA---LPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLL---DKDF 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 163 PVKLGGFGVAIQL--GESGLVAGGRV--GTPHFMAPEVVKREPYGKPV-DVWGCGVILFILLSGCLPFYGTKERLFEGII 237
Cdd:cd14165   140 NIKLTDFGFSKRClrDENGRIVLSKTfcGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQ 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039796143 238 KgKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14165   220 K-EHRVRFPRSKNLTSECKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
18-283 1.01e-36

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: 139.11  E-value: 1.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglstEGKRWIsnLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd06648    15 IGEGSTGIVCIATDKSTGRQVAVKKMDLRK---------QQRREL--LFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLCfEIVKradAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGE 177
Cdd:cd06648    84 EFLEGGALT-DIVT---HTRMNEEQIAT-VCRAVLKALSFLHSQGVIHRDIKSDSILLTS---DGRVKLSDFGFCAQVSK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYgtKERLFEGiIKGKYKMNPRQWSH---ISES 254
Cdd:cd06648   156 EVPRRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYF--NEPPLQA-MKRIRDNEPPKLKNlhkVSPR 232
                         250       260
                  ....*....|....*....|....*....
gi 1039796143 255 AKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd06648   233 LRSFLDRMLVRDPAQRATAAELLNHPFLA 261
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
12-281 1.04e-36

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: 140.01  E-value: 1.04e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglsTEGKRW---ISNLkREASICHMLKHPHIVELLETYS 88
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIR-----------MENEKEgfpITAI-REIKLLQKLDHPNVVRLKEIVT 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SD------GMLYMVFEFMDgADLcfeivkradAGFVYSEAVAS------HYMRQILEALRYCHDNNIIHRDVKPHCVLLA 156
Cdd:cd07840    69 SKgsakykGSIYMVFEYMD-HDL---------TGLLDNPEVKFtesqikCYMKQLLEGLQYLHSNGILHRDIKGSNILIN 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 157 SKENsapVKLGGFGVAIQL-GESGLVAGGRVGTPHFMAPEVV---KRepYGKPVDVWGCGVILFILLSGCLPFYGTKE-- 230
Cdd:cd07840   139 NDGV---LKLADFGLARPYtKENNADYTNRVITLWYRPPELLlgaTR--YGPEVDMWSVGCILAELFTGKPIFQGKTEle 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 231 ---RLFE-----------GIIKGKYKMNPRQ-----------WSH-ISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd07840   214 qleKIFElcgspteenwpGVSDLPWFENLKPkkpykrrlrevFKNvIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
18-270 1.19e-36

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: 138.44  E-value: 1.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRetGQQFAVKIVDVAKFTsspglstegKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd13999     1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDN---------DELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLcFEIVKraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 177
Cdd:cd13999    70 EYMPGGSL-YDLLH--KKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFT---VKIADFGLSRIKNS 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF--YGTKERLFEGIIKGKYKMNPrqwSHISESA 255
Cdd:cd13999   144 TTEKMTGVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFkeLSPIQIAAAVVQKGLRPPIP---PDCPPEL 220
                         250
                  ....*....|....*
gi 1039796143 256 KDLVRRMLMLDPAER 270
Cdd:cd13999   221 SKLIKRCWNEDPEKR 235
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
12-281 1.33e-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: 138.75  E-value: 1.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglstEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14662     2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIE------------RGLKIDENVQREIINHRSLRHPNIIRFKEVVLTPT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcFEivKRADAGfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkeNSAP-VKLGGFG 170
Cdd:cd14662    70 HLAIVMEYAAGGEL-FE--RICNAG-RFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDG--SPAPrLKICDFG 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAiqlgESGLVAG---GRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFEGIIKGKY 241
Cdd:cd14662   144 YS----KSSVLHSqpkSTVGTPAYIAPEVLSRKEYdGKVADVWSCGVTLYVMLVGAYPFEDPDDpknfrKTIQRIMSVQY 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039796143 242 KMNprQWSHISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14662   220 KIP--DYVRVSQDCRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
18-281 2.21e-36

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: 137.78  E-value: 2.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVdvakftsspglSTEGKRwISNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFV-----------SKKMKK-KEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLcFEIVKRADAgfVYSEAVAsHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLge 177
Cdd:cd14115    69 ELMDDGRL-LDYLMNHDE--LMEEKVA-FYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQI-- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 sglvAGGR-----VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHI 251
Cdd:cd14115   143 ----SGHRhvhhlLGNPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDeSKEETCINVCRVDFSFPDEYFGDV 218
                         250       260       270
                  ....*....|....*....|....*....|
gi 1039796143 252 SESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14115   219 SQAARDFINVILQEDPRRRPTAATCLQHPW 248
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
10-280 2.73e-36

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: 138.26  E-value: 2.73e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstegkrwISNLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd06610     1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTS----------MDELRKEIQAMSQCNHPNVVSYYTSFVV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADlCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGF 169
Cdd:cd06610    71 GDELWLVMPLLSGGS-LLDIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGE---DGSVKIADF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGLVAGGR----VGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPFY-------------GTKER 231
Cdd:cd06610   147 GVSASLATGGDRTRKVrktfVGTPCWMAPEVMEQVRgYDFKADIWSFGITAIELATGAAPYSkyppmkvlmltlqNDPPS 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039796143 232 LFEGIIKGKYkmnprqwshiSESAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd06610   227 LETGADYKKY----------SKSFRKMISLCLQKDPSKRPTAEELLKHK 265
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
18-283 3.69e-36

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: 137.61  E-value: 3.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstegKRWISNLKREASICHMLKH-PHIVELLETYSSDGMLYMV 96
Cdd:cd05611     4 ISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIA--------KNQVTNVKAERAIMMIQGEsPYVAKLYYSFQSKDYLYLV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMDGADlCFEIVKRADagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGvaiqLG 176
Cdd:cd05611    76 MEYLNGGD-CASLIKTLG---GLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLI---DQTGHLKLTDFG----LS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 177 ESGLVagGR-----VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY-GTKERLFEGIIKGKYKMNPRQWSH 250
Cdd:cd05611   145 RNGLE--KRhnkkfVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHaETPDAVFDNILSRRINWPEEVKEF 222
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039796143 251 ISESAKDLVRRMLMLDPAERI---TVYEALNHPWLK 283
Cdd:cd05611   223 CSPEAVDLINRLLCMDPAKRLganGYQEIKSHPFFK 258
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
9-296 4.08e-36

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: 137.95  E-value: 4.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglsTEGKRWISNLKREASICHMLKHPHIVELLETYS 88
Cdd:cd06611     4 NDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQ-----------IESEEELEDFMVEIDILSECKHPNIVGLYEAYF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCfEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGG 168
Cdd:cd06611    73 YENKLWILIEFCDGGALD-SIMLELERGL--TEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGD---VKLAD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLVAGGRVGTPHFMAPEVV-----KREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYK 242
Cdd:cd06611   147 FGVSAKNKSTLQKRDTFIGTPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHHELNPmRVLLKILKSEPP 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 243 --MNPRQWshiSESAKDLVRRMLMLDPAERITVYEALNHPWLKER-DRYAYKIHLPE 296
Cdd:cd06611   227 tlDQPSKW---SSSFNDFLKSCLVKDPDDRPTAAELLKHPFVSDQsDNKAIKDLLAE 280
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
12-282 7.16e-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: 137.28  E-value: 7.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvAKFTSspglstegkrW--ISNLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMK-KKFYS----------WeeCMNLREVKSLRKLNEHPNIVKLKEVFRE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGaDLcFEIVKRADaGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGF 169
Cdd:cd07830    70 NDELYFVFEYMEG-NL-YQLMKDRK-GKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEV---VKIADF 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLgESGLVAGGRVGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPFYGTKErlfegiIKGKYKM----- 243
Cdd:cd07830   144 GLAREI-RSRPPYTDYVSTRWYRAPEILLRSTsYSSPVDIWALGCIMAELYTLRPLFPGSSE------IDQLYKIcsvlg 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 244 --NPRQWS--------------------------HISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd07830   217 tpTKQDWPegyklasklgfrfpqfaptslhqlipNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
12-284 1.08e-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: 135.35  E-value: 1.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKivDVAKFTSSPglsTEGKRWIsnlkREASICHMLKHPHIVELL-----ET 86
Cdd:cd07834     2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIK--KISNVFDDL---IDAKRIL----REIKILRHLKHENIIGLLdilrpPS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYMVFEFMDgADLCfEIVKradAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKL 166
Cdd:cd07834    73 PEEFNDVYIVTELME-TDLH-KVIK---SPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCD---LKI 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVA--IQLGESGLVAGGRVGTPHFMAPEVV---KRepYGKPVDVWGCGVILFILLSGCLPFYGT------------- 228
Cdd:cd07834   145 CDFGLArgVDPDEDKGFLTEYVVTRWYRAPELLlssKK--YTKAIDIWSVGCIFAELLTRKPLFPGRdyidqlnlivevl 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796143 229 ---KERLFEGI--------IKGKYKMNPRQWSHI----SESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd07834   223 gtpSEEDLKFIssekarnyLKSLPKKPKKPLSEVfpgaSPEAIDLLEKMLVFNPKKRITADEALAHPYLAQ 293
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
12-282 1.21e-34

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: 133.13  E-value: 1.21e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVD---VAKFTSSPGLStegkrwisnlKREASICHMLK-----HPHIVEL 83
Cdd:cd14005     2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPksrVTEWAMINGPV----------PVPLEIALLLKaskpgVPGVIRL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  84 LETYS-SDGMLyMVFEFMDGA-DLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENS 161
Cdd:cd14005    72 LDWYErPDGFL-LIMERPEPCqDL-FDFITERGA---LSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 162 apVKLGGFGVAIQLGESglVAGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKgk 240
Cdd:cd14005   147 --VKLIDFGCGALLKDS--VYTDFDGTRVYSPPEWIRHGRYhGRPATVWSLGILLYDMLCGDIPFENDEQILRGNVLF-- 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1039796143 241 ykmnprqWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14005   221 -------RPRLSKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
12-282 1.87e-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: 133.54  E-value: 1.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGL------------STEGKRWISNLKR---EASICHMLK 76
Cdd:cd14200     2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLKQYGFprrppprgskaaQGEQAKPLAPLERvyqEIAILKKLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  77 HPHIVELLETYS--SDGMLYMVFEFMDGADlcfeiVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVL 154
Cdd:cd14200    82 HVNIVKLIEVLDdpAEDNLYMVFDLLRKGP-----VMEVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 155 LAskeNSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVV--KREPY-GKPVDVWGCGVILFILLSGCLPFYGTKER 231
Cdd:cd14200   157 LG---DDGHVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLsdSGQSFsGKALDVWAMGVTLYCFVYGKCPFIDEFIL 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039796143 232 LFEGIIKGKYKMNPRQwSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14200   234 ALHNKIKNKPVEFPEE-PEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
12-282 1.99e-34

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: 133.55  E-value: 1.99e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGL-----------STEG----KRWISNLKREASICHMLK 76
Cdd:cd14199     4 YKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRQAGFprrppprgaraAPEGctqpRGPIERVYQEIAILKKLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  77 HPHIVELLETYS--SDGMLYMVFEFMD-GADLCFEIVKRadagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCV 153
Cdd:cd14199    84 HPNVVKLVEVLDdpSEDHLYMVFELVKqGPVMEVPTLKP------LSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 154 LLASKENsapVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVK--REPY-GKPVDVWGCGVILFILLSGCLPFYGTKE 230
Cdd:cd14199   158 LVGEDGH---IKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSetRKIFsGKALDVWAMGVTLYCFVFGQCPFMDERI 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 231 RLFEGIIKGKYKMNPRQwSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14199   235 LSLHSKIKTQPLEFPDQ-PDISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
12-282 2.40e-34

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: 133.22  E-value: 2.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspGLSTEGKRWISNLKreasicHMLKHPHIVELLETYSSDG 91
Cdd:cd07832     2 YKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEG--GIPNQALREIKALQ------ACQGHPYVVKLRDVFPHGT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGaDLcFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd07832    74 GFVLVFEYMLS-SL-SEVLRDEERPL--TEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGV---LKIADFGL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 A-IQLGESGLVAGGRVGTPHFMAPEVV--KREpYGKPVDVWGCGVILFILLSGCLPFYGT----------------KERL 232
Cdd:cd07832   147 ArLFSEEDPRLYSHQVATRWYRAPELLygSRK-YDEGVDLWAVGCIFAELLNGSPLFPGEndieqlaivlrtlgtpNEKT 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796143 233 FEGII------KGKYKMNPRQ-WSHI----SESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd07832   226 WPELTslpdynKITFPESKGIrLEEIfpdcSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
16-282 5.11e-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: 131.58  E-value: 5.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglsTEGKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd14190    10 EVLGGGKFGKVHTCTEKRTGLKLAAKVIN-----------KQNSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLCFEIVkraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKeNSAPVKLGGFGVAIQL 175
Cdd:cd14190    79 FMEYVEGGELFERIV---DEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNR-TGHQVKIIDFGLARRY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 G-ESGLVAGgrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPRQWSHISE 253
Cdd:cd14190   155 NpREKLKVN--FGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDtETLNNVLMGNWYFDEETFEHVSD 232
                         250       260
                  ....*....|....*....|....*....
gi 1039796143 254 SAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14190   233 EAKDFVSNLIIKERSARMSATQCLKHPWL 261
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
10-286 6.60e-34

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: 132.17  E-value: 6.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstegKRWISNLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd05612     1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIR--------LKQEQHVHNEKRVLKEVSHPFIIRLFWTEHD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSapVKLGGF 169
Cdd:cd05612    73 QRFLYMLMEYVPGGEL-FSYLRNSGR---FSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILL-DKEGH--IKLTDF 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnPRqw 248
Cdd:cd05612   146 GFAKKLRDRTWTL---CGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDdNPFGIYEKILAGKLEF-PR-- 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1039796143 249 sHISESAKDLVRRMLMLDPAERI-----TVYEALNHPWLKERD 286
Cdd:cd05612   220 -HLDLYAKDLIKKLLVVDRTRRLgnmknGADDVKNHRWFKSVD 261
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
16-282 7.35e-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: 7.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRrCINRETGQQFAVKIVDVakftsSPGLSTEGKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd06631     7 NVLGKGAYGTVY-CGLTSTGQLIAVKQVEL-----DTSDKEKAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQL 175
Cdd:cd06631    81 FMEFVPGGSIA-SILARFGA---LEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMP---NGVIKLIDFGCAKRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GESGLVAG-GRV-----GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLP----------FYgtkerlfegiIKG 239
Cdd:cd06631   154 CINLSSGSqSQLlksmrGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPwadmnpmaaiFA----------IGS 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1039796143 240 KYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd06631   224 GRKPVPRLPDKFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
SH3_MPP1 cd12080
Src Homology 3 domain of Membrane Protein, Palmitoylated 1 (or MAGUK p55 subfamily member 1); ...
599-660 8.08e-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: 8.08e-34
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 599 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPEL 660
Cdd:cd12080     1 YMRAQFDYDPKKDNLIPCKEAGLKFQTGDIIQIINKDDSNWWQGRVEGSGEESAGLIPSPEL 62
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
12-282 8.22e-34

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: 131.63  E-value: 8.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkfTSSPGLSTEGKRWISNLKReasICHmLKHPHIVELLE-----T 86
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVP--LSEEGIPLSTIREIALLKQ---LES-FEHPNVVRLLDvchgpR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYMVFEFMDgADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKL 166
Cdd:cd07838    75 TDRELKLTLVFEHVD-QDLATYLDKCPKPGL--PPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTS---DGQVKL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAIQLG-ESGLVAggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFEGIIKGK 240
Cdd:cd07838   149 ADFGLARIYSfEMALTS--VVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEadqlgKIFDVIGLPS 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796143 241 YKMNPRQ----WS---------------HISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd07838   227 EEEWPRNsalpRSsfpsytprpfksfvpEIDEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
12-281 9.21e-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: 131.39  E-value: 9.21e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQqfavkIVDVAKFTSSPGLSTEGKRWIsnlkREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd07846     3 YENLGLVGEGSYGMVMKCRHKETGQ-----IVAIKKFLESEDDKMVKKIAM----REIKMLKQLRHENLVNLIEVFRRKK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcfEIVKRADAGFVYSeaVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGV 171
Cdd:cd07846    74 RWYLVFEFVDHTVL--DDLEKYPNGLDES--RVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQ---SGVVKLCDFGF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVGTPHFMAPE-VVKREPYGKPVDVWGCGVILFILLSGCLPFYG----------------------- 227
Cdd:cd07846   147 ARTLAAPGEVYTDYVATRWYRAPElLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGdsdidqlyhiikclgnliprhqe 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 228 --TKERLFEGI----IKGKYKMNpRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd07846   227 lfQKNPLFAGVrlpeVKEVEPLE-RRYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
12-282 1.60e-33

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: 130.22  E-value: 1.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCE-----VIGKGPFSVVRRCINRETGQQFAVKIVDVakftsspglstEGKRWISNLKREASICHMLKHPHIVELLET 86
Cdd:cd06624     5 YEYDEsgervVLGKGTFGVVYAARDLSTQVRIAIKEIPE-----------RDSREVQPLHEEIALHSRLSHKNIVQYLGS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYMVFEFMDGADLCfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKenSAPVKL 166
Cdd:cd06624    74 VSEDGFFKIFMEQVPGGSLS-ALLRSKWGPLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTY--SGVVKI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREP--YGKPVDVW--GCGVILfiLLSGCLPFY--GTKErlfEGIIK-G 239
Cdd:cd06624   151 SDFGTSKRLAGINPCTETFTGTLQYMAPEVIDKGQrgYGPPADIWslGCTIIE--MATGKPPFIelGEPQ---AAMFKvG 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1039796143 240 KYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd06624   226 MFKIHPEIPESLSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
12-282 2.21e-33

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: 129.34  E-value: 2.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglstEGKRWISN-LKREASICHMLKHPHIVELLETYSSD 90
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKK---------APEDYLQKfLPREIEVIKGLKHPNLICFYEAIETT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLcFEIVKRADAGfvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFG 170
Cdd:cd14162    73 SRVYIIMELAENGDL-LDYIRKNGAL---PEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNN---LKITDFG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAiqLGESGLVAGGRV------GTPHFMAPEVVKREPYgKPV--DVWGCGVILFILLSGCLPFYGTKER-LFEGIIKG-K 240
Cdd:cd14162   146 FA--RGVMKTKDGKPKlsetycGSYAYASPEILRGIPY-DPFlsDIWSMGVVLYTMVYGRLPFDDSNLKvLLKQVQRRvV 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1039796143 241 YKMNPrqwsHISESAKDLVRRMLMLDPaERITVYEALNHPWL 282
Cdd:cd14162   223 FPKNP----TVSEECKDLILRMLSPVK-KRITIEEIKRDPWF 259
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-282 2.67e-33

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: 129.16  E-value: 2.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFtsSPGLSTEGKRWISNLKReasichmLKHPHIVELLETYSSDG 91
Cdd:cd08218     2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKM--SPKEREESRKEVAVLSK-------MKHPNIVQYQESFEENG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIvkRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGV 171
Cdd:cd08218    73 NLYIVMDYCDGGDLYKRI--NAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLT---KDGIIKLGDFGI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF-YGTKERLFEGIIKGKYKMNPrqwSH 250
Cdd:cd08218   148 ARVLNSTVELARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFeAGNMKNLVLKIIRGSYPPVP---SR 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1039796143 251 ISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd08218   225 YSYDLRSLVSQLFKRNPRDRPSINSILEKPFI 256
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
12-283 2.79e-33

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: 132.02  E-value: 2.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIV---DVAKFTSSPGLSTEgkrwiSNLKREASichmlkHPHIVELLETYS 88
Cdd:cd05573     3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILrksDMLKREQIAHVRAE-----RDILADAD------SPWIVRLHYAFQ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGG 168
Cdd:cd05573    72 DEDHLYLVMEYMPGGDLMNLLIKYD----VFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGH---IKLAD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLV-----------------------------AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILL 219
Cdd:cd05573   145 FGLCTKMNKSGDResylndsvntlfqdnvlarrrphkqrrvrAYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEML 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 220 SGCLPFYG-TKERLFEGIIKGKYKMN-PRQwSHISESAKDLVRRmLMLDPAERITVYEAL-NHPWLK 283
Cdd:cd05573   225 YGFPPFYSdSLVETYSKIMNWKESLVfPDD-PDVSPEAIDLIRR-LLCDPEDRLGSAEEIkAHPFFK 289
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-270 2.82e-33

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: 128.94  E-value: 2.82e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstegkrwISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd08219     2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSA----------VEDSRKEAVLLAKMKHPNIVAFKESFEADG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIvkRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd08219    72 HLYIVMEYCDGGDLMQKI--KLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGK---VKLGDFGS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY-GTKERLFEGIIKGKYKMNPrqwSH 250
Cdd:cd08219   147 ARLLTSPGAYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQaNSWKNLILKVCQGSYKPLP---SH 223
                         250       260
                  ....*....|....*....|
gi 1039796143 251 ISESAKDLVRRMLMLDPAER 270
Cdd:cd08219   224 YSYELRSLIKQMFKRNPRSR 243
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-282 3.00e-33

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: 128.92  E-value: 3.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakFTSSPGLSTEGKrwisnlKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd08225     2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEID---LTKMPVKEKEAS------KKEVILLAKMKHPNIVTFFASFQENG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRAdaGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkeNSAPVKLGGFGV 171
Cdd:cd08225    73 RLFIVMEYCDGGDLMKRINRQR--GVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSK--NGMVAKLGDFGI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYK-MNPrqws 249
Cdd:cd08225   149 ARQLNDSMELAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNlHQLVLKICQGYFApISP---- 224
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1039796143 250 HISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd08225   225 NFSRDLRSLISQLFKVSPRDRPSITSILKRPFL 257
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
17-282 3.05e-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: 129.58  E-value: 3.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKIVDvakfTSSPGLSTEG--KRWISNLKREASICHMLKHPHIVELLETYSSDGMLY 94
Cdd:cd06628     7 LIGSGSFGSVYLGMNASSGELMAVKQVE----LPSVSAENKDrkKSMLDALQREIALLRELQHENIVQYLGSSSDANHLN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  95 MVFEFMDGAdlcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQ 174
Cdd:cd06628    83 IFLEYVPGG----SVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILV---DNKGGIKISDFGISKK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 175 LGESGLVAGGRVGTPHF------MAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKErlFEGIIKGKYKMNPRQW 248
Cdd:cd06628   156 LEANSLSTKNNGARPSLqgsvfwMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQ--MQAIFKIGENASPTIP 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796143 249 SHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd06628   234 SNISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
17-286 3.95e-33

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: 130.41  E-value: 3.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKIV--DVAkftsspgLSTEGKRWISNLKREASICHmlKHPHIVELLETYSSDGMLY 94
Cdd:cd05570     2 VLGKGSFGKVMLAERKKTDELYAIKVLkkEVI-------IEDDDVECTMTEKRVLALAN--RHPFLTGLHACFQTEDRLY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  95 MVFEFMDGADLCFEIVKradaGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGvaiq 174
Cdd:cd05570    73 FVMEYVNGGDLMFHIQR----ARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGH---IKIADFG---- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 175 LGESGLVAGGRV----GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnPRqws 249
Cdd:cd05570   142 MCKEGIWGGNTTstfcGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGdDEDELFEAILNDEVLY-PR--- 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1039796143 250 HISESAKDLVRRMLMLDPAERITVY-----EALNHPWLKERD 286
Cdd:cd05570   218 WLSREAVSILKGLLTKDPARRLGCGpkgeaDIKAHPFFRNID 259
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
16-281 5.89e-33

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: 130.17  E-value: 5.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKI----VDVAKFTSSPGLStegkrwisnlkrEASICHMLKHPHIVELLETYSSDG 91
Cdd:cd05571     1 KVLGKGTFGKVILCREKATGELYAIKIlkkeVIIAKDEVAHTLT------------ENRVLQNTRHPFLTSLKYSFQTND 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSapVKLGGFGV 171
Cdd:cd05571    69 RLCFVMEYVNGGELFFHLSRER----VFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLL-DKDGH--IKITDFGL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnPRqwsH 250
Cdd:cd05571   142 CKEEISYGATTKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDhEVLFELILMEEVRF-PS---T 217
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039796143 251 ISESAKDLVRRMLMLDPAERI-----TVYEALNHPW 281
Cdd:cd05571   218 LSPEAKSLLAGLLKKDPKKRLgggprDAKEIMEHPF 253
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
18-283 7.27e-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: 129.08  E-value: 7.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVakfTSSPGLSTEgkrwisnLKREASICHMLKHPHIVELLETY--SSDGMLYM 95
Cdd:cd06621     9 LGEGAGGSVTKCRLRNTKTIFALKTITT---DPNPDVQKQ-------ILRELEINKSCASPYIVKYYGAFldEQDSSIGI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLcFEIVKRADA-GFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQ 174
Cdd:cd06621    79 AMEYCEGGSL-DSIYKKVKKkGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQ---VKLCDFGVSGE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 175 LGESglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER------LFEGIIKGK-YKM---- 243
Cdd:cd06621   155 LVNS--LAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPPEGEPplgpieLLSYIVNMPnPELkdep 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1039796143 244 -NPRQWshiSESAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd06621   233 eNGIKW---SESFKDFIEKCLEKDGTRRPGPWQMLAHPWIK 270
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
8-278 1.23e-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: 1.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVyelcEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsspglsTEGKRWISNLKREASICHMLKHPHIVELLETY 87
Cdd:cd13996     8 FEEI----ELLGSGGFGSVYKVRNKVDGVTYAIKKIRL----------TEKSSASEKVLREVKALAKLNHPNIVRYYTAW 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCFEIVKRaDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLG 167
Cdd:cd13996    74 VEEPPLYIQMELCEGGTLRDWIDRR-NSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQ--VKIG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVA----IQLGESGLVAG----------GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSgclPFYGTKERL- 232
Cdd:cd13996   151 DFGLAtsigNQKRELNNLNNnnngntsnnsVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLH---PFKTAMERSt 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1039796143 233 -FEGIIKGKYKMNPRQWsHISEsaKDLVRRMLMLDPAERITVYEALN 278
Cdd:cd13996   228 iLTDLRNGILPESFKAK-HPKE--ADLIQSLLSKNPEERPSAEQLLR 271
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
16-280 1.31e-32

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: 127.55  E-value: 1.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEGKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd06630     6 PLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSS-----EQEEVVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLCFeIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkeNSAPVKLGGFGVAIQL 175
Cdd:cd06630    81 FVEWMAGGSVAS-LLSKYGA---FSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDS--TGQRLRIADFGAAARL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GE----SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIkgkYKMN-----PR 246
Cdd:cd06630   155 ASkgtgAGEFQGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALI---FKIAsattpPP 231
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796143 247 QWSHISESAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd06630   232 IPEHLSPGLRDVTLRCLELQPEDRPPARELLKHP 265
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
18-282 1.68e-32

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


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 127.03  E-value: 1.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKftSSPGLstegkrwISNLKREASICHMLKHPHIVEL--LETYSSDGMLYM 95
Cdd:cd06626     8 IGEGTFGKVYTAVNLDTGELMAMKEIRFQD--NDPKT-------IKEIADEMKVLEGLDHPNLVRYygVEVHREEVYIFM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 vfEFMDGADLcFEIVKRadaGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQL 175
Cdd:cd06626    79 --EYCQEGTL-EELLRH---GRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDS---NGLIKLGDFGSAVKL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GESG-LVAGGR----VGTPHFMAPEVVKREP---YGKPVDVWGCGVILFILLSGCLPFYgTKERLFEGIIKGKYKMNPR- 246
Cdd:cd06626   150 KNNTtTMAPGEvnslVGTPAYMAPEVITGNKgegHGRAADIWSLGCVVLEMATGKRPWS-ELDNEWAIMYHVGMGHKPPi 228
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1039796143 247 -QWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd06626   229 pDSLQLSPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
10-286 2.79e-32

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: 127.13  E-value: 2.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglstegKRWISNLKR------EASICHMLKHPHIVEL 83
Cdd:cd14209     1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILD--------------KQKVVKLKQvehtlnEKRILQAINFPFLVKL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  84 LETYSSDGMLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAP 163
Cdd:cd14209    67 EYSFKDNSNLYMVMEYVPGGEM-FSHLRRIGR---FSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQ---GY 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 164 VKLGGFGVAIQLGesglvagGRV----GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIK 238
Cdd:cd14209   140 IKVTDFGFAKRVK-------GRTwtlcGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPiQIYEKIVS 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039796143 239 GKYKMnPrqwSHISESAKDLVRRMLMLDPAERI-----TVYEALNHPWLKERD 286
Cdd:cd14209   213 GKVRF-P---SHFSSDLKDLLRNLLQVDLTKRFgnlknGVNDIKNHKWFATTD 261
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
17-284 4.32e-32

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: 126.68  E-value: 4.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEgkrwisnlKREASICHMLKHPHIVELLETYSSDGMLYMV 96
Cdd:cd05630     7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMA--------LNEKQILEKVNSRFVVSLAYAYETKDALCLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMDGADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLG 176
Cdd:cd05630    79 LTLMNGGDLKFHIYHMGQAGF--PEARAVFYAAEICCGLEDLHRERIVYRDLKPENILL---DDHGHIRISDLGLAVHVP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 177 EsGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWS-HISESA 255
Cdd:cd05630   154 E-GQTIKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSeKFSPQA 232
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796143 256 KDLVRRMLMLDPAERI-----TVYEALNHPWLKE 284
Cdd:cd05630   233 RSLCSMLLCKDPAERLgcrggGAREVKEHPLFKK 266
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
12-284 5.18e-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: 5.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVK-IVDVakFtsspGLSTEGKRWIsnlkREASICHMLK-HPHIVELLETYSS 89
Cdd:cd07852     9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKkIFDA--F----RNATDAQRTF----REIMFLQELNdHPNIIKLLNVIRA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGM--LYMVFEFMDgADLcfEIVKRADAgfvySEAVASHY-MRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKL 166
Cdd:cd07852    79 ENDkdIYLVFEYME-TDL--HAVIRANI----LEDIHKQYiMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCR---VKL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVA-----IQLGESGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-----ERLFEG 235
Cdd:cd07852   149 ADFGLArslsqLEEDDENPVLTDYVATRWYRAPEIlLGSTRYTKGVDMWSVGCILGEMLLGKPLFPGTStlnqlEKIIEV 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 236 I----------IKGKY------KMNPRQ-------WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd07852   229 IgrpsaediesIQSPFaatmleSLPPSRpksldelFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQ 300
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
10-282 5.31e-32

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: 125.40  E-value: 5.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAvkivdvAKFTSSPGLSTEGKRwisnlkREASICHMLKHPHIVELLETYSS 89
Cdd:cd14108     2 DYYDIHKEIGRGAFSYLRRVKEKSSDLSFA------AKFIPVRAKKKTSAR------RELALLAELDHKSIVRFHDAFEK 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEfmdgadLCFE-IVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkENSAPVKLGG 168
Cdd:cd14108    70 RRVVIIVTE------LCHEeLLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMAD-QKTDQVRICD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQL--GESGLVaggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNP 245
Cdd:cd14108   143 FGNAQELtpNEPQYC---KYGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRtTLMNIRNYNVAFEE 219
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1039796143 246 RQWSHISESAKDLVRRMLMLDPAeRITVYEALNHPWL 282
Cdd:cd14108   220 SMFKDLCREAKGFIIKVLVSDRL-RPDAEETLEHPWF 255
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
18-307 7.58e-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: 126.25  E-value: 7.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVrrCINRE--TGQQFAVKIVDVAKftsspglstEGKRWIsnLKREASICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd06659    29 IGEGSTGVV--CIAREkhSGRQVAVKMMDLRK---------QQRREL--LFNEVVIMRDYQHPNVVEMYKSYLVGEELWV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLCfEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQL 175
Cdd:cd06659    96 LMEYLQGGALT-DIVSQTR----LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTL---DGRVKLSDFGFCAQI 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESA 255
Cdd:cd06659   168 SKDVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNSHKASPVL 247
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796143 256 KDLVRRMLMLDPAERITVYEALNHPWLkerdryaYKIHLPET----VEQLRKFNAR 307
Cdd:cd06659   248 RDFLERMLVRDPQERATAQELLDHPFL-------LQTGLPEClvplIQQYRKRTST 296
PDZ_MPP6-MPP2-like cd10832
PDZ domain of membrane palmitoylated protein 6 (MPP6), MPP2, and related domains; PDZ (PSD-95 ...
495-575 1.12e-31

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: 118.10  E-value: 1.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 495 RLVQFQKNTDEPMGITLKMNElNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQtvEQLQKMLREMRGSITFKIV 574
Cdd:cd10832     1 RMVGIRKNPGEPLGVTVRLEE-GELVIARILHGGMIDRQGLLHVGDIIKEVNGVPVGSP--EQLQEMLKNASGSVTLKIL 77

                  .
gi 1039796143 575 P 575
Cdd:cd10832    78 P 78
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
17-271 1.30e-31

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: 125.11  E-value: 1.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEgkrwiSNLKReasICHMLKHPHIVELLETYSSDGMLYMV 96
Cdd:cd05631     7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMA-----LNEKR---ILEKVNSRFVVSLAYAYETKDALCLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMDGADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLG 176
Cdd:cd05631    79 LTIMNGGDLKFHIYNMGNPGF--DEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILL---DDRGHIRISDLGLAVQIP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 177 EsGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSH-ISESA 255
Cdd:cd05631   154 E-GETVRGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRRVKEDQEEYSEkFSEDA 232
                         250
                  ....*....|....*.
gi 1039796143 256 KDLVRRMLMLDPAERI 271
Cdd:cd05631   233 KSICRMLLTKNPKERL 248
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-282 1.91e-31

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: 123.70  E-value: 1.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspgLSTEGKRWISNLKREASICHMLKHPHIVELLETYSS-D 90
Cdd:cd08223     2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLN---------LKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGeD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLCFEIvkRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFG 170
Cdd:cd08223    73 GFLYIVMGFCEGGDLYTRL--KEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLT---KSNIIKVGDLG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMNPRQWs 249
Cdd:cd08223   148 IARVLESSSDMATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDmNSLVYKILEGKLPPMPKQY- 226
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1039796143 250 hiSESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd08223   227 --SPELGELIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
10-281 2.22e-31

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: 124.41  E-value: 2.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQqfavkIVDVAKFTSS---PGLSTEGKRWISNLKreasichMLKHPHIVELLET 86
Cdd:cd07847     1 EKYEKLSKIGEGSYGVVFKCRNRETGQ-----IVAIKKFVESeddPVIKKIALREIRMLK-------QLKHPNLVNLIEV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYMVFEFMDGADLcFEIVKradagfvYSEAVASHYMR----QILEALRYCHDNNIIHRDVKPHCVLLaSKENSa 162
Cdd:cd07847    69 FRRKRKLHLVFEYCDHTVL-NELEK-------NPRGVPEHLIKkiiwQTLQAVNFCHKHNCIHRDVKPENILI-TKQGQ- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 163 pVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPE-VVKREPYGKPVDVWGCGVILFILLSGClPFYGTK---ERLFEgIIK 238
Cdd:cd07847   139 -IKLCDFGFARILTGPGDDYTDYVATRWYRAPElLVGDTQYGPPVDVWAIGCVFAELLTGQ-PLWPGKsdvDQLYL-IRK 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 239 GKYKMNPR---------------------------QWSHISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd07847   216 TLGDLIPRhqqifstnqffkglsipepetreplesKFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
17-283 2.63e-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: 124.39  E-value: 2.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKivdvakftsspglSTEGKRwISNLKREA------SICHMLKHPHIVELLETYSSD 90
Cdd:cd05605     7 VLGKGGFGEVCACQVRATGKMYACK-------------KLEKKR-IKKRKGEAmalnekQILEKVNSRFVVSLAYAYETK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFG 170
Cdd:cd05605    73 DALCLVLTIMNGGDLKFHIYNMGNPGF--EEERAVFYAAEITCGLEHLHSERIVYRDLKPENILL---DDHGHVRISDLG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLGESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSH 250
Cdd:cd05605   148 LAVEIPEGETIRG-RVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRRVKEDQEEYSE 226
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1039796143 251 -ISESAKDLVRRMLMLDPAERI-----TVYEALNHPWLK 283
Cdd:cd05605   227 kFSEEAKSICSQLLQKDPKTRLgcrgeGAEDVKSHPFFK 265
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
12-282 4.93e-31

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: 122.50  E-value: 4.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAK-----FTSSPGLSTegkrwisnLKREASICHMLK---HPHIVEL 83
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERilvdtWVRDRKLGT--------VPLEIHILDTLNkrsHPNIVKL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  84 LETYSSDGMLYMVFE-FMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensa 162
Cdd:cd14004    74 LDFFEDDEFYYLVMEkHGSGMDL-FDFIERKPN---MDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGN---- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 163 pvklgGFGVAIQLGESGLVAGGR----VGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKErlfegII 237
Cdd:cd14004   146 -----GTIKLIDFGSAAYIKSGPfdtfVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPFYNIEE-----IL 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039796143 238 KGKYKMNprqwSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14004   216 EADLRIP----YAVSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
12-286 5.28e-31

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: 123.28  E-value: 5.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSpglSTEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd05609     2 FETIKLISNGAYGAVYLVRHRETRQRFAMK-----KINKQ---NLILRNQIQQVFVERDILTFAENPFVVSMYCSFETKR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADlCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd05609    74 HLCMVMEYVEGGD-CATLLKNIGP---LPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGH---IKLTDFGL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 --------AIQLGESGLVAGGR-------VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEG 235
Cdd:cd05609   147 skiglmslTTNLYEGHIEKDTRefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGdTPEELFGQ 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 236 IIKGKYkMNPRQWSHISESAKDLVRRMLMLDPAERI---TVYEALNHPWLKERD 286
Cdd:cd05609   227 VISDEI-EWPEGDDALPDDAQDLITRLLQQNPLERLgtgGAEEVKQHPFFQDLD 279
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
12-282 5.60e-31

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: 123.30  E-value: 5.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspgLSTEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd07861     2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIR---------LESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQEN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFmdgadLCFEIVKRADA----GFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLG 167
Cdd:cd07861    73 RLYLVFEF-----LSMDLKKYLDSlpkgKYMDAELVKS-YLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGV---IKLA 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLF-------E 234
Cdd:cd07861   144 DFGLARAFGIPVRVYTHEVVTLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHGDSEidqlfRIFrilgtptE 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 235 GIIKG-----KYKMNPRQWS---------HISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd07861   224 DIWPGvtslpDYKNTFPKWKkgslrtavkNLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
12-282 5.79e-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: 123.17  E-value: 5.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspgLSTEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd07835     1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIR---------LETEDEGVPSTAIREISLLKELNHPNIVRLLDVVHSEN 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDgADLcfeiVKRADA--GFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCvLLASKENSapVKLGGF 169
Cdd:cd07835    72 KLYLVFEFLD-LDL----KKYMDSspLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQN-LLIDTEGA--LKLADF 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGLVAGGRVGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLF-------EGI 236
Cdd:cd07835   144 GLARAFGVPVRTYTHEVVTLWYRAPEILLGSKhYSTPVDIWSVGCIFAEMVTRRPLFPGDSEidqlfRIFrtlgtpdEDV 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 237 IKG-----KYKMN-----PRQWSHI----SESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd07835   224 WPGvtslpDYKPTfpkwaRQDLSKVvpslDEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
10-282 5.87e-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: 5.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspgLSTEGKRWISNLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd07864     7 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVR---------LDNEKEGFPITAIREIKILRQLNHRSVVNLKEIVTD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 D----------GMLYMVFEFMDgadlcFEIVKRADAGFV-YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLask 158
Cdd:cd07864    78 KqdaldfkkdkGAFYLVFEYMD-----HDLMGLLESGLVhFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILL--- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 159 ENSAPVKLGGFGVA-IQLGESGLVAGGRVGTPHFMAPE-VVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERL-FEG 235
Cdd:cd07864   150 NNKGQIKLADFGLArLYNSEESRPYTNKVITLWYRPPElLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAqLEL 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039796143 236 IIKGKYKMNPRQW--------------------------SHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd07864   230 ISRLCGSPCPAVWpdviklpyfntmkpkkqyrrrlreefSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
12-282 6.36e-31

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: 122.71  E-value: 6.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINrETGQQFAVKIVDVAKFTSSPglstegkrwISNLKREASICHMLKH-PHIVELL--ETYS 88
Cdd:cd14131     3 YEILKQLGKGGSSKVYKVLN-PKKKIYALKRVDLEGADEQT---------LQSYKNEIELLKKLKGsDRIIQLYdyEVTD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGaDLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnsapVKLGG 168
Cdd:cd14131    73 EDDYLYMVMECGEI-DLATILKKKRPKPI--DPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKGR----LKLID 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVA--IQLGESGLVAGGRVGTPHFMAPEVVK--------REPY--GKPVDVWGCGVILFILLSGCLPFYgtkeRLFEGI 236
Cdd:cd14131   146 FGIAkaIQNDTTSIVRDSQVGTLNYMSPEAIKdtsasgegKPKSkiGRPSDVWSLGCILYQMVYGKTPFQ----HITNPI 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039796143 237 IKGKYKMNPR---QWSHISE-SAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14131   222 AKLQAIIDPNheiEFPDIPNpDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
10-282 6.96e-31

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: 122.37  E-value: 6.96e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpGLSTEgkrwisnLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd14116     5 EDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKA-GVEHQ-------LRREVEIQSHLRHPNILRLYGYFHD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGF 169
Cdd:cd14116    77 ATRVYLILEYAPLGTVYRELQKLSK----FDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGS---AGELKIADF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGLVAggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPrqw 248
Cdd:cd14116   150 GWSVHAPSSRRTT--LCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEAnTYQETYKRISRVEFTFPD--- 224
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796143 249 sHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14116   225 -FVTEGARDLISRLLKHNPSQRPMLREVLEHPWI 257
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
12-282 8.07e-31

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: 122.59  E-value: 8.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVR-----RCINRETGQQFAVKIVdvakftSSPGLSTEGKrwISNLKREASICHMLKHPHIVELLET 86
Cdd:cd14076     3 YILGRTLGEGEFGKVKlgwplPKANHRSGVQVAIKLI------RRDTQQENCQ--TSKIMREINILKGLTHPNIVRLLDV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKL 166
Cdd:cd14076    75 LKTKKYIGIVLEFVSGGEL-FDYILARRR---LKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRN---LVI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAIQLGES-GLVAGGRVGTPHFMAPE-VVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKE--------RLFeg 235
Cdd:cd14076   148 TDFGFANTFDHFnGDLMSTSCGSPCYAAPElVVSDSMYaGRKADIWSCGVILYAMLAGYLPFDDDPHnpngdnvpRLY-- 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039796143 236 iikgKYKMN-PRQW-SHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14076   226 ----RYICNtPLIFpEYVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
12-282 8.42e-31

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: 121.89  E-value: 8.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvaKFTSSPGLSTEgkrwisNLKREASICHMLKHPHIVELLETYS-SD 90
Cdd:cd14164     2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVD--RRRASPDFVQK------FLPRELSILRRVNHPNIVQMFECIEvAN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEfMDGADLCFEIVKRADAGFVYSEAVashyMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLGGFG 170
Cdd:cd14164    74 GRLYIVME-AAATDLLQKIQEVHHIPKDLARDM----FAQMVGAVNYLHDMNIVHRDLKCENILLSADDRK--IKIADFG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLGESGLVAGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGkyKMNPRQWS 249
Cdd:cd14164   147 FARFVEDYPELSTTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPFDETNVRRLRLQQRG--VLYPSGVA 224
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1039796143 250 hISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14164   225 -LEEPCRALIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
16-271 9.62e-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: 123.58  E-value: 9.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstegKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd05595     1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIA--------KDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQL 175
Cdd:cd05595    73 VMEYANGGELFFHLSRER----VFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLML---DKDGHIKITDFGLCKEG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnPRQwshISES 254
Cdd:cd05595   146 ITDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDhERLFELILMEEIRF-PRT---LSPE 221
                         250
                  ....*....|....*..
gi 1039796143 255 AKDLVRRMLMLDPAERI 271
Cdd:cd05595   222 AKSLLAGLLKKDPKQRL 238
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
9-283 1.02e-30

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: 123.54  E-value: 1.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEgkrwisnlKREASICHMLKHPHIVELLETYS 88
Cdd:cd05632     1 KNTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMA--------LNEKQILEKVNSQFVVNLAYAYE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGG 168
Cdd:cd05632    73 TKDALCLVLTIMNGGDLKFHIYNMGNPGF--EEERALFYAAEILCGLEDLHRENTVYRDLKPENILL---DDYGHIRISD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQW 248
Cdd:cd05632   148 LGLAVKIPEGESIRG-RVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVY 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1039796143 249 S-HISESAKDLVRRMLMLDPAERITVY-----EALNHPWLK 283
Cdd:cd05632   227 SaKFSEEAKSICKMLLTKDPKQRLGCQeegagEVKRHPFFR 267
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
12-281 1.15e-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: 122.43  E-value: 1.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsSPGLSTEGKR-WISNLKREASICHMLKHPHIVELLETYSSD 90
Cdd:cd13990     2 YLLLNLLGKGGFSEVYKAFDLVEQRYVACKIHQL-----NKDWSEEKKQnYIKHALREYEIHKSLDHPRIVKLYDVFEID 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 -GMLYMVFEFMDGADLCFeIVKRADagfVYSEAVASHYMRQILEALRYC--HDNNIIHRDVKPHCVLLASKENSAPVKLG 167
Cdd:cd13990    77 tDSFCTVLEYCDGNDLDF-YLKQHK---SIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGNVSGEIKIT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVAIQLGESGLVAGGR------VGTPHFMAPE--VVKREP--YGKPVDVWGCGVILFILLSGCLPFyG---TKER-LF 233
Cdd:cd13990   153 DFGLSKIMDDESYNSDGMeltsqgAGTYWYLPPEcfVVGKTPpkISSKVDVWSVGVIFYQMLYGRKPF-GhnqSQEAiLE 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039796143 234 EGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd13990   232 ENTILKATEVEFPSKPVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
17-271 1.31e-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: 123.20  E-value: 1.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKIVdvakftsspglsteGKRWIsnLKR-EASicHM----------LKHPHIVELLE 85
Cdd:cd05575     2 VIGKGSFGKVLLARHKAEGKLYAVKVL--------------QKKAI--LKRnEVK--HImaernvllknVKHPFLVGLHY 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  86 TYSSDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVK 165
Cdd:cd05575    64 SFQTKDKLYFVLDYVNGGELFFHLQRER----HFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGH---VV 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 166 LGGFGvaiqLGESGLVAGGRV----GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG--TKErLFEGIIKG 239
Cdd:cd05575   137 LTDFG----LCKEGIEPSDTTstfcGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSrdTAE-MYDNILHK 211
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1039796143 240 KYKMNPrqwsHISESAKDLVRRMLMLDPAERI 271
Cdd:cd05575   212 PLRLRT----NVSPSARDLLEGLLQKDRTKRL 239
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
68-282 2.03e-30

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: 121.00  E-value: 2.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  68 EASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRD 147
Cdd:cd08221    49 EIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQKNQLF--PEEVVLWYLYQIVSAVSHIHKAGILHRD 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 148 VKPHCVLLAskeNSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 227
Cdd:cd08221   127 IKTLNIFLT---KADLVKLGDFGISKVLDSESSMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDA 203
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796143 228 TKE-RLFEGIIKGKYKMNPRQWshiSESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd08221   204 TNPlRLAVKIVQGEYEDIDEQY---SEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
11-283 2.46e-30

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: 121.43  E-value: 2.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspgLSTEGKRwISNLKREASICHMLKH---PHIVELLETY 87
Cdd:cd06917     2 LYRRLELVGRGSYGAVYRGYHVKTGRVVALKVLN---------LDTDDDD-VSDIQKEVALLSQLKLgqpKNIIKYYGSY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLcfEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLG 167
Cdd:cd06917    72 LKGPSLWIIMDYCEGGSI--RTLMRAGP---IAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGN---VKLC 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVAIQLGESGLVAGGRVGTPHFMAPEVVKR-EPYGKPVDVWGCGVILFILLSGCLPFygTKERLFEGIIKGKYKMNPR 246
Cdd:cd06917   144 DFGVAASLNQNSSKRSTFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPY--SDVDALRAVMLIPKSKPPR 221
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039796143 247 -QWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd06917   222 lEGNGYSPLLKEFVAACLDEEPKDRLSADELLKSKWIK 259
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-280 2.56e-30

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: 120.61  E-value: 2.56e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkftsspGLSTEGKRWISNlkrEASICHMLKHPHIVELLETYSSDG 91
Cdd:cd08220     2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVE------QMTKEERQAALN---EVKVLSMLHHPNIIEYYESFLEDK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRADAgfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLGGFGV 171
Cdd:cd08220    73 ALMIVMEYAPGGTLFEYIQQRKGS--LLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTV--VKIGDFGI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLvAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSgclpfygtKERLFEG---------IIKGKYK 242
Cdd:cd08220   149 SKILSSKSK-AYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELAS--------LKRAFEAanlpalvlkIMRGTFA 219
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039796143 243 MNPRQWshiSESAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd08220   220 PISDRY---SEELRHLILSMLHLDPNKRPTLSEIMAQP 254
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
12-281 3.88e-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: 120.48  E-value: 3.88e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVV---RRcinRETGQQFAVKIVDvakftsspglstEGKRwiSNLKREASICHMLKHPHIVELLETYS 88
Cdd:cd14010     2 YVLYDEIGRGKHSVVykgRR---KGTIEFVAIKCVD------------KSKR--PEVLNEVRLTHELKHPNVLKFYEWYE 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLcfEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGG 168
Cdd:cd14010    65 TSNHLWLVVEYCTGGDL--ETLLRQDGNL--PESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILL---DGNGTLKLSD 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGES-----GLVAG-----------GRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ER 231
Cdd:cd14010   138 FGLARREGEIlkelfGQFSDegnvnkvskkqAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESfTE 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 232 LFEGIIKGKYK-MNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHP-W 281
Cdd:cd14010   218 LVEKILNEDPPpPPPKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
18-271 4.40e-30

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: 120.71  E-value: 4.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEgkrwisnlKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMA--------LNEKIILEKVSSPFIVSLAYAFETKDKLCLVL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 177
Cdd:cd05577    73 TLMNGGDLKYHIYNVGTRGF--SEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGH---VRISDLGLAVEFKG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 sGLVAGGRVGTPHFMAPEVVKRE-PYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSH-ISESA 255
Cdd:cd05577   148 -GKKIKGRVGTHGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMAVEYPDsFSPEA 226
                         250
                  ....*....|....*.
gi 1039796143 256 KDLVRRMLMLDPAERI 271
Cdd:cd05577   227 RSLCEGLLQKDPERRL 242
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
12-281 4.97e-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: 120.66  E-value: 4.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvaKFTSSPGLSTEGKRWISNLKReasichmLKHPHIVELLETYSSDG 91
Cdd:cd07836     2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEI---HLDAEEGTPSTAIREISLMKE-------LKHENIVRLHDVIHTEN 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGaDLCFEIVKRADAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGV 171
Cdd:cd07836    72 KLMLVFEYMDK-DLKKYMDTHGVRGALDPNTVKS-FTYQLLKGIAFCHENRVLHRDLKPQNLLINKR---GELKLADFGL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGT----------------KERLFE 234
Cdd:cd07836   147 ARAFGIPVNTFSNEVVTLWYRAPDVlLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTnnedqllkifrimgtpTESTWP 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 235 GI-----IKGKYKMNPRQ-----WSHISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd07836   227 GIsqlpeYKPTFPRYPPQdlqqlFPHADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
12-280 5.90e-30

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: 120.49  E-value: 5.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSpglsTEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd07848     3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIK-----KFKDS----EENEEVKETTLRELKMLRTLKQENIVELKEAFRRRG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcfEIVKRADAGfVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnsaPVKLGGFGV 171
Cdd:cd07848    74 KLYLVFEYVEKNML--ELLEEMPNG-VPPEKVRS-YIYQLIKAIHWCHKNDIVHRDIKPENLLISHND---VLKLCDFGF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGE-SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE--RLFE-----GIIKGK--- 240
Cdd:cd07848   147 ARNLSEgSNANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEidQLFTiqkvlGPLPAEqmk 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 241 -YKMNPR-------QWSH-----------ISESAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd07848   227 lFYSNPRfhglrfpAVNHpqslerrylgiLSGVLLDLMKNLLKLNPTDRYLTEQCLNHP 285
SH3_MPP cd11862
Src Homology 3 domain of Membrane Protein, Palmitoylated (or MAGUK p55 subfamily member) ...
599-659 7.04e-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: 7.04e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796143 599 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPE 659
Cdd:cd11862     1 FVRALFDYDPEEDPLIPCKEAGLSFKKGDILQIVNQDDPNWWQARKVGDPNGRAGLIPSQD 61
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
16-286 7.10e-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: 121.17  E-value: 7.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIV--DVAkftsspgLSTEGKRWISNLKREASICHmlKHPHIVELLETYSSDGML 93
Cdd:cd05590     1 RVLGKGSFGKVMLARLKESGRLYAVKVLkkDVI-------LQDDDVECTMTEKRILSLAR--NHPFLTQLYCCFQTPDRL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  94 YMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAI 173
Cdd:cd05590    72 FFVMEFVNGGDLMFHIQKSRR----FDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLL---DHEGHCKLADFGMCK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 174 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNprqwSHIS 252
Cdd:cd05590   145 EGIFNGKTTSTFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAeNEDDLFEAILNDEVVYP----TWLS 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039796143 253 ESAKDLVRRMLMLDPAERITVYE------ALNHPWLKERD 286
Cdd:cd05590   221 QDAVDILKAFMTKNPTMRLGSLTlggeeaILRHPFFKELD 260
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
12-282 7.32e-30

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: 119.32  E-value: 7.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakfTSSPglstegKRWISN-LKREASICHMLKHPHIVELLETY-SS 89
Cdd:cd14163     2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDK---SGGP------EEFIQRfLPRELQIVERLDHKNIIHVYEMLeSA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLcFEIVKRadaGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnsapVKLGGF 169
Cdd:cd14163    73 DGKIYLVMELAEDGDV-FDCVLH---GGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFT----LKLTDF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGL-VAGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEgiiKGKYKMNP 245
Cdd:cd14163   145 GFAKQLPKGGReLSQTFCGSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPFDDTDipKMLCQ---QQKGVSLP 221
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1039796143 246 RQWShISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14163   222 GHLG-VSRTCQDLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
12-281 7.65e-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: 119.92  E-value: 7.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkfTSSPGLSTEGKRWISNLKReasichmLKHPHIVELLETYSSDG 91
Cdd:cd07860     2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLD--TETEGVPSTAIREISLLKE-------LNHPNIVKLLDVIHTEN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDgADLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGV 171
Cdd:cd07860    73 KLYLVFEFLH-QDLKKFMDASALTGI--PLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLI---NTEGAIKLADFGL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFEGI--------- 236
Cdd:cd07860   147 ARAFGVPVRTYTHEVVTLWYRAPEIlLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEidqlfRIFRTLgtpdevvwp 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 237 -------IKGKYKMNPRQ-WSHI----SESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd07860   227 gvtsmpdYKPSFPKWARQdFSKVvpplDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
12-286 8.69e-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: 120.80  E-value: 8.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstegKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd05599     3 FEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLE--------KEQVAHVRAERDILAEADNPWVVKLYYSFQDEE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd05599    75 NLYLIMEFLPGGDMMTLLMKKD----TLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGH---IKLSDFGL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLvAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGtkerlfEGIIKGKYK-MNPRQW-- 248
Cdd:cd05599   148 CTGLKKSHL-AYSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCS------DDPQETCRKiMNWRETlv 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039796143 249 ----SHISESAKDLVRRmLMLDPAERI---TVYEALNHPWLKERD 286
Cdd:cd05599   221 fppeVPISPEAKDLIER-LLCDAEHRLganGVEEIKSHPFFKGVD 264
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
18-278 9.15e-30

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: 119.27  E-value: 9.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVdvakfTSSPGLSTEGKRWISnlkREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd14187    15 LGKGGFAKCYEITDADTKEVFAGKIV-----PKSLLLKPHQKEKMS---MEIAIHRSLAHQHVVGFHGFFEDNDFVYVVL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGE 177
Cdd:cd14187    87 ELCRRRSL-LELHKRRKA---LTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFL---NDDMEVKIGDFGLATKVEY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT--KERLFEgIIKGKYKMnPRqwsHISESA 255
Cdd:cd14187   160 DGERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSclKETYLR-IKKNEYSI-PK---HINPVA 234
                         250       260
                  ....*....|....*....|...
gi 1039796143 256 KDLVRRMLMLDPAERITVYEALN 278
Cdd:cd14187   235 ASLIQKMLQTDPTARPTINELLN 257
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
17-287 1.04e-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: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAkftsspGLSTEGKRWISNLKreasICHMLKHPHIVELLETYSSDGMLYMV 96
Cdd:cd06605     8 ELGEGNGGVVSKVRHRPSGQIMAVKVIRLE------IDEALQKQILRELD----VLHKCNSPYIVGFYGAFYSEGDISIC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHDN-NIIHRDVKPHCVLLASKENsapVKLGGFGVAIQL 175
Cdd:cd06605    78 MEYMDGGSLD-KILKEVGR---IPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQ---VKLCDFGVSGQL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GESglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF-------YGTKERLFEGIIKGKykmNPRQW 248
Cdd:cd06605   151 VDS--LAKTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYpppnakpSMMIFELLSYIVDEP---PPLLP 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039796143 249 SHI-SESAKDLVRRMLMLDPAERITVYEALNHPWLKERDR 287
Cdd:cd06605   226 SGKfSPDFQDFVSQCLQKDPTERPSYKELMEHPFIKRYEY 265
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
720-888 1.06e-29

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: 116.05  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 720 LVLLGAHGVGRRHIKNTLITKHPDrFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLE 799
Cdd:TIGR03263   3 IVISGPSGAGKSTLVKALLEEDPN-LKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTPKS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 800 TIRKIHEQGLIAILDVEPQ-ALKVLRTAEFAPFvVFIAAPTItpglneDESLQRLQK-----ESDVLQR--------TYA 865
Cdd:TIGR03263  82 PVEEALAAGKDVLLEIDVQgARQVKKKFPDAVS-IFILPPSL------EELERRLRKrgtdsEEVIERRlakakkeiAHA 154
                         170       180
                  ....*....|....*....|...
gi 1039796143 866 HYFDLTIINNEIDETIRHLEEAV 888
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 ...
18-280 5.37e-29

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: 116.70  E-value: 5.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRE-TGQQFAVKIVDVAKFTSSPGLstegkrwisnLKREASICHMLKHPHIVELLETYSSDGMLYMV 96
Cdd:cd14120     1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKSQNL----------LGKEIKILKELSHENVVALLDCQETSSSVYLV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLL--ASKENSAP----VKLGGFG 170
Cdd:cd14120    71 MEYCNGGDLADYLQAKG----TLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLshNSGRKPSPndirLKIADFG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLfegiiKGKYKMN----P 245
Cdd:cd14120   147 FARFL-QDGMMAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAqTPQEL-----KAFYEKNanlrP 220
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1039796143 246 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd14120   221 NIPSGTSPALKDLLLGLLKRNPKDRIDFEDFFSHP 255
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
16-282 6.95e-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: 116.65  E-value: 6.95e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQ-QFAVKIVDVAKFTSSPGLstegkrwisnLKREASICHMLKHPHIVELLETYSSDGMLY 94
Cdd:cd14202     8 DLIGHGAFAVVFKGRHKEKHDlEVAVKCINKKNLAKSQTL----------LGKEIKILKELKHENIVALYDFQEIANSVY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  95 MVFEFMDGADLcfeivkradAGFVYSEAVASH-----YMRQILEALRYCHDNNIIHRDVKPHCVLLA------SKENSAP 163
Cdd:cd14202    78 LVMEYCNGGDL---------ADYLHTMRTLSEdtirlFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrkSNPNNIR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 164 VKLGGFGVAIQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKM 243
Cdd:cd14202   149 IKIADFGFARYL-QNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSL 227
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1039796143 244 NPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14202   228 SPNIPRETSSHLRQLLLGLLQRNQKDRMDFDEFFHHPFL 266
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
11-280 9.00e-29

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: 116.25  E-value: 9.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftsspglSTEGKRWISNLKREASICHMLKHPHIVELLETYSSD 90
Cdd:cd06613     1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVI-----------KLEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFG 170
Cdd:cd06613    70 DKLWIVMEYCGGGSLQ-DIYQVTGP---LSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTE---DGDVKLADFG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLGESGLVAGGRVGTPHFMAPEVV---KREPYGKPVDVWGCGVILFILLSGCLPFYGTKER--LFegiIKGKYKMNP 245
Cdd:cd06613   143 VSAQLTATIAKRKSFIGTPYWMAPEVAaveRKGGYDGKCDIWALGITAIELAELQPPMFDLHPMraLF---LIPKSNFDP 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1039796143 246 ------RQWS---HisesakDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd06613   220 pklkdkEKWSpdfH------DFIKKCLTKNPKKRPTATKLLQHP 257
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
12-283 9.36e-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: 116.18  E-value: 9.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglsTEGKRWISNlkrEASICHMLKHPHIVELLETYSSDG 91
Cdd:cd06647     9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQ--------QPKKELIIN---EILVMRENKNPNIVNYLDSYLVGD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCfEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGV 171
Cdd:cd06647    78 ELWVVMEYLAGGSLT-DVVTET----CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGM---DGSVKLTDFGF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHI 251
Cdd:cd06647   150 CAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKL 229
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1039796143 252 SESAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd06647   230 SAIFRDFLNRCLEMDVEKRGSAKELLQHPFLK 261
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
18-281 1.03e-28

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: 115.88  E-value: 1.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVdvakftssPGLSTEgkrwISNLKREASI-CHMLKHPHIVELLETY-SSDGMLYM 95
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFV--------PKPSTK----LKDFLREYNIsLELSVHPHIIKTYDVAfETEDYYVF 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLcFEIVKrADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGFGVAIQl 175
Cdd:cd13987    69 AQEYAPYGDL-FSIIP-PQVGL--PEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRR-VKLCDFGLTRR- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 gesglvAGGRV----GTPHFMAPEV---VKREPY--GKPVDVWGCGVILFILLSGCLP---------FYgtkeRLFEGII 237
Cdd:cd13987   143 ------VGSTVkrvsGTIPYTAPEVceaKKNEGFvvDPSIDVWAFGVLLFCCLTGNFPwekadsddqFY----EEFVRWQ 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1039796143 238 KGKYKMNPRQWSHISESAKDLVRRMLMLDPAERIT---VYEALNHPW 281
Cdd:cd13987   213 KRKNTAVPSQWRRFTPKALRMFKKLLAPEPERRCSikeVFKYLGDRW 259
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
12-278 1.76e-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: 115.53  E-value: 1.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakFTSSPGLSTEGKRWISNLKREASICHML-KHPHIVELLETYSSD 90
Cdd:cd13993     2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCL----YKSGPNSKDGNDFQKLPQLREIDLHRRVsRHPNIITLHDVFETE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLcFEIVkRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLGGFG 170
Cdd:cd13993    78 VAIYIVLEYCPNGDL-FEAI-TENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGT--VKLCDFG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLGESGLVaggRVGTPHFMAPEVV-----KREPYG-KPVDVWGCGVILFILLSGCLPF-------------YGTKER 231
Cdd:cd13993   154 LATTEKISMDF---GVGSEFYMAPECFdevgrSLKGYPcAAGDIWSLGIILLNLTFGRNPWkiasesdpifydyYLNSPN 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1039796143 232 LFegiikgkykmnpRQWSHISESAKDLVRRMLMLDPAERITVYEALN 278
Cdd:cd13993   231 LF------------DVILPMSDDFYNLLRQIFTVNPNNRILLPELQL 265
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
12-280 4.45e-28

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: 115.00  E-value: 4.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELcEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspgLSTEGKRWISNLKREasICHMLKHPHIVELLETYSSDG 91
Cdd:cd05607     5 YEF-RVLGKGGFGEVCAVQVKNTGQMYACKKLDKKR------LKKKSGEKMALLEKE--ILEKVNSPFIVSLAYAFETKT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd05607    76 HLCLVMSLMNGGDLKYHIYNVGERGIEMERVI--FYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGN---CRLSDLGL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGEsGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSH- 250
Cdd:cd05607   151 AVEVKE-GKPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELKRRTLEDEVKFEHq 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1039796143 251 -ISESAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd05607   230 nFTEEAKDICRLFLAKKPENRLGSRTNDDDP 260
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
12-282 5.08e-28

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: 113.90  E-value: 5.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftsspglsTEGKRWISNLKREASICHMLK------HPHIVELLE 85
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKII------------KNNKDYLDQSLDEIRLLELLNkkdkadKYHIVRLKD 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  86 TYSSDGMLYMVFEfMDGADLcFEIVKraDAGFVY-SEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApV 164
Cdd:cd14133    69 VFYFKNHLCIVFE-LLSQNL-YEFLK--QNKFQYlSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQ-I 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 165 KLGGFGVAIQLGEsglvaggRVGT----PHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFEG 235
Cdd:cd14133   144 KIIDFGSSCFLTQ-------RLYSyiqsRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEvdqlaRIIGT 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039796143 236 IIKGKYKMnprqwshISESA------KDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14133   217 IGIPPAHM-------LDQGKaddelfVDFLKKLLEIDPKERPTASQALSHPWL 262
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
720-885 5.57e-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: 5.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 720 LVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLE 799
Cdd:cd00071     2 IVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSKA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 800 TIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPtitpglnedeslqrlqkesdvlqrtyahyfDLTIINNEIDE 879
Cdd:cd00071    82 AVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP------------------------------DYVIVNDDLEK 131

                  ....*.
gi 1039796143 880 TIRHLE 885
Cdd:cd00071   132 AYEELK 137
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
12-276 8.36e-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: 113.75  E-value: 8.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQF-AVKIVdvakFTSSPGL---STEGKRWISNLKREASIC-HMLKHPHIVELLET 86
Cdd:cd08528     2 YAVLELLGSGAFGCVYKVRKKSNGQTLlALKEI----NMTNPAFgrtEQERDKSVGDIISEVNIIkEQLRHPNIVRYYKT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCH-DNNIIHRDVKPHCVLLASKENsapVK 165
Cdd:cd08528    78 FLENDRLYIVMELIEGAPLGEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDK---VT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 166 LGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKmn 244
Cdd:cd08528   155 ITDFGLAKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMlTLATKIVEAEYE-- 232
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1039796143 245 PRQWSHISESAKDLVRRMLMLDPAERITVYEA 276
Cdd:cd08528   233 PLPEGMYSDDITFVIRSCLTPDPEARPDIVEV 264
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
12-283 1.03e-27

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: 114.05  E-value: 1.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglsTEGKRWISNlkrEASICHMLKHPHIVELLETYSSDG 91
Cdd:cd06655    21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQK--------QPKKELIIN---EILVMKELKNPNIVNFLDSFLVGD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCfEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGV 171
Cdd:cd06655    90 ELFVVMEYLAGGSLT-DVVTET----CMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMD---GSVKLTDFGF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEGIIKGKYKM-NPRQW 248
Cdd:cd06655   162 CAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENplRALYLIATNGTPELqNPEKL 241
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1039796143 249 SHIsesAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd06655   242 SPI---FRDFLNRCLEMDVEKRGSAKELLQHPFLK 273
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
9-282 1.23e-27

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: 113.58  E-value: 1.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglsTEGKRWISNLKREASICHMLKHPHIVELLETYS 88
Cdd:cd06643     4 EDFWEIVGELGDGAFGKVYKAQNKETGILAAAKVID-----------TKSEEELEDYMVEIDILASCDHPNIVKLLDAFY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGA--DLCFEIVKRAdagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKL 166
Cdd:cd06643    73 YENNLWILIEFCAGGavDAVMLELERP-----LTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGD---IKL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAIQLGESGLVAGGRVGTPHFMAPEVV-----KREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGK 240
Cdd:cd06643   145 ADFGVSAKNTRTLQRRDSFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPmRVLLKIAKSE 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1039796143 241 YKM--NPRQWshiSESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd06643   225 PPTlaQPSRW---SPEFKDFLRKCLEKNVDARWTTSQLLQHPFV 265
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
16-281 1.50e-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: 112.87  E-value: 1.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftSSPGLSTEgkrwISNLKREASICHMLKHPHIVELLETYSSDG--ML 93
Cdd:cd06651    13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQFDP--ESPETSKE----VSALECEIQLLKNLQHERIVQYYGCLRDRAekTL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  94 YMVFEFMDGAdlcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLlasKENSAPVKLGGFGVAI 173
Cdd:cd06651    87 TIFMEYMPGG----SVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDFGASK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 174 QLGE---SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFygTKERLFEGIIK-GKYKMNPRQWS 249
Cdd:cd06651   160 RLQTicmSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW--AEYEAMAAIFKiATQPTNPQLPS 237
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1039796143 250 HISESAKDLVRRmLMLDPAERITVYEALNHPW 281
Cdd:cd06651   238 HISEHARDFLGC-IFVEARHRPSAEELLRHPF 268
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
17-271 1.54e-27

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


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 114.03  E-value: 1.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFS---VVRRCINRETGQQFAVKIVDVAKFTSSPGLSTegkrwisnlKREASICHMLKHPHIVELLETYSSDGML 93
Cdd:cd05582     2 VLGQGSFGkvfLVRKITGPDAGTLYAMKVLKKATLKVRDRVRT---------KMERDILADVNHPFIVKLHYAFQTEGKL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  94 YMVFEFMDGADLCFEIVKRadagFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAI 173
Cdd:cd05582    73 YLILDFLRGGDLFTRLSKE----VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDE---DGHIKLTDFGLSK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 174 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT-KERLFEGIIKGKYKMnPRqwsHIS 252
Cdd:cd05582   146 ESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKdRKETMTMILKAKLGM-PQ---FLS 221
                         250
                  ....*....|....*....
gi 1039796143 253 ESAKDLVRRMLMLDPAERI 271
Cdd:cd05582   222 PEAQSLLRALFKRNPANRL 240
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
17-271 1.84e-27

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: 113.05  E-value: 1.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLstEGKrwisnlKREASICHMLKHPHIVELLETYSSDGMLYMV 96
Cdd:cd05608     8 VLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGY--EGA------MVEKRILAKVHSRFIVSLAYAFQTKTDLCLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMDGADLCFEI--VKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQ 174
Cdd:cd05608    80 MTIMNGGDLRYHIynVDEENPGF--QEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLL---DDDGNVRISDLGLAVE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 175 LGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWS-HISE 253
Cdd:cd05608   155 LKDGQTKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARGEKVENKELKQRILNDSVTYSeKFSP 234
                         250
                  ....*....|....*...
gi 1039796143 254 SAKDLVRRMLMLDPAERI 271
Cdd:cd05608   235 ASKSICEALLAKDPEKRL 252
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
10-282 2.08e-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: 111.93  E-value: 2.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRET-------GQQFAVKIVDVakfTSSPglstegKRwISNlkrEASICHMLK-HPHIV 81
Cdd:cd14019     1 NKYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIYP---TSSP------SR-ILN---ELECLERLGgSNNVS 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  82 ELLETYSSDGMLYMVFEFMDGADlcfeivkRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENS 161
Cdd:cd14019    68 GLITAFRNEDQVVAVLPYIEHDD-------FRDFYRKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLY-NRETG 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 162 APVkLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKERlFEGIIkgk 240
Cdd:cd14019   140 KGV-LVDFGLAQREEDRPEQRAPRAGTRGFRAPEVLFKCPHqTTAIDIWSAGVILLSILSGRFPFFFSSDD-IDALA--- 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1039796143 241 ykmnprQWSHI--SESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14019   215 ------EIATIfgSDEAYDLLDKLLELDPSKRITAEEALKHPFF 252
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
720-889 2.09e-27

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 110.16  E-value: 2.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 720 LVLLGAHGVGRRHIKNTLITKHPDrFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLE 799
Cdd:COG0194     5 IVLSGPSGAGKTTLVKALLERDPD-LRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLEWAEVHGNYYGTPKA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 800 TIRKIHEQGLIAILDVEPQ-ALKVLRTAEFAPFvVFIAAPTItpglneDESLQRL----QKESDVLQR---------TYA 865
Cdd:COG0194    84 EVEEALAAGKDVLLEIDVQgARQVKKKFPDAVS-IFILPPSL------EELERRLrgrgTDSEEVIERrlakareelAHA 156
                         170       180
                  ....*....|....*....|....
gi 1039796143 866 HYFDLTIINNEIDETIRHLEEAVE 889
Cdd:COG0194   157 DEFDYVVVNDDLDRAVEELKAIIR 180
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
16-282 2.69e-27

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: 112.09  E-value: 2.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKfTSSPGLSTEGKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd06629     7 ELIGKGTYGRVYLAMNATTGEMLAVKQVELPK-TSSDRADSRQKTVVDALKSEIDTLKDLDHPNIVQYLGFEETEDYFSI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADL--CFeivkRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAI 173
Cdd:cd06629    86 FLEYVPGGSIgsCL----RKYGKF--EEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGI---CKISDFGISK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 174 Q----LGESGlvAGGRVGTPHFMAPEVV--KREPYGKPVDVWGCGVILFILLSGCLPFygTKERLFEGIIK-GKYKMNP- 245
Cdd:cd06629   157 KsddiYGNNG--ATSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPW--SDDEAIAAMFKlGNKRSAPp 232
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039796143 246 -RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd06629   233 vPEDVNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
12-281 2.97e-27

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: 113.18  E-value: 2.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVK--IVDVAKftsspglstEGKRwISNLkREASICHMLKHPHIVELLE---- 85
Cdd:cd07866    10 YEILGKLGEGTFGEVYKARQIKTGRVVALKkiLMHNEK---------DGFP-ITAL-REIKILKKLKHPNVVPLIDmave 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  86 ----TYSSDGMLYMVFEFMDgADLCfEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENs 161
Cdd:cd07866    79 rpdkSKRKRGSVYMVTPYMD-HDLS-GLLENPSVKL--TESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGI- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 162 apVKLGGFGVA------IQLGESGLVAGGR-----VGTPHFMAPEVV---KRepYGKPVDVWGCGVILFILLSG------ 221
Cdd:cd07866   154 --LKIADFGLArpydgpPPNPKGGGGGGTRkytnlVVTRWYRPPELLlgeRR--YTTAVDIWGIGCVFAEMFTRrpilqg 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 222 -------------C-------------LPfyGTKERLFEGIIKGKYKMnpRQWSHISESAkDLVRRMLMLDPAERITVYE 275
Cdd:cd07866   230 ksdidqlhlifklCgtpteetwpgwrsLP--GCEGVHSFTNYPRTLEE--RFGKLGPEGL-DLLSKLLSLDPYKRLTASD 304

                  ....*.
gi 1039796143 276 ALNHPW 281
Cdd:cd07866   305 ALEHPY 310
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
12-282 3.52e-27

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: 111.75  E-value: 3.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKI---VDVAKFtsSPGLSTEGKRwisnlkrEASICHMLKHPHIVELLETYS 88
Cdd:cd08222     2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVlkeISVGEL--QPDETVDANR-------EAKLLSKLDHPAIVKFHDSFV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLasKENSapVKLGG 168
Cdd:cd08222    73 EKESFCIVTEYCEGGDLDDKISEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL--KNNV--IKVGD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLsgCLpfygtkERLFEG---------IIKG 239
Cdd:cd08222   149 FGISRILMGTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMC--CL------KHAFDGqnllsvmykIVEG 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1039796143 240 KykmNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd08222   221 E---TPSLPDKYSKELNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
12-284 4.59e-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: 4.59e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglstEGKRWISnlkREASICHMLKHPHIVELLE-TYSSD 90
Cdd:cd14137     6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVL------------QDKRYKN---RELQIMRRLKHPNIVKLKYfFYSSG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 G-----MLYMVFEFMDGaDLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLasKENSAPVK 165
Cdd:cd14137    71 EkkdevYLNLVMEYMPE-TLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLV--DPETGVLK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 166 LGGFGVAIQlgesgLVAGGR----VGTPHFMAPE-VVKREPYGKPVDVWGCG-VILFILLSGCLpFYGTK--ERLFEgII 237
Cdd:cd14137   148 LCDFGSAKR-----LVPGEPnvsyICSRYYRAPElIFGATDYTTAIDIWSAGcVLAELLLGQPL-FPGESsvDQLVE-II 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 238 K--GK------YKMNP------------RQWS-----HISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd14137   221 KvlGTptreqiKAMNPnytefkfpqikpHPWEkvfpkRTPPDAIDLLSKILVYNPSKRLTALEALAHPFFDE 292
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
10-281 4.69e-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: 111.93  E-value: 4.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvaKFTSSpglsTEGKRwISNLkREASICHMLKHPHIVELLETYSS 89
Cdd:cd07843     5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKL---KMEKE----KEGFP-ITSL-REINILLKLQHPNIVTVKEVVVG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGM--LYMVFEFMDgADLCfEIVKRADAGFVYSEaVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLG 167
Cdd:cd07843    76 SNLdkIYMVMEYVE-HDLK-SLMETMKQPFLQSE-VKC-LMLQLLSGVAHLHDNWILHRDLKTSNLLL---NNRGILKIC 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLF-------E 234
Cdd:cd07843   149 DFGLAREYGSPLKPYTQLVVTLWYRAPELLLGAKeYSTAIDMWSVGCIFAELLTKKPLFPGKSEidqlnKIFkllgtptE 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 235 GI---------IKGKYKMNPRQW--------SHISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd07843   229 KIwpgfselpgAKKKTFTKYPYNqlrkkfpaLSLSDNGFDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
18-283 4.86e-27

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: 112.05  E-value: 4.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglstEGKRWIsnLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd06658    30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRK---------QQRREL--LFNEVVIMRDYHHENVVDMYNSYLVGDELWVVM 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLCfEIVKRADAGfvySEAVASHYMrQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGE 177
Cdd:cd06658    99 EFLEGGALT-DIVTHTRMN---EEQIATVCL-SVLRALSYLHNQGVIHRDIKSDSILLTS---DGRIKLSDFGFCAQVSK 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYgtKERLFEGIIKGKYKMNPR-QWSH-ISESA 255
Cdd:cd06658   171 EVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYF--NEPPLQAMRRIRDNLPPRvKDSHkVSSVL 248
                         250       260
                  ....*....|....*....|....*...
gi 1039796143 256 KDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd06658   249 RGFLDLMLVREPSQRATAQELLQHPFLK 276
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
18-280 4.93e-27

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: 110.94  E-value: 4.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKivdvakfTSSPGLSTEGKRwiSNLKREASICHMLK-HPHIVELLETYSSDGMLYMV 96
Cdd:cd13997     8 IGSGSFSEVFKVRSKVDGCLYAVK-------KSKKPFRGPKER--ARALREVEAHAALGqHPNIVRYYSSWEEGGHLYIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMDGADLCfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLG 176
Cdd:cd13997    79 MELCENGSLQ-DALEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGT---CKIGDFGLATRLE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 177 ESGLVaggRVGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGC-LPFYGTkerLFEGIIKGKYKMNPRqwSHISES 254
Cdd:cd13997   155 TSGDV---EEGDSRYLAPELLNENYtHLPKADIFSLGVTVYEAATGEpLPRNGQ---QWQQLRQGKLPLPPG--LVLSQE 226
                         250       260
                  ....*....|....*....|....*.
gi 1039796143 255 AKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd13997   227 LTRLLKVMLDPDPTRRPTADQLLAHD 252
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
10-284 5.79e-27

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: 112.05  E-value: 5.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglsTEGKRWISNLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd06644    12 EVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIE-----------TKSEEELEDYMVEIEILATCNHPYIVKLLGAFYW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLCfEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGF 169
Cdd:cd06644    81 DGKLWIMIEFCPGGAVD-AIMLELDRGL--TEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGD---IKLADF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGLVAGGRVGTPHFMAPEVV-----KREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYK- 242
Cdd:cd06644   155 GVSAKNVKTLQRRDSFIGTPYWMAPEVVmcetmKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPmRVLLKIAKSEPPt 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1039796143 243 -MNPRQWshiSESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd06644   235 lSQPSKW---SMEFRDFLKTALDKHPETRPSAAQLLEHPFVSS 274
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
12-263 6.83e-27

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: 113.24  E-value: 6.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvAKFtsspglstegkrwiSNLKREASIC-----HMLKH---PHIVEL 83
Cdd:cd05596    28 FDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLL--SKF--------------EMIKRSDSAFfweerDIMAHansEWIVQL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  84 LETYSSDGMLYMVFEFMDGADLCfEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAP 163
Cdd:cd05596    92 HYAFQDDKYLYMVMDYMPGGDLV-NLMSNYD----VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDA---SGH 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 164 VKLGGFGVAIQLGESGLV-AGGRVGTPHFMAPEVVKREP----YGKPVDVWGCGVILFILLSGCLPFY-----GTkerlF 233
Cdd:cd05596   164 LKLADFGTCMKMDKDGLVrSDTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYadslvGT----Y 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 1039796143 234 EGIIKGKYKMNPRQWSHISESAKDLVRRML 263
Cdd:cd05596   240 GKIMNHKNSLQFPDDVEISKDAKSLICAFL 269
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
10-283 6.98e-27

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: 111.62  E-value: 6.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspGLSTEgkrwisnLKREASICHML-KHPHIVELLET-Y 87
Cdd:cd06639    22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPIS-----DVDEE-------IEAEYNILRSLpNHPNVVKFYGMfY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSD----GMLYMVFEFMDGADLCfEIVKRA-DAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensA 162
Cdd:cd06639    90 KADqyvgGQLWLVLELCNGGSVT-ELVKGLlKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTE---G 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 163 PVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKRE-----PYGKPVDVWGCGVILFILLSGCLPFYGTKErlfegiI 237
Cdd:cd06639   166 GVKLVDFGVSAQLTSARLRRNTSVGTPFWMAPEVIACEqqydySYDARCDVWSLGITAIELADGDPPLFDMHP------V 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039796143 238 KGKYK---------MNPRQWshiSESAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd06639   240 KALFKiprnppptlLNPEKW---CRGFSHFISQCLIKDFEKRPSVTHLLEHPFIK 291
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
9-282 7.55e-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: 110.39  E-value: 7.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglstEGKRWISnlkREASICHMLKHPHIVELLETYS 88
Cdd:cd14110     2 EKTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKP---------EDKQLVL---REYQVLRRLSHPRIAQLHSAYL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnsaPVKLGG 168
Cdd:cd14110    70 SPRHLVLIEELCSGPELLYNLAERN----SYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKN---LLKIVD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLG-ESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY--GTKERLfEGIIKGKYKMNp 245
Cdd:cd14110   143 LGNAQPFNqGKVLMTDKKGDYVETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSsdLNWERD-RNIRKGKVQLS- 220
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1039796143 246 RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14110   221 RCYAGLSGGAVNFLKSTLCAKPWGRPTASECLQNPWL 257
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
10-287 1.01e-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: 110.72  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakFTSSpgLSTEGKRwiSNLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd14117     6 DDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVL----FKSQ--IEKEGVE--HQLRREIEIQSHLRHPNILRLYNYFHD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGF 169
Cdd:cd14117    78 RKRIYLILEYAPRGELYKELQKHGR----FDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYK---GELKIADF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQlgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF-YGTKERLFEGIIKGKYKMNPrqw 248
Cdd:cd14117   151 GWSVH--APSLRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFeSASHTETYRRIVKVDLKFPP--- 225
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1039796143 249 sHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDR 287
Cdd:cd14117   226 -FLSDGSRDLISKLLRYHPSERLPLKGVMEHPWVKANSR 263
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
12-279 1.05e-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: 110.52  E-value: 1.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftSSPGLSTEgkrwISNLKREASICHMLKHPHIVELLETY--SS 89
Cdd:cd06652     4 WRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQFDP--ESPETSKE----VNALECEIQLLKNLLHERIVQYYGCLrdPQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGAdlcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLlasKENSAPVKLGGF 169
Cdd:cd06652    78 ERTLSIFMEYMPGG----SIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANIL---RDSVGNVKLGDF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGLVAGGR---VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFygTKERLFEGIIK-GKYKMNP 245
Cdd:cd06652   151 GASKRLQTICLSGTGMksvTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPW--AEFEAMAAIFKiATQPTNP 228
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796143 246 RQWSHISESAKDLVRRMLmLDPAERITVYEALNH 279
Cdd:cd06652   229 QLPAHVSDHCRDFLKRIF-VEAKLRPSADELLRH 261
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
12-271 1.38e-26

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: 112.10  E-value: 1.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstegKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd05593    17 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIA--------KDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGV 171
Cdd:cd05593    89 RLCFVMEYVNGGELFFHLSRER----VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLML---DKDGHIKITDFGL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnPRQwsh 250
Cdd:cd05593   162 CKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDhEKLFELILMEDIKF-PRT--- 237
                         250       260
                  ....*....|....*....|.
gi 1039796143 251 ISESAKDLVRRMLMLDPAERI 271
Cdd:cd05593   238 LSADAKSLLSGLLIKDPNKRL 258
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
16-271 1.44e-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: 111.60  E-value: 1.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstegKRWISNLKREASIC-HMLKHPHIVELLETYSSDGMLY 94
Cdd:cd05603     1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILK--------KKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  95 MVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQ 174
Cdd:cd05603    73 FVLDYVNGGELFFHLQRER----CFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGH---VVLTDFGLCKE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 175 LGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMNPRQwshiSE 253
Cdd:cd05603   146 GMEPEETTSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDvSQMYDNILHKPLHLPGGK----TV 221
                         250
                  ....*....|....*...
gi 1039796143 254 SAKDLVRRMLMLDPAERI 271
Cdd:cd05603   222 AACDLLQGLLHKDQRRRL 239
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
16-282 1.82e-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: 111.21  E-value: 1.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglstegKRWISNLKREASI-------CHMLKHPHIVELLETYS 88
Cdd:cd05604     2 KVIGKGSFGKVLLAKRKRDGKYYAVKVLQ--------------KKVILNRKEQKHImaernvlLKNVKHPFLVGLHYSFQ 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGG 168
Cdd:cd05604    68 TTDKLYFVLDFVNGGELFFHLQRER----SFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGH---IVLTD 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGV---AIQLGESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMN 244
Cdd:cd05604   141 FGLckeGISNSDTTTTF---CGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDtAEMYENILHKPLVLR 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1039796143 245 PrqwsHISESAKDLVRRMLMLDPAERITVYEAL----NHPWL 282
Cdd:cd05604   218 P----GISLTAWSILEELLEKDRQLRLGAKEDFleikNHPFF 255
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
12-281 2.58e-26

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: 110.54  E-value: 2.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftSSPGLStegkrwISNLkREASICHMLKHPHIVELLETYSSD- 90
Cdd:cd07865    14 YEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMEN--EKEGFP------ITAL-REIKILQLLKHENVVNLIEICRTKa 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 -------GMLYMVFEFMDgADLcfeivkradAGFV------YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaS 157
Cdd:cd07865    85 tpynrykGSIYLVFEFCE-HDL---------AGLLsnknvkFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILI-T 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 158 KEnsAPVKLGGFGVA----IQLGESGLVAGGRVGTPHFMAPEVVKRE-PYGKPVDVWGCGVI------------------ 214
Cdd:cd07865   154 KD--GVLKLADFGLArafsLAKNSQPNRYTNRVVTLWYRPPELLLGErDYGPPIDMWGAGCImaemwtrspimqgnteqh 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 215 ---LFILLSGC-----------LPFYgTKERLFEGiikGKYKMNPRQWSHISE-SAKDLVRRMLMLDPAERITVYEALNH 279
Cdd:cd07865   232 qltLISQLCGSitpevwpgvdkLELF-KKMELPQG---QKRKVKERLKPYVKDpYALDLIDKLLVLDPAKRIDADTALNH 307

                  ..
gi 1039796143 280 PW 281
Cdd:cd07865   308 DF 309
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
10-284 2.96e-26

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 109.91  E-value: 2.96e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspgLSTEGKRWISNLKREASICHMLKHPHIVELLETYSS 89
Cdd:PLN00009    2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIR---------LEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDgadlcFEIVKRADAG--FVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLG 167
Cdd:PLN00009   73 EKRLYLVFEYLD-----LDLKKHMDSSpdFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNA--LKLA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVAIQLGESGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE--RLF----------E 234
Cdd:PLN00009  146 DFGLARAFGIPVRTFTHEVVTLWYRAPEIlLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEidELFkifrilgtpnE 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 235 GIIKG-----KYKMNPRQWS---------HISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:PLN00009  226 ETWPGvtslpDYKSAFPKWPpkdlatvvpTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKD 289
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
10-282 3.24e-26

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: 109.31  E-value: 3.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsSPGLSTEGKRWISNLKREASichmlkHPHIVELLETY-- 87
Cdd:cd06608     6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDI-----IEDEEEEIKLEINILRKFSN------HPNIATFYGAFik 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 ----SSDGMLYMVFEFMDGADLCfEIVKRA-DAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSA 162
Cdd:cd06608    75 kdppGGDDQLWLVMEYCGGGSVT-DLVKGLrKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLT---EEA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 163 PVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVV----KREP-YGKPVDVWGCGVILFILLSGCLPF---YGTKErLFE 234
Cdd:cd06608   151 EVKLVDFGVSAQLDSTLGRRNTFIGTPYWMAPEVIacdqQPDAsYDARCDVWSLGITAIELADGKPPLcdmHPMRA-LFK 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039796143 235 gIIKGKYK--MNPRQWSHiseSAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd06608   230 -IPRNPPPtlKSPEKWSK---EFNDFISECLIKNYEQRPFTEELLEHPFI 275
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
10-283 4.29e-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: 109.17  E-value: 4.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIV----DVAKFtsspglstegkrwiSNLKREASICHMLKHPHIVELLE 85
Cdd:cd06622     1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIrlelDESKF--------------NQIIMELDILHKAVSPYIVDFYG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  86 TYSSDGMLYMVFEFMDGADLcfeivKRADAGFVYSEAVASHYMRQILEA----LRYCHDN-NIIHRDVKPHCVLLASKen 160
Cdd:cd06622    67 AFFIEGAVYMCMEYMDAGSL-----DKLYAGGVATEGIPEDVLRRITYAvvkgLKFLKEEhNIIHRDVKPTNVLVNGN-- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 161 sAPVKLGGFGVAIQLGESglVAGGRVGTPHFMAPEVVKRE-PYGKPV-----DVWGCGVILFILLSGCLPF----YGTKE 230
Cdd:cd06622   140 -GQVKLCDFGVSGNLVAS--LAKTNIGCQSYMAPERIKSGgPNQNPTytvqsDVWSLGLSILEMALGRYPYppetYANIF 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039796143 231 RLFEGIIKGKykmNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd06622   217 AQLSAIVDGD---PPTLPSGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLV 266
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
12-271 5.30e-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: 110.50  E-value: 5.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstegKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd05594    27 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVA--------KDEVAHTLTENRVLQNSRHPFLTALKYSFQTHD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCH-DNNIIHRDVKPHCVLLaskENSAPVKLGGFG 170
Cdd:cd05594    99 RLCFVMEYANGGELFFHLSRER----VFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLML---DKDGHIKITDFG 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnPRQws 249
Cdd:cd05594   172 LCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDhEKLFELILMEEIRF-PRT-- 248
                         250       260
                  ....*....|....*....|..
gi 1039796143 250 hISESAKDLVRRMLMLDPAERI 271
Cdd:cd05594   249 -LSPEAKSLLSGLLKKDPKQRL 269
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
16-277 5.47e-26

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: 108.24  E-value: 5.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRetGQQFAVKIVD-VAKFTSSpglstegkrwISNLKREASICHmLKHPHIVELL-----ETYSS 89
Cdd:cd13979     9 EPLGSGGFGSVYKATYK--GETVAVKIVRrRRKNRAS----------RQSFWAELNAAR-LRHENIVRVLaaetgTDFAS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMvfEFMDGADLCFEIVKRADAGFVYSEAVashYMRQILEALRYCHDNNIIHRDVKPHCVLLAskENSAPvKLGGF 169
Cdd:cd13979    76 LGLIIM--EYCGNGTLQQLIYEGSEPLPLAHRIL---ISLDIARALRFCHSHGIVHLDVKPANILIS--EQGVC-KLCDF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGEsGLVAGGRV----GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIkgKYKMNP 245
Cdd:cd13979   148 GCSVKLGE-GNEVGTPRshigGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYAVV--AKDLRP 224
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1039796143 246 RQwSHISESA-----KDLVRRMLMLDPAERITVYEAL 277
Cdd:cd13979   225 DL-SGLEDSEfgqrlRSLISRCWSAQPAERPNADESL 260
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
17-286 5.56e-26

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: 109.78  E-value: 5.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKIV--DVAkftsspglstegkrwisnLKREASICHML---------KHPHIVELLE 85
Cdd:cd05592     2 VLGKGSFGKVMLAELKGTNQYFAIKALkkDVV------------------LEDDDVECTMIerrvlalasQHPFLTHLFC 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  86 TYSSDGMLYMVFEFMDGADLCFEIvkrADAGfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSapVK 165
Cdd:cd05592    64 TFQTESHLFFVMEYLNGGDLMFHI---QQSG-RFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLL-DREGH--IK 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 166 LGGFGVAIQ--LGESglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIikgkyk 242
Cdd:cd05592   137 IADFGMCKEniYGEN--KASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEdELFWSI------ 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039796143 243 MNPRQW--SHISESAKDLVRRMLMLDPAERITVYEAL-----NHPWLKERD 286
Cdd:cd05592   209 CNDTPHypRWLTKEAASCLSLLLERNPEKRLGVPECPagdirDHPFFKTID 259
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
10-284 6.38e-26

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: 110.08  E-value: 6.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKivdvaKFtSSPGLSTE-GKRwisnLKREASICHMLKHPHIVELLETYS 88
Cdd:cd07851    15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIK-----KL-SRPFQSAIhAKR----TYRELRLLKHMKHENVIGLLDVFT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGML------YMVFEFMdGADLcFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCvlLASKENSA 162
Cdd:cd07851    85 PASSLedfqdvYLVTHLM-GADL-NNIVKCQ----KLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSN--LAVNEDCE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 163 pVKLGGFGVAIQLGESglvAGGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGT------------- 228
Cdd:cd07851   157 -LKILDFGLARHTDDE---MTGYVATRWYRAPEIMlNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSdhidqlkrimnlv 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796143 229 ---KERLFEGI--------IKGKYKMNPRQWSHI----SESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd07851   233 gtpDEELLKKIssesarnyIQSLPQMPKKDFKEVfsgaNPLAIDLLEKMLVLDPDKRITAAEALAHPYLAE 303
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
12-271 6.48e-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: 110.11  E-value: 6.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVD---VAKFTSSPGLSTEGKRWISNLKreasichmlkHPHIVELLETYS 88
Cdd:cd05602     9 FHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQkkaILKKKEEKHIMSERNVLLKNVK----------HPFLVGLHFSFQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGG 168
Cdd:cd05602    79 TTDKLYFVLDYINGGELFYHLQRER----CFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGH---IVLTD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPrq 247
Cdd:cd05602   152 FGLCKENIEPNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSrNTAEMYDNILNKPLQLKP-- 229
                         250       260
                  ....*....|....*....|....
gi 1039796143 248 wsHISESAKDLVRRMLMLDPAERI 271
Cdd:cd05602   230 --NITNSARHLLEGLLQKDRTKRL 251
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
9-282 8.81e-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: 107.62  E-value: 8.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINR--ETGQQFAVKIVDVAKFTSspglstegkrwisNLKREASICHMLKHPHIVELLET 86
Cdd:cd14112     2 TGRFSFGSEIFRGRFSVIVKAVDSttETDAHCAVKIFEVSDEAS-------------EAVREFESLRTLQHENVQRLIAA 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYMVFEfmdgaDLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnSAPVKL 166
Cdd:cd14112    69 FKPSNFAYLVME-----KLQEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVR-SWQVKL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAIQLGESGLVAGGrvGTPHFMAPEVVKREPYGKP-VDVWGCGVILFILLSGCLPF---YGTKERLFEGIIKGKYK 242
Cdd:cd14112   143 VDFGRAQKVSKLGKVPVD--GDTDWASPEFHNPETPITVqSDIWGLGVLTFCLLSGFHPFtseYDDEEETKENVIFVKCR 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1039796143 243 MN--PRQwshISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14112   221 PNliFVE---ATQEALRFATWALKKSPTRRMRTDEALEHRWL 259
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
18-282 9.37e-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: 108.19  E-value: 9.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglstEGKRWIsnLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd06657    28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRK---------QQRREL--LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVM 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLCfEIVKRADAgfvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQLGE 177
Cdd:cd06657    97 EFLEGGALT-DIVTHTRM----NEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLT---HDGRVKLSDFGFCAQVSK 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKD 257
Cdd:cd06657   169 EVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNLHKVSPSLKG 248
                         250       260
                  ....*....|....*....|....*
gi 1039796143 258 LVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd06657   249 FLDRLLVRDPAQRATAAELLKHPFL 273
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
10-286 9.56e-26

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: 109.36  E-value: 9.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPF---SVVRRcinRETGQQFAVKIV---------DVAKFTSSPGLSTEG-KRWISNLkreasicHMlk 76
Cdd:cd05597     1 DDFEILKVIGRGAFgevAVVKL---KSTEKVYAMKILnkwemlkraETACFREERDVLVNGdRRWITKL-------HY-- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  77 hphivelleTYSSDGMLYMVFEFMDGADLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLa 156
Cdd:cd05597    69 ---------AFQDENYLYLVMDYYCGGDLLTLLSKFEDR---LPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLL- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 157 skENSAPVKLGGFGVAIQLGESGLVAGG-RVGTPHFMAPEVVK-----REPYGKPVDVWGCGVILFILLSGCLPFYGtkE 230
Cdd:cd05597   136 --DRNGHIRLADFGSCLKLREDGTVQSSvAVGTPDYISPEILQamedgKGRYGPECDWWSLGVCMYEMLYGETPFYA--E 211
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 231 RLFE--GII---KGKYKMnPRQWSHISESAKDLVRRmLMLDPAERI---TVYEALNHPWLKERD 286
Cdd:cd05597   212 SLVEtyGKImnhKEHFSF-PDDEDDVSEEAKDLIRR-LICSRERRLgqnGIDDFKKHPFFEGID 273
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
12-283 9.88e-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: 108.27  E-value: 9.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglsTEGKRWISNlkrEASICHMLKHPHIVELLETYSSDG 91
Cdd:cd06656    21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQ--------QPKKELIIN---EILVMRENKNPNIVNYLDSYLVGD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCfEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGV 171
Cdd:cd06656    90 ELWVVMEYLAGGSLT-DVVTET----CMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGM---DGSVKLTDFGF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEGIIKGKYKM-NPRQW 248
Cdd:cd06656   162 CAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENplRALYLIATNGTPELqNPERL 241
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1039796143 249 SHIsesAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd06656   242 SAV---FRDFLNRCLEMDVDRRGSAKELLQHPFLK 273
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
9-304 1.07e-25

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: 107.84  E-value: 1.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkftsspglstEGKRWISNLKREASICHMLKHPHIVELLETYS 88
Cdd:cd06642     3 EELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLE----------EAEDEIEDIQQEITVLSQCDSPYITRYYGSYL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADlCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGG 168
Cdd:cd06642    73 KGTKLWIIMEYLGGGS-ALDLLKPGP----LEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGD---VKLAD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKykmNPRQ 247
Cdd:cd06642   145 FGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPmRVLFLIPKNS---PPTL 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796143 248 WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKerdRYAYKIH-LPETVEQLRKF 304
Cdd:cd06642   222 EGQHSKPFKEFVEACLNKDPRFRPTAKELLKHKFIT---RYTKKTSfLTELIDRYKRW 276
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
12-283 1.13e-25

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: 108.48  E-value: 1.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTsspglstegKRwiSNLKR---EASICHMLKHPHIVELLETYS 88
Cdd:cd05574     3 FKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMI---------KR--NKVKRvltEREILATLDHPFLPTLYASFQ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLcFEIVKRAdAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLL------------- 155
Cdd:cd05574    72 TSTHLCFVMDYCPGGEL-FRLLQKQ-PGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLhesghimltdfdl 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 156 ---ASKENSAPVKLGGFGVAIQLGESGL------VAGGR----VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGC 222
Cdd:cd05574   150 skqSSVTPPPVRKSLRKGSRRSSVKSIEketfvaEPSARsnsfVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGT 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796143 223 LPFYG-TKERLFEGIIKGK--YKMNPrqwsHISESAKDLVRRMLMLDPAERI----TVYEALNHPWLK 283
Cdd:cd05574   230 TPFKGsNRDETFSNILKKEltFPESP----PVSSEAKDLIRKLLVKDPSKRLgskrGASEIKRHPFFR 293
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
12-286 1.28e-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: 108.94  E-value: 1.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvaKFtsspglSTEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd05601     3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLK--KS------ETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGV 171
Cdd:cd05601    75 NLYLVMEYHPGGDL-LSLLSRYDDIF--EESMARFYLAELVLAIHSLHSMGYVHRDIKPENILI---DRTGHIKLADFGS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLV-AGGRVGTPHFMAPEV------VKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKM 243
Cdd:cd05601   149 AAKLSSDKTVtSKMPVGTPDYIAPEVltsmngGSKGTYGVECDWWSLGIVAYEMLYGKTPFTEdTVIKTYSNIMNFKKFL 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1039796143 244 NPRQWSHISESAKDLVRRmLMLDPAERITvYEAL-NHPWLKERD 286
Cdd:cd05601   229 KFPEDPKVSESAVDLIKG-LLTDAKERLG-YEGLcCHPFFSGID 270
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
12-281 1.28e-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: 107.03  E-value: 1.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsSPGlSTEGKRWISNLKREASICHMLKHPHIVELLETYS--S 89
Cdd:cd06653     4 WRLGKLLGRGAFGEVYLCYDADTGRELAVKQVPF-----DPD-SQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRdpE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGAdlcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLlasKENSAPVKLGGF 169
Cdd:cd06653    78 EKKLSIFVEYMPGG----SVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANIL---RDSAGNVKLGDF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVA--IQ-LGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFygTKERLFEGIIK-GKYKMNP 245
Cdd:cd06653   151 GASkrIQtICMSGTGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPW--AEYEAMAAIFKiATQPTKP 228
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039796143 246 RQWSHISESAKDLVRRmLMLDPAERITVYEALNHPW 281
Cdd:cd06653   229 QLPDGVSDACRDFLRQ-IFVEEKRRPTAEFLLRHPF 263
PDZ_MPP3-MPP4-MPP7-like cd06799
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ...
494-575 1.34e-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: 100.78  E-value: 1.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 494 VRLVqfqKNtDEPMGITLKMNELNHCI-VARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFK 572
Cdd:cd06799     3 VRLV---KN-NEPLGATIKRDEKTGAIvVARIMRGGAADRSGLIHVGDELREVNGISVEGKDPEEVIQILANSQGPITFK 78

                  ...
gi 1039796143 573 IVP 575
Cdd:cd06799    79 LIP 81
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
12-281 1.34e-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: 1.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspgLSTEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd07839     2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVR---------LDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDgADLcfeiVKRADA--GFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGF 169
Cdd:cd07839    73 KLTLVFEYCD-QDL----KKYFDScnGDIDPEIVKS-FMFQLLKGLAFCHSHNVLHRDLKPQNLLI---NKNGELKLADF 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGLVAGGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFY----------------GT-KER 231
Cdd:cd07839   144 GLARAFGIPVRCYSAEVVTLWYRPPDVLfGAKLYSTSIDMWSAGCIFAELANAGRPLFpgndvddqlkrifrllGTpTEE 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 232 LFEGIIK-GKYKMNPRQ-----WSHI----SESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd07839   224 SWPGVSKlPDYKPYPMYpattsLVNVvpklNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
10-298 1.52e-25

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: 110.09  E-value: 1.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglSTEGKRWisnlkREASICHMLKHPHIVELLETYSS 89
Cdd:cd05622    73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKR---SDSAFFW-----EERDIMAFANSPWVVQLFYAFQD 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLCfEIVKRADAgfvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGF 169
Cdd:cd05622   145 DRYLYMVMEYMPGGDLV-NLMSNYDV----PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL---DKSGHLKLADF 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGLV-AGGRVGTPHFMAPEVVKREP----YGKPVDVWGCGVILFILLSGCLPFY-----GTkerlFEGIIKG 239
Cdd:cd05622   217 GTCMKMNKEGMVrCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYadslvGT----YSKIMNH 292
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 240 KYKMNPRQWSHISESAKDLVRRMLMlDPAERI---TVYEALNHPWLKErDRYAYKiHLPETV 298
Cdd:cd05622   293 KNSLTFPDDNDISKEAKNLICAFLT-DREVRLgrnGVEEIKRHLFFKN-DQWAWE-TLRDTV 351
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
9-280 1.63e-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: 108.01  E-value: 1.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIvdvakftsspgLSTEGKRWIsnlKREASICHMLK-HPHIVELL--- 84
Cdd:cd14132    17 QDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKV-----------LKPVKKKKI---KREIKILQNLRgGPNIVKLLdvv 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  85 -----ETYSsdgmlyMVFEFMDGADLcfeivKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE 159
Cdd:cd14132    83 kdpqsKTPS------LIFEYVNNTDF-----KTLYPTLTDYDIR--YYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 160 NSapVKLGGFGVA----------IqlgesglvaggRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFY-- 226
Cdd:cd14132   150 RK--LRLIDWGLAefyhpgqeynV-----------RVASRYYKGPELlVDYQYYDYSLDMWSLGCMLASMIFRKEPFFhg 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 227 --------------GTKErLFE-----GI--------IKGKYKMNPrqWSH---------ISESAKDLVRRMLMLDPAER 270
Cdd:cd14132   217 hdnydqlvkiakvlGTDD-LYAyldkyGIelpprlndILGRHSKKP--WERfvnsenqhlVTPEALDLLDKLLRYDHQER 293
                         330
                  ....*....|
gi 1039796143 271 ITVYEALNHP 280
Cdd:cd14132   294 ITAKEAMQHP 303
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
18-270 2.31e-25

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: 106.65  E-value: 2.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLStegkrwisNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd08228    10 IGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKARQ--------DCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGE 177
Cdd:cd08228    82 ELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITA---TGVVKLGDLGLGRFFSS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLF---EGIIKGKYKMNPRQwsHISES 254
Cdd:cd08228   159 KTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFslcQKIEQCDYPPLPTE--HYSEK 236
                         250
                  ....*....|....*.
gi 1039796143 255 AKDLVRRMLMLDPAER 270
Cdd:cd08228   237 LRELVSMCIYPDPDQR 252
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
12-284 2.35e-25

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: 107.45  E-value: 2.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftSSPGLStegkrwISNLkREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd07845     9 FEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDN--ERDGIP------ISSL-REITLLLNLRHPNIVELKEVVVGKH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 M--LYMVFEFMDgADLCfEIVKRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGF 169
Cdd:cd07845    80 LdsIFLVMEYCE-QDLA-SLLDNMPTPF--SESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDK---GCLKIADF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGLVAGGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGTKE----------------RL 232
Cdd:cd07845   153 GLARTYGLPAKPMTPKVVTLWYRAPELLlGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEieqldliiqllgtpneSI 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 233 FEGIIK----GKYKMnPRQ--------WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd07845   233 WPGFSDlplvGKFTL-PKQpynnlkhkFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYFKE 295
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
13-270 2.38e-25

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: 106.09  E-value: 2.38e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   13 ELCEVIGKGPFSVVRRCINRETGQqfaVKIVDVAKFTSSPGLSTEGKRwisNLKREASICHMLKHPHIVELLETYSSDGM 92
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTLKGKGD---GKEVEVAVKTLKEDASEQQIE---EFLREARIMRKLDHPNIVKLLGVCTEEEP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   93 LYMVFEFMDGADLCFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVA 172
Cdd:smart00221  76 LMIVMEYMPGGDLLDYLRKNRPKELSLSDLL--SFALQIARGMEYLESKNFIHRDLAARNCLVGENLV---VKISDFGLS 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  173 IQLGESGL--VAGGRVgtP-HFMAPEVVKREPYGKPVDVWGCGVILFILLSGC-LPFYG-TKERLFEGIIKGKYKMNPrq 247
Cdd:smart00221 151 RDLYDDDYykVKGGKL--PiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGeEPYPGmSNAEVLEYLKKGYRLPKP-- 226
                          250       260
                   ....*....|....*....|....*.
gi 1039796143  248 wshiSESAKDLVRRMLM---LDPAER 270
Cdd:smart00221 227 ----PNCPPELYKLMLQcwaEDPEDR 248
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
17-283 2.76e-25

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: 106.32  E-value: 2.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFS---VVRRCINRETGQQFAVK------IVDVAKFTSSpglsTEGKRWISNLKREAsichmlkhPHIVELLETY 87
Cdd:cd05583     1 VLGTGAYGkvfLVRKVGGHDAGKLYAMKvlkkatIVQKAKTAEH----TMTERQVLEAVRQS--------PFLVTLHYAF 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLG 167
Cdd:cd05583    69 QTDAKLHLILDYVNGGELFTHLYQREH----FTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGH---VVLT 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVA-IQLGESGLVAGGRVGTPHFMAPEVVKREPYG--KPVDVWGCGVILFILLSGCLPFYGTKERLFEG-IIKGKYKM 243
Cdd:cd05583   142 DFGLSkEFLPGENDRAYSFCGTIEYMAPEVVRGGSDGhdKAVDWWSLGVLTYELLTGASPFTVDGERNSQSeISKRILKS 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039796143 244 NPRQWSHISESAKDLVRRMLMLDPAERI-----TVYEALNHPWLK 283
Cdd:cd05583   222 HPPIPKTFSAEAKDFILKLLEKDPKKRLgagprGAHEIKEHPFFK 266
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
9-283 2.94e-25

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 110.49  E-value: 2.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGP----FSVVRrcinretGQQFAVKIVdvAKFTSspgLSTEgkRWISNLKREASICHMLKHPHIVELL 84
Cdd:PTZ00267   66 EHMYVLTTLVGRNPttaaFVATR-------GSDPKEKVV--AKFVM---LNDE--RQAAYARSELHCLAACDHFGIVKHF 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  85 ETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPV 164
Cdd:PTZ00267  132 DDFKSDDKLLLIMEYGSGGDLNKQIKQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMP---TGII 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 165 KLGGFGVAIQLGESGL--VAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKY 241
Cdd:PTZ00267  209 KLGDFGFSKQYSDSVSldVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQReIMQQVLYGKY 288
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1039796143 242 KMNPrqwSHISESAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:PTZ00267  289 DPFP---CPVSSGMKALLDPLLSKNPALRPTTQQLLHTEFLK 327
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
12-282 4.40e-25

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: 106.86  E-value: 4.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvaKFTsspglstegKRWISNLKREASICHMLKH------PHIVELLE 85
Cdd:cd14210    15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKII---RNK---------KRFHQQALVEVKILKHLNDndpddkHNIVRYKD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  86 TYSSDGMLYMVFEfMDGADLcFEIVKRAD-AGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSAPV 164
Cdd:cd14210    83 SFIFRGHLCIVFE-LLSINL-YELLKSNNfQGL--SLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILL-KQPSKSSI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 165 KLGGFGvaiqlgeSGLVAGGRVGT----PHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIK- 238
Cdd:cd14210   158 KVIDFG-------SSCFEGEKVYTyiqsRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEeQLACIMEv 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 239 --------------------GKYKMNPRQWSHI-----------------SESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd14210   231 lgvppkslidkasrrkkffdSNGKPRPTTNSKGkkrrpgskslaqvlkcdDPSFLDFLKKCLRWDPSERMTPEEALQHPW 310

                  .
gi 1039796143 282 L 282
Cdd:cd14210   311 I 311
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
12-283 4.81e-25

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: 105.86  E-value: 4.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRE-TGQQFAVKIVDVAKFTSSPGLstegkrwisnLKREASICHMLKHPHIVELLETYSSD 90
Cdd:cd14201     8 YSRKDLVGHGAFAVVFKGRHRKkTDWEVAIKSINKKNLSKSQIL----------LGKEIKILKELQHENIVALYDVQEMP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLcfeiVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLL--ASKENSA----PV 164
Cdd:cd14201    78 NSVFLVMEYCNGGDL----ADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLsyASRKKSSvsgiRI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 165 KLGGFGVAIQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMN 244
Cdd:cd14201   154 KIADFGFARYL-QSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNKNLQ 232
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1039796143 245 PRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd14201   233 PSIPRETSPYLADLLLGLLQRNQKDRMDFEAFFSHPFLE 271
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
12-286 5.30e-25

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: 106.93  E-value: 5.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFS---VVRRCINRETGQQFAVKIVD----VAKFTSSPGLSTEgkRWISNLKREAsichmlkhPHIVELL 84
Cdd:cd05614     2 FELLKVLGTGAYGkvfLVRKVSGHDANKLYAMKVLRkaalVQKAKTVEHTRTE--RNVLEHVRQS--------PFLVTLH 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  85 ETYSSDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapV 164
Cdd:cd05614    72 YAFQTDAKLHLILDYVSGGELFTHLYQRDH----FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGH---V 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 165 KLGGFGVAIQ-LGESGLVAGGRVGTPHFMAPEVVK-REPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGK-Y 241
Cdd:cd05614   145 VLTDFGLSKEfLTEEKERTYSFCGTIEYMAPEIIRgKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRRiL 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039796143 242 KMNPRQWSHISESAKDLVRRMLMLDPAERI-----TVYEALNHPWLKERD 286
Cdd:cd05614   225 KCDPPFPSFIGPVARDLLQKLLCKDPKKRLgagpqGAQEIKEHPFFKGLD 274
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
12-283 5.88e-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: 105.96  E-value: 5.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglsTEGKRWISNlkrEASICHMLKHPHIVELLETYSSDG 91
Cdd:cd06654    22 YTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQ--------QPKKELIIN---EILVMRENKNPNIVNYLDSYLVGD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCfEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGV 171
Cdd:cd06654    91 ELWVVMEYLAGGSLT-DVVTET----CMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGM---DGSVKLTDFGF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEGIIKGKYKM-NPRQW 248
Cdd:cd06654   163 CAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENplRALYLIATNGTPELqNPEKL 242
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1039796143 249 SHIsesAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd06654   243 SAI---FRDFLNRCLEMDVEKRGSAKELLQHQFLK 274
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
12-279 7.88e-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: 7.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsspglsTEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14046     8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKL----------RSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIvkraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd14046    78 NLYIQMEYCEKSTLRDLI----DSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGN---VKIGDFGL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQL-----------GESGLVAG-------GRVGTPHFMAPEVVKREP--YGKPVDVWGCGVILFILlsgCLPFYGTKER 231
Cdd:cd14046   151 ATSNklnvelatqdiNKSTSAALgssgdltGNVGTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEM---CYPFSTGMER 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039796143 232 LFE-GIIKGKYKMNPRQW--SHISESAKdLVRRMLMLDPAERITVYEALNH 279
Cdd:cd14046   228 VQIlTALRSVSIEFPPDFddNKHSKQAK-LIRWLLNHDPAKRPSAQELLKS 277
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
9-283 8.53e-25

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: 107.39  E-value: 8.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDvYELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvAKFTSSPgLSTEGKRWisnlkREASICHMLKHPHIVELLETYS 88
Cdd:cd05621    52 ED-YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLL--SKFEMIK-RSDSAFFW-----EERDIMAFANSPWVVQLFCAFQ 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCfEIVKRADAgfvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGG 168
Cdd:cd05621   123 DDKYLYMVMEYMPGGDLV-NLMSNYDV----PEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLL---DKYGHLKLAD 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLV-AGGRVGTPHFMAPEVVKREP----YGKPVDVWGCGVILFILLSGCLPFY-----GTkerlFEGIIK 238
Cdd:cd05621   195 FGTCMKMDETGMVhCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYadslvGT----YSKIMD 270
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039796143 239 GKYKMNPRQWSHISESAKDLVRRMLMlDPAERI---TVYEALNHPWLK 283
Cdd:cd05621   271 HKNSLNFPDDVEISKHAKNLICAFLT-DREVRLgrnGVEEIKQHPFFR 317
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
10-282 1.25e-24

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: 104.71  E-value: 1.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftssPGLSTEgkrwiSNLKREASICHMLK-HPHIVELLETY- 87
Cdd:cd06638    18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILD-------PIHDID-----EEIEAEYNILKALSdHPNVVKFYGMYy 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 ----SSDGMLYMVFEFMDGA---DLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKen 160
Cdd:cd06638    86 kkdvKNGDQLWLVLELCNGGsvtDLVKGFLKRGER---MEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTE-- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 161 sAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKRE-----PYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLF 233
Cdd:cd06638   161 -GGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEqqldsTYDARCDVWSLGITAIELGDGDPPLADLHpmRALF 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039796143 234 egiikgKYKMNP----RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd06638   240 ------KIPRNPpptlHQPELWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
12-271 1.32e-24

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: 105.08  E-value: 1.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFS---VVRRCINRETGQQFAVKIVDVAKFTSSpGLSTEGKRwisnLKREAsICHMLKHPHIVELLETYS 88
Cdd:cd05613     2 FELLKVLGTGAYGkvfLVRKVSGHDAGKLYAMKVLKKATIVQK-AKTAEHTR----TERQV-LEHIRQSPFLVTLHYAFQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGG 168
Cdd:cd05613    76 TDTKLHLILDYINGGELFTHLSQRER----FTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDS---SGHVVLTD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQ-LGESGLVAGGRVGTPHFMAPEVVKREPYG--KPVDVWGCGVILFILLSGCLPFY--GTKERLFEgIIKGKYKM 243
Cdd:cd05613   149 FGLSKEfLLDENERAYSFCGTIEYMAPEIVRGGDSGhdKAVDWWSLGVLMYELLTGASPFTvdGEKNSQAE-ISRRILKS 227
                         250       260
                  ....*....|....*....|....*...
gi 1039796143 244 NPRQWSHISESAKDLVRRMLMLDPAERI 271
Cdd:cd05613   228 EPPYPQEMSALAKDIIQRLLMKDPKKRL 255
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
12-281 1.85e-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: 104.28  E-value: 1.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVK-----IVDVAKFTSSpglstegkRWISNLKREASichmlkHPHIVELLET 86
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKcmkkhFKSLEQVNNL--------REIQALRRLSP------HPNILRLIEV 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 Y--SSDGMLYMVFEFMDGAdlCFEIVKradaGFVY--SEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnsa 162
Cdd:cd07831    67 LfdRKTGRLALVFELMDMN--LYELIK----GRKRplPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDI--- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 163 pVKLGGFG----VAIQLGESGLVAggrvgTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPFYGTKE------- 230
Cdd:cd07831   138 -LKLADFGscrgIYSKPPYTEYIS-----TRWYRAPECLLTDGyYGPKMDIWAVGCVFFEILSLFPLFPGTNEldqiaki 211
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 231 ------------RLFEGIIKGKYKMNPRQWS-------HISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd07831   212 hdvlgtpdaevlKKFRKSRHMNYNFPSKKGTglrkllpNASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
9-304 1.96e-24

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: 104.00  E-value: 1.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkftsspglstEGKRWISNLKREASICHMLKHPHIVELLETYS 88
Cdd:cd06641     3 EELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLE----------EAEDEIEDIQQEITVLSQCDSPYVTKYYGSYL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGAdlcfEIVKRADAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGG 168
Cdd:cd06641    73 KDTKLWIIMEYLGGG----SALDLLEPGPLDETQIAT-ILREILKGLDYLHSEKKIHRDIKAANVLLSEH---GEVKLAD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKgkyKMNPRQW 248
Cdd:cd06641   145 FGVAGQLTDTQIKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIP---KNNPPTL 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796143 249 S-HISESAKDLVRRMLMLDPAERITVYEALNHPWLKerdRYAYKI-HLPETVEQLRKF 304
Cdd:cd06641   222 EgNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFIL---RNAKKTsYLTELIDRYKRW 276
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
16-279 2.77e-24

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: 103.17  E-value: 2.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspgLSTEGKRwiSNLKREASICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd14188     7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSR------VSKPHQR--EKIDKEIELHRILHHKHVVQFYHYFEDKENIYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQL 175
Cdd:cd14188    79 LLEYCSRRSMAHILKARK----VLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFI---NENMELKVGDFGLAARL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMNprqwSHISES 254
Cdd:cd14188   152 EPLEHRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNlKETYRCIREARYSLP----SSLLAP 227
                         250       260
                  ....*....|....*....|....*
gi 1039796143 255 AKDLVRRMLMLDPAERITVYEALNH 279
Cdd:cd14188   228 AKHLIASMLSKNPEDRPSLDEIIRH 252
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
12-271 2.97e-24

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: 104.69  E-value: 2.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIV---DVAKFTSSPGLSTEgkrwisnlKREASICHMLKHPHIVELLETYS 88
Cdd:cd05589     1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALkkgDIIARDEVESLMCE--------KRIFETVNSARHPFLVNLFACFQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIvkRADagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGG 168
Cdd:cd05589    73 TPEHVCFVMEYAAGGDLMMHI--HED---VFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDT---EGYVKIAD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGvaiqLGESGLVAGGRV----GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKM 243
Cdd:cd05589   145 FG----LCKEGMGFGDRTstfcGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGdDEEEVFDSIVNDEVRY 220
                         250       260
                  ....*....|....*....|....*...
gi 1039796143 244 nPRqwsHISESAKDLVRRMLMLDPAERI 271
Cdd:cd05589   221 -PR---FLSTEAISIMRRLLRKNPERRL 244
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
8-285 3.38e-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: 104.76  E-value: 3.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTEGKRWIsnlkREASICHMLKHPHIVELLETY 87
Cdd:cd07855     3 VGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIK-----KIPNAFDVVTTAKRTL----RELKILRHFKHDNIIAIRDIL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGML------YMVFEFMDGaDLCFEIvkRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenS 161
Cdd:cd07855    74 RPKVPYadfkdvYVVLDLMES-DLHHII--HSDQPL--TLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNE---N 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 162 APVKLGGFGVAIQLGESGL----VAGGRVGTPHFMAPEVVKREP-YGKPVDVWGCGVIL--------------------- 215
Cdd:cd07855   146 CELKIGDFGMARGLCTSPEehkyFMTEYVATRWYRAPELMLSLPeYTQAIDMWSVGCIFaemlgrrqlfpgknyvhqlql 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 216 -----------FILLSGClpfygtkERLfEGIIKGKYKMNPRQWSHI----SESAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd07855   226 iltvlgtpsqaVINAIGA-------DRV-RRYIQNLPNKQPVPWETLypkaDQQALDLLSQMLRFDPSERITVAEALQHP 297

                  ....*
gi 1039796143 281 WLKER 285
Cdd:cd07855   298 FLAKY 302
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
13-270 3.43e-24

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 102.61  E-value: 3.43e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   13 ELCEVIGKGPFSVVRRCINRETGQQfavKIVDVAKFTSSPGLSTEGKRwisNLKREASICHMLKHPHIVELLETYSSDGM 92
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKLKGKGGK---KKVEVAVKTLKEDASEQQIE---EFLREARIMRKLDHPNVVKLLGVCTEEEP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   93 LYMVFEFMDGADLcFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVA 172
Cdd:smart00219  76 LYIVMEYMEGGDL-LSYLRKNRPKLSLSDLL--SFALQIARGMEYLESKNFIHRDLAARNCLVGENLV---VKISDFGLS 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  173 IQLGESGL--VAGGRVgtP-HFMAPEVVKREPYGKPVDVWGCGVILFILLSGC-LPFYG-TKERLFEGIIKGKYKMNPrq 247
Cdd:smart00219 150 RDLYDDDYyrKRGGKL--PiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGeQPYPGmSNEEVLEYLKNGYRLPQP-- 225
                          250       260
                   ....*....|....*....|....*.
gi 1039796143  248 wshiSESAKDLVRRMLM---LDPAER 270
Cdd:smart00219 226 ----PNCPPELYDLMLQcwaEDPEDR 247
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
18-282 3.52e-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: 3.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTEGKRWIsnlkREASICHMLKHPHIVELLETYSSDGM----- 92
Cdd:cd07858    13 IGRGAYGIVCSAKNSETNEKVAIK-----KIANAFDNRIDAKRTL----REIKLLRHLDHENVIAIKDIMPPPHReafnd 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  93 LYMVFEFMDgADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVA 172
Cdd:cd07858    84 VYIVYELMD-TDL-HQIIRSSQT---LSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNAN---CDLKICDFGLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 173 IQLGESGLVAGGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGT----KERLFEGIIKG-------- 239
Cdd:cd07858   156 RTTSEKGDFMTEYVVTRWYRAPELLlNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKdyvhQLKLITELLGSpseedlgf 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 240 -------KYKMN----PRQ-----WSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd07858   236 irnekarRYIRSlpytPRQsfarlFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYL 294
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
12-283 5.19e-24

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 106.88  E-value: 5.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsspglstEGKRWISNLKREASICHMLKHPH--IVELLETYS- 88
Cdd:PTZ00283   34 YWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDM-----------EGMSEADKNRAQAEVCCLLNCDFfsIVKCHEDFAk 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SD-------GMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenS 161
Cdd:PTZ00283  103 KDprnpenvLMIALVLDYANAGDLRQEIKSRAKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCS---N 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 162 APVKLGGFGVAIQLGE--SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIK 238
Cdd:PTZ00283  180 GLVKLGDFGFSKMYAAtvSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENmEEVMHKTLA 259
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039796143 239 GKYKMNPrqwSHISESAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:PTZ00283  260 GRYDPLP---PSISPEMQEIVTALLSSDPKRRPSSSKLLNMPICK 301
gmk PRK00300
guanylate kinase; Provisional
720-885 5.60e-24

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 100.55  E-value: 5.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 720 LVLLGAHGVGrrhiKNTLIT---KHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGT 796
Cdd:PRK00300    8 IVLSGPSGAG----KSTLVKallERDPNLQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLEWAEVFGNYYGT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 797 KLETIRKIHEQGLIAILDVEPQ-ALKVLRTAEFAPFvVFIAAPTItpglneDESLQRLQK---ES-DVLQR--------- 862
Cdd:PRK00300   84 PRSPVEEALAAGKDVLLEIDWQgARQVKKKMPDAVS-IFILPPSL------EELERRLRGrgtDSeEVIARrlakareei 156
                         170       180
                  ....*....|....*....|...
gi 1039796143 863 TYAHYFDLTIINNEIDETIRHLE 885
Cdd:PRK00300  157 AHASEYDYVIVNDDLDTALEELK 179
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
48-280 6.16e-24

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: 102.05  E-value: 6.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  48 FTSSPGLSTE-GKRWISNLKREASICHMLKHPHIVELLE------TYSSDGMLYMVFEFMDGADLcFEIVKRAdaGFVYS 120
Cdd:cd14012    27 LTSQEYFKTSnGKKQIQLLEKELESLKKLRHPNLVSYLAfsierrGRSDGWKVYLLTEYAPGGSL-SELLDSV--GSVPL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 121 EAVaSHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFG----VAIQLGESGLVAggrVGTPHFMAPEV 196
Cdd:cd14012   104 DTA-RRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTGIVKLTDYSlgktLLDMCSRGSLDE---FKQTYWLPPEL 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 197 VK-REPYGKPVDVWGCGVILFILLSGCLPF-YGTKERLFEGIIKgkykmnprqwshISESAKDLVRRMLMLDPAERITVY 274
Cdd:cd14012   180 AQgSKSPTRKTDVWDLGLLFLQMLFGLDVLeKYTSPNPVLVSLD------------LSASLQDFLSKCLSLDPKKRPTAL 247

                  ....*.
gi 1039796143 275 EALNHP 280
Cdd:cd14012   248 ELLPHE 253
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
10-281 6.43e-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: 102.99  E-value: 6.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKivdvakftsSPGLSTEGKRWISNLKREASICHMLKH-PHIVELL--ET 86
Cdd:cd07837     1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALK---------KTRLEMEEEGVPSTALREVSLLQMLSQsIYIVRLLdvEH 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDG--MLYMVFEFMDgADL--CFEIVKRADAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENS- 161
Cdd:cd07837    72 VEENGkpLLYLVFEYLD-TDLkkFIDSYGRGPHNPLPAKTIQS-FMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLl 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 162 --APVKLG-GFGVAIQLGESGLVaggrvgTPHFMAPEV-VKREPYGKPVDVWGCGVI---------LFI------LLSGC 222
Cdd:cd07837   150 kiADLGLGrAFTIPIKSYTHEIV------TLWYRAPEVlLGSTHYSTPVDMWSVGCIfaemsrkqpLFPgdselqQLLHI 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 223 LPFYGT-KERLFEGIIKGKYKMNPRQWS---------HISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd07837   224 FRLLGTpNEEVWPGVSKLRDWHEYPQWKpqdlsravpDLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
18-225 9.24e-24

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: 102.53  E-value: 9.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKivdVAKFTSSPGLSTEgKRWisnlKREASICHMLKHPHIV------ELLETYSSDG 91
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIK---KCRQELSPSDKNR-ERW----CLEVQIMKKLNHPNVVsardvpPELEKLSPND 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGV 171
Cdd:cd13989    73 LPLLAMEYCSGGDL-RKVLNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIYKLIDLGY 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 172 AIQLGESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF 225
Cdd:cd13989   152 AKELDQGSLCTS-FVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
17-271 9.41e-24

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 103.24  E-value: 9.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKIvdvakftsspglstegkrwisnLKREASI------CHML---------KHPHIV 81
Cdd:cd05587     3 VLGKGSFGKVMLAERKGTDELYAIKI----------------------LKKDVIIqdddveCTMVekrvlalsgKPPFLT 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  82 ELLETYSSDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENS 161
Cdd:cd05587    61 QLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGK----FKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML---DAE 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 162 APVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIkgk 240
Cdd:cd05587   134 GHIKIADFGMCKEGIFGGKTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEdELFQSIM--- 210
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1039796143 241 yKMNPRQWSHISESAKDLVRRMLMLDPAERI 271
Cdd:cd05587   211 -EHNVSYPKSLSKEAVSICKGLLTKHPAKRL 240
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
12-227 9.89e-24

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 106.42  E-value: 9.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRR--CI--NRETgqqfAVKIVD---------VAKFtsspglstegkrwisnlKREA----Sichm 74
Cdd:NF033483    9 YEIGERIGRGGMAEVYLakDTrlDRDV----AVKVLRpdlardpefVARF-----------------RREAqsaaS---- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  75 LKHPHIVELLETYSSDGMLYMVFEFMDGADLcFEIVkRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVL 154
Cdd:NF033483   64 LSHPNIVSVYDVGEDGGIPYIVMEYVDGRTL-KDYI-REHGPLSPEEAV--EIMIQILSALEHAHRNGIVHRDIKPQNIL 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 155 LAskeNSAPVKLGGFGVAIQLGESGLVAGGRV-GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 227
Cdd:NF033483  140 IT---KDGRVKVTDFGIARALSSTTMTQTNSVlGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFDG 210
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
13-272 1.03e-23

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 101.42  E-value: 1.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  13 ELCEVIGKGPFSVVRRCI----NRETGQQFAVKIVdvaKFTSSPGLSTEgkrwisnLKREASICHMLKHPHIVELLETYS 88
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGTlkgeGENTKIKVAVKTL---KEGADEEERED-------FLEEASIMKKLDHPNIVKLLGVCT 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLcFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGG 168
Cdd:pfam07714  72 QGEPLYIVTEYMPGGDL-LDFLRKHKRKLTLKDLL--SMALQIAKGMEYLESKNFVHRDLAARNCLVSENLV---VKISD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESG--LVAGGRVGTPHFMAPEVVKrepYGK---PVDVWGCGVILFILLSGC-LPFYG-TKERLFEGIIKGkY 241
Cdd:pfam07714 146 FGLSRDIYDDDyyRKRGGGKLPIKWMAPESLK---DGKftsKSDVWSFGVLLWEIFTLGeQPYPGmSNEEVLEFLEDG-Y 221
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1039796143 242 KMN-PRQWshiSESAKDLVRRMLMLDPAERIT 272
Cdd:pfam07714 222 RLPqPENC---PDELYDLMKQCWAYDPEDRPT 250
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
16-282 1.69e-23

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: 100.76  E-value: 1.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglsTEGKRwisnLKREASICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd13983     7 EVLGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPK-----AERQR----FKQEIEILKSLKHPNIIKFYDSWESKSKKEV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VF--EFMDGADLcFEIVKRADagfVYSEAVASHYMRQILEALRYCH--DNNIIHRDVKphCVLLASKENSAPVKLGGFGV 171
Cdd:cd13983    78 IFitELMTSGTL-KQYLKRFK---RLKLKVIKSWCRQILEGLNYLHtrDPPIIHRDLK--CDNIFINGNTGEVKIGDLGL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESglVAGGRVGTPHFMAPEVVKrEPYGKPVDVWGCGVILFILLSGCLPFYGTKE--RLFEGIIKGKykmNPRQWS 249
Cdd:cd13983   152 ATLLRQS--FAKSVIGTPEFMAPEMYE-EHYDEKVDIYAFGMCLLEMATGEYPYSECTNaaQIYKKVTSGI---KPESLS 225
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796143 250 HI-SESAKDLVrRMLMLDPAERITVYEALNHPWL 282
Cdd:cd13983   226 KVkDPELKDFI-EKCLKPPDERPSARELLEHPFF 258
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
9-304 1.72e-23

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: 101.28  E-value: 1.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkftsspglstEGKRWISNLKREASICHMLKHPHIVELLETYS 88
Cdd:cd06640     3 EELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLE----------EAEDEIEDIQQEITVLSQCDSPYVTKYYGSYL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADlCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGG 168
Cdd:cd06640    73 KGTKLWIIMEYLGGGS-ALDLLRAGP----FDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQ---GDVKLAD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKykmNPRQ 247
Cdd:cd06640   145 FGVAGQLTDTQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPmRVLFLIPKNN---PPTL 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796143 248 WSHISESAKDLVRRMLMLDPAERITVYEALNHPWL-KERDRYAYkihLPETVEQLRKF 304
Cdd:cd06640   222 VGDFSKPFKEFIDACLNKDPSFRPTAKELLKHKFIvKNAKKTSY---LTELIDRFKRW 276
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
16-283 1.98e-23

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: 101.94  E-value: 1.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIV--DVAKFTSSPGLSTEGKRWISnLKREasichmlkHPHIVELLETYSSDGML 93
Cdd:cd05620     1 KVLGKGSFGKVLLAELKGKGEYFAVKALkkDVVLIDDDVECTMVEKRVLA-LAWE--------NPFLTHLYCTFQTKEHL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  94 YMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAI 173
Cdd:cd05620    72 FFVMEFLNGGDLMFHIQDKGR----FDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVML---DRDGHIKIADFGMCK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 174 Q--LGESGlvAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGiIKGKYKMNPRqWsh 250
Cdd:cd05620   145 EnvFGDNR--ASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEdELFES-IRVDTPHYPR-W-- 218
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039796143 251 ISESAKDLVRRMLMLDPAERITVYEALN-HPWLK 283
Cdd:cd05620   219 ITKESKDILEKLFERDPTRRLGVVGNIRgHPFFK 252
SH3_MPP7 cd12033
Src Homology 3 domain of Membrane Protein, Palmitoylated 7 (or MAGUK p55 subfamily member 7); ...
599-657 2.44e-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: 2.44e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 599 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPS 657
Cdd:cd12033     1 FIKALFDYNPNEDKAIPCKEAGLSFKKGDILQIMSQDDATWWQAKHEGDANPRAGLIPS 59
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
12-271 2.60e-23

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: 102.00  E-value: 2.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIvdvakftsspglstegkrwisnLKREASI------CHML---------K 76
Cdd:cd05616     2 FNFLMVLGKGSFGKVMLAERKGTDELYAVKI----------------------LKKDVVIqdddveCTMVekrvlalsgK 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  77 HPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLA 156
Cdd:cd05616    60 PPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGR----FKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLD 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 157 SKENsapVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEG 235
Cdd:cd05616   136 SEGH---IKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEdELFQS 212
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039796143 236 IIKGKYKMnPRQwshISESAKDLVRRMLMLDPAERI 271
Cdd:cd05616   213 IMEHNVAY-PKS---MSKEAVAICKGLMTKHPGKRL 244
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
77-280 3.23e-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: 100.42  E-value: 3.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  77 HPHIVELLETYSSDGMLYMVFEfmdgadLC----FEIVKRADAG--FVYSEAVASHYMRQILEALRYCHDNNIIHRDVKP 150
Cdd:cd13982    54 HPNVIRYFCTEKDRQFLYIALE------LCaaslQDLVESPRESklFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKP 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 151 HCVLLA--SKENSAPVKLGGFGVAIQL--GESGLVA-GGRVGTPHFMAPEVVKREPYGKP---VDVWGCGVILFILLSGC 222
Cdd:cd13982   128 QNILIStpNAHGNVRAMISDFGLCKKLdvGRSSFSRrSGVAGTSGWIAPEMLSGSTKRRQtraVDIFSLGCVFYYVLSGG 207
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 223 L-PFYGTKERlfEG-IIKGKYKMNP--RQWSHISEsAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd13982   208 ShPFGDKLER--EAnILKGKYSLDKllSLGEHGPE-AQDLIERMIDFDPEKRPSAEEVLNHP 266
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
6-286 3.49e-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: 101.54  E-value: 3.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   6 VLFEDvYELCEVIGKGPFSVVRRCINRETGQQFAVKIV--DVAKFTSSPGLSTEGKRWISnLKREasichmlkHPHIVEL 83
Cdd:cd05619     2 LTIED-FVLHKMLGKGSFGKVFLAELKGTNQFFAIKALkkDVVLMDDDVECTMVEKRVLS-LAWE--------HPFLTHL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  84 LETYSSDGMLYMVFEFMDGADLCFEIvkraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAP 163
Cdd:cd05619    72 FCTFQTKENLFFVMEYLNGGDLMFHI----QSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILL---DKDGH 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 164 VKLGGFGVAIQ--LGESGlvAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT-KERLFEGiIKGK 240
Cdd:cd05619   145 IKIADFGMCKEnmLGDAK--TSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQdEEELFQS-IRMD 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1039796143 241 YKMNPRqWshISESAKDLVRRMLMLDPAERITVYEAL-NHPWLKERD 286
Cdd:cd05619   222 NPFYPR-W--LEKEAKDILVKLFVREPERRLGVRGDIrQHPFFREIN 265
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
12-282 4.47e-23

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: 100.42  E-value: 4.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkfTSSPGLSTEGKRWISNLKReasiCHMLKHPHIVELLETYSS-- 89
Cdd:cd07863     2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQ--TNEDGLPLSTVREVALLKR----LEAFDHPNIVRLMDVCATsr 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 ---DGMLYMVFEFMDgADLCFEIVKRADAGFVySEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKL 166
Cdd:cd07863    76 tdrETKVTLVFEHVD-QDLRTYLDKVPPPGLP-AETIKD-LMRQFLRGLDFLHANCIVHRDLKPENILVTSG---GQVKL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAiQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFEGI----- 236
Cdd:cd07863   150 ADFGLA-RIYSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEadqlgKIFDLIglppe 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 237 -------IKGKYKMNPRQWS-------HISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd07863   229 ddwprdvTLPRGAFSPRGPRpvqsvvpEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
24-282 1.08e-22

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: 97.88  E-value: 1.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  24 SVVRRCINRETGQQFAVKIVDVAKFTSspglstegkrwisnlKREASIChMLKHPHIVELLETYSSDGMLYMVFEfMDGA 103
Cdd:cd13976     7 SSLYRCVDIHTGEELVCKVVPVPECHA---------------VLRAYFR-LPSHPNISGVHEVIAGETKAYVFFE-RDHG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 104 DLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKpHCVLLASKENSAPVKLGGF-GVAIQLGESGLVA 182
Cdd:cd13976    70 DLHSYVRSRKR----LREPEAARLFRQIASAVAHCHRNGIVLRDLK-LRKFVFADEERTKLRLESLeDAVILEGEDDSLS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 183 GgRVGTPHFMAPEVVK-REPY-GKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMnPrqwSHISESAKDLV 259
Cdd:cd13976   145 D-KHGCPAYVSPEILNsGATYsGKAADVWSLGVILYTMLVGRYPFHDSEPaSLFAKIRRGQFAI-P---ETLSPRARCLI 219
                         250       260
                  ....*....|....*....|...
gi 1039796143 260 RRMLMLDPAERITVYEALNHPWL 282
Cdd:cd13976   220 RSLLRREPSERLTAEDILLHPWL 242
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
7-263 1.10e-22

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: 101.63  E-value: 1.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   7 LFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglstegkRWiSNLKREASICHMLKHPHIVE---- 82
Cdd:cd05623    69 LHKEDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILN---------------KW-EMLKRAETACFREERDVLVNgdsq 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  83 ----LLETYSSDGMLYMVFEFMDGADLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLask 158
Cdd:cd05623   133 wittLHYAFQDDNNLYLVMDYYVGGDLLTLLSKFEDR---LPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILM--- 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 159 ENSAPVKLGGFGVAIQLGESGLVAGG-RVGTPHFMAPEVVK-----REPYGKPVDVWGCGVILFILLSGCLPFYGtkERL 232
Cdd:cd05623   207 DMNGHIRLADFGSCLKLMEDGTVQSSvAVGTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGETPFYA--ESL 284
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1039796143 233 FE---GIIKGKYKMN-PRQWSHISESAKDLVRRML 263
Cdd:cd05623   285 VEtygKIMNHKERFQfPTQVTDVSENAKDLIRRLI 319
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
18-215 1.36e-22

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: 97.95  E-value: 1.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVdvaKFTSSPGlstegkrwisNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKEL---KRFDEQR----------SFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFIT 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLcFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGE 177
Cdd:cd14065    68 EYVNGGTL-EELLKSMDEQLPWSQRV--SLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVVADFGLAREMPD 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039796143 178 SGLVAGGR------VGTPHFMAPEVVKREPYGKPVDVWGCGVIL 215
Cdd:cd14065   145 EKTKKPDRkkrltvVGSPYWMAPEMLRGESYDEKVDVFSFGIVL 188
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
12-281 1.72e-22

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: 99.28  E-value: 1.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVV--RRCINRETGQQFAVKivdvaKFTSSP----GLSTegkrwiSNLkREASICHMLKHPHIVELLE 85
Cdd:cd07842     2 YEIEGCIGRGTYGRVykAKRKNGKDGKEYAIK-----KFKGDKeqytGISQ------SAC-REIALLRELKHENVVSLVE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  86 TY--SSDGMLYMVFEFMDgADLcFEIVK---RADAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASK-E 159
Cdd:cd07842    70 VFleHADKSVYLLFDYAE-HDL-WQIIKfhrQAKRVSIPPSMVKS-LLWQILNGIHYLHSNWVLHRDLKPANILVMGEgP 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 160 NSAPVKLGGFGVAiQLGESGLVA----GGRVGTPHFMAPEVV--KREpYGKPVDVWGCGVILFILLSGCLPFYGTK---- 229
Cdd:cd07842   147 ERGVVKIGDLGLA-RLFNAPLKPladlDPVVVTIWYRAPELLlgARH-YTKAIDIWAIGCIFAELLTLEPIFKGREakik 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 230 ----------ERLFE-----------GIIK-------------GKY-KMNPRQWSHI----SESAKDLVRRMLMLDPAER 270
Cdd:cd07842   225 ksnpfqrdqlERIFEvlgtptekdwpDIKKmpeydtlksdtkaSTYpNSLLAKWMHKhkkpDSQGFDLLRKLLEYDPTKR 304
                         330
                  ....*....|.
gi 1039796143 271 ITVYEALNHPW 281
Cdd:cd07842   305 ITAEEALEHPY 315
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
7-263 1.87e-22

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: 100.85  E-value: 1.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   7 LFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDvakftsspglstegkRWiSNLKREASICHMLKHPHIVE---- 82
Cdd:cd05624    69 LHRDDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILN---------------KW-EMLKRAETACFREERNVLVNgdcq 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  83 ----LLETYSSDGMLYMVFEFMDGADLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLask 158
Cdd:cd05624   133 wittLHYAFQDENYLYLVMDYYVGGDLLTLLSKFEDK---LPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLL--- 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 159 ENSAPVKLGGFGVAIQLGESGLVAGG-RVGTPHFMAPEVVKRE-----PYGKPVDVWGCGVILFILLSGCLPFYGtkERL 232
Cdd:cd05624   207 DMNGHIRLADFGSCLKMNDDGTVQSSvAVGTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFYA--ESL 284
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039796143 233 FEgiIKGKYkMN-------PRQWSHISESAKDLVRRML 263
Cdd:cd05624   285 VE--TYGKI-MNheerfqfPSHVTDVSEEAKDLIQRLI 319
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
33-302 1.96e-22

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: 104.16  E-value: 1.96e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   33 ETGQQFAVKIVDVakftsspgLSTEGKRWISNLKREASICHMLKHPHIVELLET-YSSDGMLYMVFEFMDGADLcfeiVK 111
Cdd:TIGR03903    1 MTGHEVAIKLLRT--------DAPEEEHQRARFRRETALCARLYHPNIVALLDSgEAPPGLLFAVFEYVPGRTL----RE 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  112 RADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGR------ 185
Cdd:TIGR03903   69 VLAADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRPHAKVLDFGIGTLLPGVRDADVATltrtte 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  186 -VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG--TKERLFEGIIKGKYKMNPRQWSHiseSAKDLVRRM 262
Cdd:TIGR03903  149 vLGTPTYCAPEQLRGEPVTPNSDLYAWGLIFLECLTGQRVVQGasVAEILYQQLSPVDVSLPPWIAGH---PLGQVLRKA 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1039796143  263 LMLDPAERitvyeALNHPWLKERDRyayKIHLPETVEQLR 302
Cdd:TIGR03903  226 LNKDPRQR-----AASAPALAERFR---ALELCALVGILR 257
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
18-283 2.02e-22

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 99.45  E-value: 2.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVdvaKFTSSPGLSTEGKRWISN------LKREASICHMLKHPHIVELLETYSSDG 91
Cdd:PTZ00024   17 LGEGTYGKVEKAYDTLTGKIVAIKKV---KIIEISNDVTKDRQLVGMcgihftTLRELKIMNEIKHENIMGLVDVYVEGD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGaDLcfeiVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGV 171
Cdd:PTZ00024   94 FINLVMDIMAS-DL----KKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSK---GICKIADFGL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAG--------------GRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-----R 231
Cdd:PTZ00024  166 ARRYGYPPYSDTlskdetmqrreemtSKVVTLWYRAPELLmGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEidqlgR 245
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 232 LFEgiIKGK------------------YKMNPRQWS----HISESAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:PTZ00024  246 IFE--LLGTpnednwpqakklplytefTPRKPKDLKtifpNASDDAIDLLQSLLKLNPLERISAKEALKHEYFK 317
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
7-282 2.20e-22

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: 99.18  E-value: 2.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   7 LFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIV-DVAKFTSSPglstegkrwisnlKREASICHMLKH------PH 79
Cdd:cd14134     9 LLTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIrNVEKYREAA-------------KIEIDVLETLAEkdpngkSH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  80 IVELLETYSSDGMLYMVFEFMdGADLcFEIVKRADAGFVYSEAVAsHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE 159
Cdd:cd14134    76 CVQLRDWFDYRGHMCIVFELL-GPSL-YDFLKKNNYGPFPLEHVQ-HIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 160 ----------------NSAPVKLGGFGVAIQLGE--SGLVAggrvgTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSG 221
Cdd:cd14134   153 yvkvynpkkkrqirvpKSTDIKLIDFGSATFDDEyhSSIVS-----TRHYRAPEVILGLGWSYPCDVWSIGCILVELYTG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 222 CLPF----------------------------YGTKERLF--------EGIIKGKY-KMNPRQWSHISESAK-------D 257
Cdd:cd14134   228 ELLFqthdnlehlammerilgplpkrmirrakKGAKYFYFyhgrldwpEGSSSGRSiKRVCKPLKRLMLLVDpehrllfD 307
                         330       340
                  ....*....|....*....|....*
gi 1039796143 258 LVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14134   308 LIRKMLEYDPSKRITAKEALKHPFF 332
SH3_MPP2 cd12037
Src Homology 3 domain of Membrane Protein, Palmitoylated 2 (or MAGUK p55 subfamily member 2); ...
599-657 2.85e-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: 2.85e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 599 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLenSKNGTAGLIPS 657
Cdd:cd12037     1 FVKCHFDYDPSSDSLIPCKEAGLKFRAGDLLQIVNQEDPNWWQACH--VEGGSAGLIPS 57
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
17-279 3.59e-22

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: 96.92  E-value: 3.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAKfTSSPglstEGKRWISNlkrEASICHMLKHPHIVELLETYSSDGMLYMV 96
Cdd:cd14189     8 LLGKGGFARCYEMTDLATNKTYAVKVIPHSR-VAKP----HQREKIVN---EIELHRDLHHKHVVKFSHHFEDAENIYIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMDGADLCfEIVKradAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLG 176
Cdd:cd14189    80 LELCSRKSLA-HIWK---ARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFI---NENMELKVGDFGLAARLE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 177 ESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMNprqwSHISESA 255
Cdd:cd14189   153 PPEQRKKTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDlKETYRCIKQVKYTLP----ASLSLPA 228
                         250       260
                  ....*....|....*....|....
gi 1039796143 256 KDLVRRMLMLDPAERITVYEALNH 279
Cdd:cd14189   229 RHLLAGILKRNPGDRLTLDQILEH 252
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
12-283 4.78e-22

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: 96.46  E-value: 4.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVD---VAKFTSSPGLSTEGKRwISNLKreaSICHMLKHPHIVELLETYS 88
Cdd:cd14101     2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISrnrVQQWSKLPGVNPVPNE-VALLQ---SVGGGPGHRGVIRLLDWFE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApvKLGG 168
Cdd:cd14101    78 IPEGFLLVLERPQHCQDLFDYITERGA---LDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRTGDI--KLID 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLV--AGGRVGTPhfmaPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFygtkERlFEGIIKGKYKMNp 245
Cdd:cd14101   153 FGSGATLKDSMYTdfDGTRVYSP----PEWILYHQYhALPATVWSLGILLYDMVCGDIPF----ER-DTDILKAKPSFN- 222
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039796143 246 rqwSHISESAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd14101   223 ---KRVSNDCRSLIRSCLAYNPSDRPSLEQILLHPWMM 257
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
17-286 5.11e-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: 98.03  E-value: 5.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstegKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYMV 96
Cdd:cd05585     1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVS--------RSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApvkLGGFGVA-IQL 175
Cdd:cd05585    73 LAFINGGELFHHLQREGR----FDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIA---LCDFGLCkLNM 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GESGlVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMNprqwSHISES 254
Cdd:cd05585   146 KDDD-KTNTFCGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENtNEMYRKILQEPLRFP----DGFDRD 220
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1039796143 255 AKDLVRRMLMLDPAERITV---YEALNHPWLKERD 286
Cdd:cd05585   221 AKDLLIGLLNRDPTKRLGYngaQEIKNHPFFDQID 255
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
12-284 5.13e-22

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


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 98.15  E-value: 5.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftsSP-GLSTEGKRWIsnlkREASICHMLKHPHIVELLE----- 85
Cdd:cd07849     7 YQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKI-------SPfEHQTYCLRTL----REIKILLRFKHENIIGILDiqrpp 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  86 TYSSDGMLYMVFEFMDgADLCfEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVK 165
Cdd:cd07849    76 TFESFKDVYIVQELME-TDLY-KLIKTQH----LSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNT---NCDLK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 166 LGGFG---VAIQLGESGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSgCLPFYGTKERL--------- 232
Cdd:cd07849   147 ICDFGlarIADPEHDHTGFLTEYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLS-NRPLFPGKDYLhqlnlilgi 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 233 --------FEGIIKGKYK-------MNPRQ-----WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd07849   226 lgtpsqedLNCIISLKARnyikslpFKPKVpwnklFPNADPKALDLLDKMLTFNPHKRITVEEALAHPYLEQ 297
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
16-272 5.17e-22

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: 96.45  E-value: 5.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCI---NRETGQQFAVKIVdvakftssPGLSTEGKRwiSNLKREASICHMLKHPHIVELLETYSSDGM 92
Cdd:cd00192     1 KKLGEGAFGEVYKGKlkgGDGKTVDVAVKTL--------KEDASESER--KDFLKEARVMKKLGHPNVVRLLGVCTEEEP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  93 LYMVFEFMDGADL-CFEIVKRADAGFVYSEAVAS----HYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLG 167
Cdd:cd00192    71 LYLVMEYMEGGDLlDFLRKSRPVFPSPEPSTLSLkdllSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLV---VKIS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVA--IQLGESGLVAGGRVgTP-HFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYG-TKERLFEGIIKGkYK 242
Cdd:cd00192   148 DFGLSrdIYDDDYYRKKTGGK-LPiRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGlSNEEVLEYLRKG-YR 225
                         250       260       270
                  ....*....|....*....|....*....|
gi 1039796143 243 MNprQWSHISESAKDLVRRMLMLDPAERIT 272
Cdd:cd00192   226 LP--KPENCPDELYELMLSCWQLDPEDRPT 253
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
18-286 5.90e-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: 98.03  E-value: 5.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLS-TEGKRWIsnLKREAsichMLKHPHIVELLETYSSDGMLYMV 96
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAhTIGERNI--LVRTA----LDESPFIVGLKFSFQTPTDLYLV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApvkLGGFGVAIQLG 176
Cdd:cd05586    75 TDYMSGGELFWHLQKEGR----FSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIA---LCDFGLSKADL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 177 ESGLVAGGRVGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnPRqwSHISES 254
Cdd:cd05586   148 TDNKTTNTFCGTTEYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPFYAEDtQQMYRNIAFGKVRF-PK--DVLSDE 224
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039796143 255 AKDLVRRMLMLDPAERITVY----EALNHPWLKERD 286
Cdd:cd05586   225 GRSFVKGLLNRNPKHRLGAHddavELKEHPFFADID 260
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
10-296 7.52e-22

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: 97.77  E-value: 7.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIV---DVAKftsspglstegKRWISNLKREASICHMLKHPHIVELLET 86
Cdd:cd05598     1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLrkkDVLK-----------RNQVAHVKAERDILAEADNEWVVKLYYS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKL 166
Cdd:cd05598    70 FQDKENLYFVMDYIPGGDLMSLLIKKG----IFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILI---DRDGHIKL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAiqlgeSGL---------VAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-----TKERl 232
Cdd:cd05598   143 TDFGLC-----TGFrwthdskyyLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAqtpaeTQLK- 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796143 233 fegIIKGKYKMNPRQWSHISESAKDLVRRmLMLDPAERI---TVYEALNHPWLK----ERDRYAYKIHLPE 296
Cdd:cd05598   217 ---VINWRTTLKIPHEANLSPEAKDLILR-LCCDAEDRLgrnGADEIKAHPFFAgidwEKLRKQKAPYIPT 283
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
12-271 1.17e-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: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEGKRWISNLK---REASichmlKHPHIVELLETYS 88
Cdd:cd05618    22 FDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDD-----EDIDWVQTEKhvfEQAS-----NHPFLVGLHSCFQ 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGG 168
Cdd:cd05618    92 TESRLFFVIEYVNGGDLMFHMQRQRK----LPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGH---IKLTD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF----------YGTKERLFEGIIK 238
Cdd:cd05618   165 YGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgssdnpdQNTEDYLFQVILE 244
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1039796143 239 GKYKMnPRQwshISESAKDLVRRMLMLDPAERI 271
Cdd:cd05618   245 KQIRI-PRS---LSVKAASVLKSFLNKDPKERL 273
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
26-282 1.72e-21

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: 94.72  E-value: 1.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  26 VRRCINRETGQQFAVKIVDVAKFTSSpglstegkrwisnlkreASICHML-KHPHIVELLETYSSDGMLYMVFEFMDGAD 104
Cdd:cd14022     9 VFRAVHLHSGEELVCKVFDIGCYQES-----------------LAPCFCLpAHSNINQITEIILGETKAYVFFERSYGDM 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 105 LCF-EIVKRadagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGFGVAIQLGESGLVAG 183
Cdd:cd14022    72 HSFvRTCKK------LREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTR-VKLESLEDAYILRGHDDSLS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 184 GRVGTPHFMAPEVVKRE-PY-GKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMnPRQwshISESAKDLVR 260
Cdd:cd14022   145 DKHGCPAYVSPEILNTSgSYsGKAADVWSLGVMLYTMLVGRYPFHDIEpSSLFSKIRRGQFNI-PET---LSPKAKCLIR 220
                         250       260
                  ....*....|....*....|..
gi 1039796143 261 RMLMLDPAERITVYEALNHPWL 282
Cdd:cd14022   221 SILRREPSERLTSQEILDHPWF 242
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
4-271 1.87e-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: 96.60  E-value: 1.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   4 DDVLFEDvYELCEVIGKGPFSVVRRCINRETGQQFAVKIV--DVAKFTSSPGLSTEGKRWISNLKreasichmlKHPHIV 81
Cdd:cd05615     5 DRVRLTD-FNFLMVLGKGSFGKVMLAERKGSDELYAIKILkkDVVIQDDDVECTMVEKRVLALQD---------KPPFLT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  82 ELLETYSSDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENs 161
Cdd:cd05615    75 QLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGK----FKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGH- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 162 apVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIkgk 240
Cdd:cd05615   150 --IKIADFGMCKEHMVEGVTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEdELFQSIM--- 224
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1039796143 241 yKMNPRQWSHISESAKDLVRRMLMLDPAERI 271
Cdd:cd05615   225 -EHNVSYPKSLSKEAVSICKGLMTKHPAKRL 254
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
17-280 2.04e-21

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: 95.37  E-value: 2.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCinRETGQQFAVKIVDVAKFTSSPGLS----------TEGKRWISNLKREASICHMLKHPHIVELLET 86
Cdd:cd14000     1 LLGDGGFGSVYRA--SYKGEPVAVKIFNKHTSSNFANVPadtmlrhlraTDAMKNFRLLRQELTVLSHLHHPSIVYLLGI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYMVFEFMDGADLCFEIVKRADA--GFVYSEAVASHymrqILEALRYCHDNNIIHRDVKPHCVLLAS--KENSA 162
Cdd:cd14000    79 GIHPLMLVLELAPLGSLDHLLQQDSRSFAslGRTLQQRIALQ----VADGLRYLHSAMIIYRDLKSHNVLVWTlyPNSAI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 163 PVKLGGFGVAIQLGESGlvAGGRVGTPHFMAPEVVKRE-PYGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFEGI 236
Cdd:cd14000   155 IIKIADYGISRQCCRMG--AKGSEGTPGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSGGAPMVGHLKfpnefDIHGGL 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1039796143 237 IKGKYKMNPRQWSHIsesaKDLVRRMLMLDPAER---ITVYEALNHP 280
Cdd:cd14000   233 RPPLKQYECAPWPEV----EVLMKKCWKENPQQRptaVTVVSILNSP 275
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
12-283 2.09e-21

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: 96.39  E-value: 2.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAV-KIVDVAKFTSSPglstegkrwiSNLKREASICHMLKHPHIVELLETyssd 90
Cdd:cd07859     2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIkKINDVFEHVSDA----------TRILREIKLLRLLRHPDIVEIKHI---- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 gML----------YMVFEFMDgADLcFEIVKRADagfvysEAVASHY---MRQILEALRYCHDNNIIHRDVKPHCVLLAS 157
Cdd:cd07859    68 -MLppsrrefkdiYVVFELME-SDL-HQVIKAND------DLTPEHHqffLYQLLRALKYIHTANVFHRDLKPKNILANA 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 158 kenSAPVKLGGFG---VAIQLGESGLVAGGRVGTPHFMAPEVVKR--EPYGKPVDVWGCGVILFILLSGCLPFYGT---- 228
Cdd:cd07859   139 ---DCKLKICDFGlarVAFNDTPTAIFWTDYVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKnvvh 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 229 -----------------------KERLFEGIIKGKykmNPRQWSH----ISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd07859   216 qldlitdllgtpspetisrvrneKARRYLSSMRKK---QPVPFSQkfpnADPLALRLLERLLAFDPKDRPTAEEALADPY 292

                  ..
gi 1039796143 282 LK 283
Cdd:cd07859   293 FK 294
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
12-282 2.68e-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: 95.75  E-value: 2.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQ-FAVKIVdvakfTSSPGLSTEGKRWISNLKREASICHMLKHpHIVELLETYSSD 90
Cdd:cd14135     2 YRVYGYLGKGVFSNVVRARDLARGNQeVAIKII-----RNNELMHKAGLKELEILKKLNDADPDDKK-HCIRLLRHFEHK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGaDLcFEIVKR--ADAGFVYSeAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLGG 168
Cdd:cd14135    76 NHLCLVFESLSM-NL-REVLKKygKNVGLNIK-AVRS-YAQQLFLALKHLKKCNILHADIKPDNILVNEKKNT--LKLCD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLvaggrvgTPH-----FMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT--------------- 228
Cdd:cd14135   150 FGSASDIGENEI-------TPYlvsrfYRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKtnnhmlklmmdlkgk 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 229 -----------KERLFE--------------------------------GIIKGKYKMN---PRQWSHIsesaKDLVRRM 262
Cdd:cd14135   223 fpkkmlrkgqfKDQHFDenlnfiyrevdkvtkkevrrvmsdikptkdlkTLLIGKQRLPdedRKKLLQL----KDLLDKC 298
                         330       340
                  ....*....|....*....|
gi 1039796143 263 LMLDPAERITVYEALNHPWL 282
Cdd:cd14135   299 LMLDPEKRITPNEALQHPFI 318
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
12-271 3.78e-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: 3.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEGKRWISNLK---REASichmlKHPHIVELLETYS 88
Cdd:cd05617    17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDD-----EDIDWVQTEKhvfEQAS-----SNPFLVGLHSCFQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGG 168
Cdd:cd05617    87 TTSRLFLVIEYVNGGDLMFHMQRQRK----LPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLL---DADGHIKLTD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF--------YGTKERLFEGIIKGK 240
Cdd:cd05617   160 YGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiitdnpdMNTEDYLFQVILEKP 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1039796143 241 YKMnPRqwsHISESAKDLVRRMLMLDPAERI 271
Cdd:cd05617   240 IRI-PR---FLSVKASHVLKGFLNKDPKERL 266
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
12-225 3.95e-21

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: 94.11  E-value: 3.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCE-VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstegkrwisnlkREASICHMLKHPHIVELLETYSSD 90
Cdd:cd13991     7 WATHQlRIGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRA----------------EELMACAGLTSPRVVPLYGAVREG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApvKLGGFG 170
Cdd:cd13991    71 PWVNIFMDLKEGGSLGQLIKEQG----CLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDA--FLCDFG 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VAIQLGESG----LVAGGRV-GTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF 225
Cdd:cd13991   145 HAECLDPDGlgksLFTGDYIpGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
18-287 4.80e-21

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 95.66  E-value: 4.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVdvakftssPGLSTEGKRwiSNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:PLN00034   82 IGSGAGGTVYKVIHRPTGRLYALKVI--------YGNHEDTVR--RQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLL 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLcfeivkraDAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 177
Cdd:PLN00034  152 EFMDGGSL--------EGTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKN---VKIADFGVSRILAQ 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 SGLVAGGRVGTPHFMAPEVVKRE----PY-GKPVDVWGCGVILFILLSGCLPF----YGTKERLFEGIIkgkYKMNPRQW 248
Cdd:PLN00034  221 TMDPCNSSVGTIAYMSPERINTDlnhgAYdGYAGDIWSLGVSILEFYLGRFPFgvgrQGDWASLMCAIC---MSQPPEAP 297
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1039796143 249 SHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDR 287
Cdd:PLN00034  298 ATASREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQP 336
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
11-280 4.83e-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: 93.53  E-value: 4.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTEGKRWISNLKReasicHML--KHPHIVELLETYS 88
Cdd:cd14050     2 CFTILSKLGEGSFGEVFKVRSREDGKLYAVK-----RSRSRFRGEKDRKRKLEEVER-----HEKlgEHPNCVRFIKAWE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDG--ADLCFEIVKradagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKL 166
Cdd:cd14050    72 EKGILYIQTELCDTslQQYCEETHS-------LPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLS---KDGVCKL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAIQLGESGlVAGGRVGTPHFMAPEVVkREPYGKPVDVWGCGVIlfILLSGC---LPFYGTK-ERLFEGIIKgkyk 242
Cdd:cd14050   142 GDFGLVVELDKED-IHDAQEGDPRYMAPELL-QGSFTKAADIFSLGIT--ILELACnleLPSGGDGwHQLRQGYLP---- 213
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039796143 243 mnPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd14050   214 --EEFTAGLSPELRSIIKLMMDPDPERRPTAEDLLALP 249
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
14-227 1.06e-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: 92.80  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  14 LCEVIGKGPFSVVRRCInrETGQQFAVKivdVAKFTSSPGLStegkRWISNLKREASICHMLKHPHIVELLETYSSDGML 93
Cdd:cd14145    10 LEEIIGIGGFGKVYRAI--WIGDEVAVK---AARHDPDEDIS----QTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  94 YMVFEFMDGADLcfeivKRADAGFVYSEAVASHYMRQILEALRYCHDNNI---IHRDVKPHCVLLASK-EN----SAPVK 165
Cdd:cd14145    81 CLVMEFARGGPL-----NRVLSGKRIPPDILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILILEKvENgdlsNKILK 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 166 LGGFGVAIQLGESGLVAGGrvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 227
Cdd:cd14145   156 ITDFGLAREWHRTTKMSAA--GTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRG 215
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
18-280 1.34e-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: 94.18  E-value: 1.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstegKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd05610    12 ISRGAFGKVYLGRKKNNSKLYAVKVVKKADMIN--------KNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADlcfeiVKRADAGFVY-SEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVA-IQL 175
Cdd:cd05610    84 EYLIGGD-----VKSLLHIYGYfDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLIS---NEGHIKLTDFGLSkVTL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GE-------------------------------SGL--------------------VAGGRV-GTPHFMAPEVVKREPYG 203
Cdd:cd05610   156 NRelnmmdilttpsmakpkndysrtpgqvlsliSSLgfntptpyrtpksvrrgaarVEGERIlGTPDYLAPELLLGKPHG 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796143 204 KPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMnPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd05610   236 PAVDWWALGVCLFEFLTGIPPFNDeTPQQVFQNILNRDIPW-PEGEEELSVNAQNAIEILLTMDPTKRAGLKELKQHP 312
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
12-283 1.53e-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: 94.53  E-value: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftsspgLSTE--GKRWISNLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd05629     3 FHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTL----------LKSEmfKKDQLAHVKAERDVLAESDSPWVVSLYYSFQD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGF 169
Cdd:cd05629    73 AQYLYLIMEFLPGGDLMTMLIKYD----TFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGH---IKLSDF 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GV-----------------------------------AIQLGESG------------LVAGGRVGTPHFMAPEVVKREPY 202
Cdd:cd05629   146 GLstgfhkqhdsayyqkllqgksnknridnrnsvavdSINLTMSSkdqiatwkknrrLMAYSTVGTPDYIAPEIFLQQGY 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 203 GKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRmLMLDPAERITVY---EALN 278
Cdd:cd05629   226 GQECDWWSLGAIMFECLIGWPPFCSeNSHETYRKIINWRETLYFPDDIHLSVEAEDLIRR-LITNAENRLGRGgahEIKS 304

                  ....*
gi 1039796143 279 HPWLK 283
Cdd:cd05629   305 HPFFR 309
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
16-282 1.53e-20

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: 92.72  E-value: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTegkrwisnlkREASICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd07870     6 EKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTAI----------REASLLKGLKHANIVLLHDIIHTKETLTF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDgADLCFEIVKRAdaGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQL 175
Cdd:cd07870    76 VFEYMH-TDLAQYMIQHP--GGLHPYNVRL-FMFQLLRGLAYIHGQHILHRDLKPQNLLIS---YLGELKLADFGLARAK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GESGLVAGGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGTK-----------------ERLFEGII 237
Cdd:cd07870   149 SIPSQTYSSEVVTLWYRPPDVLlGATDYSSALDIWGAGCIFIEMLQGQPAFPGVSdvfeqlekiwtvlgvptEDTWPGVS 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796143 238 K-GKYK------MNPRQ----WSHISE--SAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd07870   229 KlPNYKpewflpCKPQQlrvvWKRLSRppKAEDLASQMLMMFPKDRISAQDALLHPYF 286
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
18-287 2.67e-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: 92.12  E-value: 2.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVakftsspglstEGKRWISN-LKREASICHMLKHPHIVELLETYSSD-GMLYM 95
Cdd:cd06620    13 LGAGNGGSVSKVLHIPTGTIMAKKVIHI-----------DAKSSVRKqILRELQILHECHSPYIVSFYGAFLNEnNNIII 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHD-NNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQ 174
Cdd:cd06620    82 CMEYMDCGSLD-KILKKKGP---FPEEVLGKIAVAVLEGLTYLYNvHRIIHRDIKPSNILVNSK---GQIKLCDFGVSGE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 175 LGESglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLF-----EGIIKGKYKM----NP 245
Cdd:cd06620   155 LINS--IADTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDgyngpMGILDLLQRIvnepPP 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1039796143 246 RQWSHI--SESAKDLVRRMLMLDPAERITVYEALNHPWLKERDR 287
Cdd:cd06620   233 RLPKDRifPKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQAVR 276
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
73-282 2.88e-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: 2.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  73 HMLKHPHIVELLETYSSDGMLYMVFEfMDGADLCFEIVKRADAGfvysEAVASHYMRQILEALRYCHDNNIIHRDVKPHC 152
Cdd:cd14023    40 QLPSHRNITGIVEVILGDTKAYVFFE-KDFGDMHSYVRSCKRLR----EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRK 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 153 VLLASKENSApVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKRE-PY-GKPVDVWGCGVILFILLSGCLPFYGTK- 229
Cdd:cd14023   115 FVFSDEERTQ-LRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILNTTgTYsGKSADVWSLGVMLYTLLVGRYPFHDSDp 193
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039796143 230 ERLFEGIIKGKYKMNprqwSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14023   194 SALFSKIRRGQFCIP----DHVSPKARCLIRSLLRREPSERLTAPEILLHPWF 242
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
16-286 2.95e-20

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: 92.94  E-value: 2.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIvdvakftsspglstegkrwisnLKREASI------CHML---------KHPHI 80
Cdd:cd05591     1 KVLGKGSFGKVMLAERKGTDEVYAIKV----------------------LKKDVILqdddvdCTMTekrilalaaKHPFL 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  81 VELLETYSSDGMLYMVFEFMDGADLCFEIvKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEN 160
Cdd:cd05591    59 TALHSCFQTKDRLFFVMEYVNGGDLMFQI-QRARK---FDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGH 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 161 sapVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKG 239
Cdd:cd05591   135 ---CKLADFGMCKEGILNGKTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEdDLFESILHD 211
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796143 240 K--YKMnprqWshISESAKDLVRRMLMLDPAERITVYEA-------LNHPWLKERD 286
Cdd:cd05591   212 DvlYPV----W--LSKEAVSILKAFMTKNPAKRLGCVASqggedaiRQHPFFREID 261
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
18-277 3.24e-20

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


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 91.57  E-value: 3.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCInRETGQQFAVKIVDVakfTSSPGLSTEgkrwisnLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd14066     1 IGSGGFGTVYKGV-LENGTVVAVKRLNE---MNCAASKKE-------FLTELEMLGRLRHPNLVRLLGYCLESDEKLLVY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLcFEIVKRADAGFVYS----EAVASHymrqILEALRYCH---DNNIIHRDVKPHCVLLasKENSAPvKLGGFG 170
Cdd:cd14066    70 EYMPNGSL-EDRLHCHKGSPPLPwpqrLKIAKG----IARGLEYLHeecPPPIIHGDIKSSNILL--DEDFEP-KLTDFG 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VA--IQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYgtKERLFEGiikgkyKMNPRQW 248
Cdd:cd14066   142 LArlIPPSESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVD--ENRENAS------RKDLVEW 213
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1039796143 249 --SHISESAKDLVRRMLMLDPAERITVYEAL 277
Cdd:cd14066   214 veSKGKEELEDILDKRLVDDDGVEEEEVEAL 244
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
18-225 3.36e-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: 91.95  E-value: 3.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKivdvakfTSSPGLSTEGK-RWisnlKREASICHMLKHPHIV------ELLETYSSD 90
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIK-------QCRQELSPKNReRW----CLEIQIMKRLNHPNVVaardvpEGLQKLAPN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFG 170
Cdd:cd14038    71 DLPLLAMEYCQGGDLRKYLNQFENCCGLREGAILT-LLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLIHKIIDLG 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039796143 171 VAIQLGESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF 225
Cdd:cd14038   150 YAKELDQGSLCT-SFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
11-282 3.72e-20

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: 90.80  E-value: 3.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTeGKRW---ISNLKREASichmlKHPHIVELLETY 87
Cdd:cd14100     1 QYQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEWGELPN-GTRVpmeIVLLKKVGS-----GFRGVIRLLDWF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLasKENSAPVKLG 167
Cdd:cd14100    75 ERPDSFVLVLERPEPVQDLFDFITERGA---LPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILI--DLNTGELKLI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVAIQLGESGLV--AGGRVGTPhfmaPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKErlfegIIKGKYKMN 244
Cdd:cd14100   150 DFGSGALLKDTVYTdfDGTRVYSP----PEWIRFHRYhGRSAAVWSLGILLYDMVCGDIPFEHDEE-----IIRGQVFFR 220
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039796143 245 PRqwshISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14100   221 QR----VSSECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
12-283 3.94e-20

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 96.34  E-value: 3.94e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   12 YELCEVIGKGPFsvvrrcinretGQQFAVKIVDVAKFTSSPGLSTEG--KRWISNLKREASICHMLKHPHIVELLETY-- 87
Cdd:PTZ00266    15 YEVIKKIGNGRF-----------GEVFLVKHKRTQEFFCWKAISYRGlkEREKSQLVIEVNVMRELKHKNIVRYIDRFln 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   88 SSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHD-------NNIIHRDVKPHCVLL----- 155
Cdd:PTZ00266    84 KANQKLYILMEFCDAGDLSRNIQKCYKMFGKIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLstgir 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  156 --------ASKENSAPV-KLGGFGVAIQLG-ESglVAGGRVGTPHFMAPEVVKRE--PYGKPVDVWGCGVILFILLSGCL 223
Cdd:PTZ00266   164 higkitaqANNLNGRPIaKIGDFGLSKNIGiES--MAHSCVGTPYYWSPELLLHEtkSYDDKSDMWALGCIIYELCSGKT 241
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039796143  224 PFYgtKERLFEGIIKgKYKMNPRQwsHISESAKD---LVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:PTZ00266   242 PFH--KANNFSQLIS-ELKRGPDL--PIKGKSKElniLIKNLLNLSAKERPSALQCLGYQIIK 299
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
12-280 4.14e-20

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: 91.33  E-value: 4.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINR-ETGQQFAVKIVDVAKftsspGLSTEGKRwisnLKREASICHMLK---HPHIVELLETY 87
Cdd:cd14052     2 FANVELIGSGEFSQVYKVSERvPTGKVYAVKKLKPNY-----AGAKDRLR----RLEEVSILRELTldgHDNIVQLIDSW 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCFEIVKRADAGfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLG 167
Cdd:cd14052    73 EYHGHLYIQTELCENGSLDVFLSELGLLG-RLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGT---LKIG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVAIQLG-ESGL-VAGGRVgtphFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYGTK------------ERL 232
Cdd:cd14052   149 DFGMATVWPlIRGIeREGDRE----YIAPEILSEHMYDKPADIFSLGLILLeAAANVVLPDNGDAwqklrsgdlsdaPRL 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 233 FEGIIKG--KYKMNPRQW----SHISESAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd14052   225 SSTDLHSasSPSSNPPPDppnmPILSGSLDRVVRWMLSPEPDRRPTADDVLATP 278
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
10-286 5.81e-20

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: 92.81  E-value: 5.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstegKRWISNLKREASICHMLKHPHIVELLETYSS 89
Cdd:cd05627     2 DDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLE--------KEQVAHIRAERDILVEADGAWVVKMFYSFQD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGF 169
Cdd:cd05627    74 KRNLYLIMEFLPGGDMMTLLMKKD----TLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGH---VKLSDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESG-----------------------------------LVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVI 214
Cdd:cd05627   147 GLCTGLKKAHrtefyrnlthnppsdfsfqnmnskrkaetwkknrrQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVI 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796143 215 LFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRmLMLDPAERI---TVYEALNHPWLKERD 286
Cdd:cd05627   227 MYEMLIGYPPFCSeTPQETYRKVMNWKETLVFPPEVPISEKAKDLILR-FCTDAENRIgsnGVEEIKSHPFFEGVD 301
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
12-284 6.08e-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: 92.08  E-value: 6.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLStegKRWISNLKReasICHMLKHPHIVELLE----TY 87
Cdd:cd07857     2 YELIKELGQGAYGIVCSARNAETSEEETVAIKKITNVFSKKILA---KRALRELKL---LRHFRGHKNITCLYDmdivFP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDgADLCfEIVKradAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLG 167
Cdd:cd07857    76 GNFNELYLYEELME-ADLH-QIIR---SGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNA---DCELKIC 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVAIQLGES-GLVAG---GRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGcLPFYGTK---ERLFEgIIK- 238
Cdd:cd07857   148 DFGLARGFSENpGENAGfmtEYVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLGR-KPVFKGKdyvDQLNQ-ILQv 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 239 ------------------------GKYKMNPRQWSHISES--AKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd07857   226 lgtpdeetlsrigspkaqnyirslPNIPKKPFESIFPNANplALDLLEKLLAFDPTKRISVEEALEHPYLAI 297
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
12-282 7.10e-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: 92.07  E-value: 7.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLsTEGKRWISNLKREASICHmlkhpHIVELLETYSSDG 91
Cdd:cd14225    45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFHHQAL-VEVKILDALRRKDRDNSH-----NVIHMKEYFYFRN 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMdGADLcFEIVKRAD-AGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSAPVKLGGFG 170
Cdd:cd14225   119 HLCITFELL-GMNL-YELIKKNNfQGF--SLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILL-RQRGQSSIKVIDFG 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 vaiqlgeSGLVAGGRVGT----PHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE---------------- 230
Cdd:cd14225   194 -------SSCYEHQRVYTyiqsRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEveqlacimevlglppp 266
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039796143 231 ---------RLF-------EGII--KG-KYKMNPRQWSHISESAK----DLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14225   267 elienaqrrRLFfdskgnpRCITnsKGkKRRPNSKDLASALKTSDplflDFIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
8-270 7.17e-20

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: 90.63  E-value: 7.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvaKFTSSpglstegkrwisNLKREASICHMLKHPHIVELLETY 87
Cdd:cd14047     4 FRQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRV---KLNNE------------KAEREVKALAKLDHPNIVRYNGCW 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 S-SDGM---------------LYMVFEFMDGADLCFEIVKRadaGFVYSEAVASHYM-RQILEALRYCHDNNIIHRDVKP 150
Cdd:cd14047    69 DgFDYDpetsssnssrsktkcLFIQMEFCEKGTLESWIEKR---NGEKLDKVLALEIfEQITKGVEYIHSKKLIHRDLKP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 151 HCVLLAskeNSAPVKLGGFGVAIQLGESGLVAGGRvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE 230
Cdd:cd14047   146 SNIFLV---DTGKVKIGDFGLVTSLKNDGKRTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEKSK 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039796143 231 rLFEGIIKGKYKMNPRQWSHISESakdLVRRMLMLDPAER 270
Cdd:cd14047   222 -FWTDLRNGILPDIFDKRYKIEKT---IIKKMLSKKPEDR 257
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
74-283 8.50e-20

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 90.30  E-value: 8.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  74 MLKHPHIVELLETYSSDGMLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCV 153
Cdd:PHA03390   65 MKDNPNFIKLYYSVTTLKGHVLIMDYIKDGDL-FDLLKKEGK---LSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENV 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 154 LLASKENSapvklggfgvaIQLGESGLVAggRVGTPH-------FMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY 226
Cdd:PHA03390  141 LYDRAKDR-----------IYLCDYGLCK--IIGTPScydgtldYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFK 207
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 227 GTKERLFEgiIKgkyKMNPRQW------SHISESAKDLVRRMLMLDPAERITVYEA-LNHPWLK 283
Cdd:PHA03390  208 EDEDEELD--LE---SLLKRQQkklpfiKNVSKNANDFVQSMLKYNINYRLTNYNEiIKHPFLK 266
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
12-279 9.69e-20

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: 90.32  E-value: 9.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPglstegkrwiSNLKREASICHMLKHPHIVELLETYSS-- 89
Cdd:cd14048     8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELAR----------EKVLREVRALAKLDHPGIVRYFNAWLErp 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 ---------DGMLYMVFEfmdgadLCF-EIVKRADAGFVYSEAVASHYM----RQILEALRYCHDNNIIHRDVKPHCVLL 155
Cdd:cd14048    78 pegwqekmdEVYLYIQMQ------LCRkENLKDWMNRRCTMESRELFVClnifKQIASAVEYLHSKGLIHRDLKPSNVFF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 156 ASKENsapVKLGGFGVA------------IQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLsgcL 223
Cdd:cd14048   152 SLDDV---VKVGDFGLVtamdqgepeqtvLTPMPAYAKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI---Y 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796143 224 PFYGTKERL--FEGIIKGKYkmnPRQWSHISESAKDLVRRMLMLDPAERITVYEALNH 279
Cdd:cd14048   226 SFSTQMERIrtLTDVRKLKF---PALFTNKYPEERDMVQQMLSPSPSERPEAHEVIEH 280
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
17-227 1.21e-19

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


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 89.37  E-value: 1.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRetGQQFAVKI--VDVAKftsspglstEGKRWISNLKREASICHMLKHPHIVELLETYSSDGMLY 94
Cdd:cd14061     1 VIGVGGFGKVYRGIWR--GEEVAVKAarQDPDE---------DISVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLC 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  95 MVFEFMDGADLcfeivKRADAGFVYSEAVASHYMRQILEALRYCHDNN---IIHRDVKPHCVLLASKENSAPV-----KL 166
Cdd:cd14061    70 LVMEYARGGAL-----NRVLAGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAIENEDLenktlKI 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796143 167 GGFGVAIQLGESGLVAGGrvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 227
Cdd:cd14061   145 TDFGLAREWHKTTRMSAA--GTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKG 203
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
131-279 1.38e-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: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 131 ILEALrycHDNNIIHRDVKPHCVLLASKENSapVKLGGFGVAIQL-GESGLVAGGRvGTPHFMAPEVVKREPY-GKPVDV 208
Cdd:cd13974   144 VVEAL---HKKNIVHRDLKLGNMVLNKRTRK--ITITNFCLGKHLvSEDDLLKDQR-GSPAYISPDVLSGKPYlGKPSDM 217
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 209 WGCGVILFILLSGCLPFY-GTKERLFEGIIKGKYKMnPRQwSHISESAKDLVRRMLMLDPAERITVYEALNH 279
Cdd:cd13974   218 WALGVVLFTMLYGQFPFYdSIPQELFRKIKAAEYTI-PED-GRVSENTVCLIRKLLVLNPQKRLTASEVLDS 287
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
12-282 2.08e-19

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: 89.36  E-value: 2.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDV-----AKFTSSpglstegkrwisnlkREASICHMLKHPHIVELLET 86
Cdd:cd07844     2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLeheegAPFTAI---------------REASLLKDLKHANIVTLHDI 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYMVFEFMDgADLCFEIvkrADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKL 166
Cdd:cd07844    67 IHTKKTLTLVFEYLD-TDLKQYM---DDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISER---GELKL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAiqlgesglvAGGRVGTpHFMAPEVVK---REP--------YGKPVDVWGCGVILFILLSGCLPFYGTK------ 229
Cdd:cd07844   140 ADFGLA---------RAKSVPS-KTYSNEVVTlwyRPPdvllgsteYSTSLDMWGVGCIFYEMATGRPLFPGSTdvedql 209
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 230 ERLFE-----------GIIK---------GKYKMNP--RQWSHIS--ESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd07844   210 HKIFRvlgtpteetwpGVSSnpefkpysfPFYPPRPliNHAPRLDriPHGEELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
11-282 2.39e-19

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: 89.30  E-value: 2.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEGKRWISNLKREAsichmlKHPHIVELLETY--- 87
Cdd:cd06636    17 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEE-----EIKLEINMLKKYS------HHRNIATYYGAFikk 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 ---SSDGMLYMVFEFMdGADLCFEIVKRADaGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskENsAPV 164
Cdd:cd06636    86 sppGHDDQLWLVMEFC-GAGSVTDLVKNTK-GNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT--EN-AEV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 165 KLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKRE-----PYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEGII 237
Cdd:cd06636   161 KLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDenpdaTYDYRSDIWSLGITAIEMAEGAPPLCDMHpmRALFLIPR 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039796143 238 KGKYKMNPRQWshiSESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd06636   241 NPPPKLKSKKW---SKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
28-282 2.41e-19

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: 88.40  E-value: 2.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  28 RCINRETGQQFAVKIVDVAKFTSSPGLSTEgkrwisnlkreasichMLKHPHIVELLETYSSDGMLYMVFEFMDGaDLCF 107
Cdd:cd14024    11 RAEHYQTEKEYTCKVLSLRSYQECLAPYDR----------------LGPHEGVCSVLEVVIGQDRAYAFFSRHYG-DMHS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 108 EIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapvKLggfgVAIQLGESGLVAGG--- 184
Cdd:cd14024    74 HVRRRRR----LSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRT---KL----VLVNLEDSCPLNGDdds 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 185 ---RVGTPHFMAPEVV--KREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNprqwSHISESAKDL 258
Cdd:cd14024   143 ltdKHGCPAYVGPEILssRRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAaLFAKIRRGAFSLP----AWLSPGARCL 218
                         250       260
                  ....*....|....*....|....
gi 1039796143 259 VRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14024   219 VSCMLRRSPAERLKASEILLHPWL 242
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
18-270 2.52e-19

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: 89.32  E-value: 2.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLStegkrwisNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd08229    32 IGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARA--------DCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGE 177
Cdd:cd08229   104 ELADAGDLSRMIKHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITA---TGVVKLGDLGLGRFFSS 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIK-GKYKMNPRQWSHISESAK 256
Cdd:cd08229   181 KTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKiEQCDYPPLPSDHYSEELR 260
                         250
                  ....*....|....
gi 1039796143 257 DLVRRMLMLDPAER 270
Cdd:cd08229   261 QLVNMCINPDPEKR 274
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
9-286 2.83e-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: 89.42  E-value: 2.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEvIGKGPFSVVRRCINRETGQQFAVKIVDVakftsspglstEGKRWISN-LKREASICHMLKHPHIVELLETY 87
Cdd:cd06615     1 DDFEKLGE-LGAGNGGVVTKVLHRPSGLIMARKLIHL-----------EIKPAIRNqIIRELKVLHECNSPYIVGFYGAF 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGA--DLCFEIVKRADAGFVYSEAVAshymrqILEALRYCHDN-NIIHRDVKPHCVLLASkenSAPV 164
Cdd:cd06615    69 YSDGEISICMEHMDGGslDQVLKKAGRIPENILGKISIA------VLRGLTYLREKhKIMHRDVKPSNILVNS---RGEI 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 165 KLGGFGVAIQLGESglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGII-----KG 239
Cdd:cd06615   140 KLCDFGVSGQLIDS--MANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKELEAMFgrpvsEG 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 240 KYKMNPRQWS------------------------------HISESAKDLVRRMLMLDPAERITVYEALNHPWLKERD 286
Cdd:cd06615   218 EAKESHRPVSghppdsprpmaifelldyivnepppklpsgAFSDEFQDFVDKCLKKNPKERADLKELTKHPFIKRAE 294
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
7-283 4.68e-19

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: 89.69  E-value: 4.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   7 LFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftsspglsTEGKRWISNLKREASICHML-KHP-----HI 80
Cdd:cd14226    10 KWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKII------------KNKKAFLNQAQIEVRLLELMnKHDtenkyYI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  81 VELLETYSSDGMLYMVFEFMDgADLcFEIVKRADAGFVySEAVASHYMRQILEALRYCH--DNNIIHRDVKPHCVLLASK 158
Cdd:cd14226    78 VRLKRHFMFRNHLCLVFELLS-YNL-YDLLRNTNFRGV-SLNLTRKFAQQLCTALLFLStpELSIIHCDLKPENILLCNP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 159 ENSApVKLGGFGVAIQLGEsglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-------- 230
Cdd:cd14226   155 KRSA-IKIIDFGSSCQLGQ---RIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEvdqmnkiv 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 231 ------------------RLFEGIIKGKY-------KMNPRQWSHISESA---------------------------KDL 258
Cdd:cd14226   231 evlgmppvhmldqapkarKFFEKLPDGTYylkktkdGKKYKPPGSRKLHEilgvetggpggrragepghtvedylkfKDL 310
                         330       340
                  ....*....|....*....|....*
gi 1039796143 259 VRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd14226   311 ILRMLDYDPKTRITPAEALQHSFFK 335
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
12-282 5.35e-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: 89.23  E-value: 5.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakfTSSPGLSTEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVL-----KNKPAYFRQAMLEIAILTLLNTKYDPEDKHHIVRLLDHFMHHG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEfMDGADLcFEIVK-RADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkENSAPVKLGGFG 170
Cdd:cd14212    76 HLCIVFE-LLGVNL-YELLKqNQFRGL--SLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVN-LDSPEIKLIDFG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VA----------IQlgesglvaggrvgTPHFMAPEVVKREPYGKPVDVW--GC-------GVILF------------ILL 219
Cdd:cd14212   151 SAcfenytlytyIQ-------------SRFYRSPEVLLGLPYSTAIDMWslGCiaaelflGLPLFpgnseynqlsriIEM 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 220 SGCLPFY----GTK-----ERLFEGIIKGKYKM--------------------------------NPRQWSHISESAK-- 256
Cdd:cd14212   218 LGMPPDWmlekGKNtnkffKKVAKSGGRSTYRLktpeefeaenncklepgkryfkyktlediimnYPMKKSKKEQIDKem 297
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1039796143 257 -------DLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14212   298 etrlafiDFLKGLLEYDPKKRWTPDQALNHPFI 330
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
17-286 5.40e-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: 88.26  E-value: 5.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTE-GKRWISNLKREASIChmlkhPHIVELLETYSSDGMLYM 95
Cdd:cd05606     1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLAlNERIMLSLVSTGGDC-----PFIVCMTYAFQTPDKLCF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQL 175
Cdd:cd05606    76 ILDLMNGGDLHYHLSQHG----VFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILL---DEHGHVRISDLGLACDF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GESGLVAGgrVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISES 254
Cdd:cd05606   149 SKKKPHAS--VGTHGYMAPEVLqKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKHEIDRMTLTMNVELPDSFSPE 226
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1039796143 255 AKDLVRRMLMLDPAERI-----TVYEALNHPWLKERD 286
Cdd:cd05606   227 LKSLLEGLLQRDVSKRLgclgrGATEVKEHPFFKGVD 263
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
10-284 6.60e-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: 88.60  E-value: 6.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTegkrwisnlkREASICHMLKHPHIVELLETYSS 89
Cdd:cd07869     5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAI----------REASLLKGLKHANIVLLHDIIHT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDgADLCFEIVKRAdaGFVYSEAVaSHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGF 169
Cdd:cd07869    75 KETLTLVFEYVH-TDLCQYMDKHP--GGLHPENV-KLFLFQLLRGLSYIHQRYILHRDLKPQNLLIS---DTGELKLADF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGTK------ERLF-------EG 235
Cdd:cd07869   148 GLARAKSVPSHTYSNEVVTLWYRPPDVlLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKdiqdqlERIFlvlgtpnED 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796143 236 IIKGKYKM--------------NPRQ-WSHIS--ESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd07869   228 TWPGVHSLphfkperftlyspkNLRQaWNKLSyvNHAEDLASKLLQCFPKNRLSAQAALSHEYFSD 293
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
3-287 8.39e-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: 88.17  E-value: 8.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   3 DDDVLFEDVYElcevIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTEgkRWiSNLKREASICHMLKHPHIVE 82
Cdd:cd06633    18 DPEEIFVDLHE----IGHGSFGAVYFATNSHTNEVVAIK-----KMSYSGKQTNE--KW-QDIIKEVKFLQQLKHPNTIE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  83 LLETYSSDGMLYMVFEFMDGA--DLcFEIVKRAdagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASken 160
Cdd:cd06633    86 YKGCYLKDHTAWLVMEYCLGSasDL-LEVHKKP-----LQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTE--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 161 SAPVKLGGFGVAIQLGEsglvAGGRVGTPHFMAPEVV---KREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEG 235
Cdd:cd06633   157 PGQVKLADFGSASIASP----ANSFVGTPYWMAPEVIlamDEGQYDGKVDIWSLGITCIELAERKPPLFNMNamSALYHI 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 236 IIKGKYKMNPRQWshiSESAKDLVRRMLMLDPAERITVYEALNHPWLKeRDR 287
Cdd:cd06633   233 AQNDSPTLQSNEW---TDSFRGFVDYCLQKIPQERPSSAELLRHDFVR-RER 280
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
11-303 8.66e-19

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: 87.85  E-value: 8.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsSPGLSTEGKRWISNLKreasichmlKHPHIVELLETYSS- 89
Cdd:cd06637     7 IFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDV-----TGDEEEEIKQEINMLK---------KYSHHRNIATYYGAf 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 --------DGMLYMVFEFMdGADLCFEIVKRADAGFVYSEAVAsHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenS 161
Cdd:cd06637    73 ikknppgmDDQLWLVMEFC-GAGSVTDLIKNTKGNTLKEEWIA-YICREILRGLSHLHQHKVIHRDIKGQNVLLTE---N 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 162 APVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKRE-----PYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFE 234
Cdd:cd06637   148 AEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDenpdaTYDFKSDLWSLGITAIEMAEGAPPLCDMHpmRALFL 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 235 GIIKGKYKMNPRQWSHISESakdLVRRMLMLDPAERITVYEALNHPWLKER-DRYAYKIHLPETVEQLRK 303
Cdd:cd06637   228 IPRNPAPRLKSKKWSKKFQS---FIESCLVKNHSQRPSTEQLMKHPFIRDQpNERQVRIQLKDHIDRTKK 294
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
12-281 9.57e-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: 87.78  E-value: 9.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQF-AVKIVDVAkfTSSPGLSTEGKRWISNLKREASichmLKHPHIVELLETYS-- 88
Cdd:cd07862     3 YECVAEIGEGAYGKVFKARDLKNGGRFvALKRVRVQ--TGEEGMPLSTIREVAVLRHLET----FEHPNVVRLFDVCTvs 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 ---SDGMLYMVFEFMDgADLCFEIVKRADAGfVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVK 165
Cdd:cd07862    77 rtdRETKLTLVFEHVD-QDLTTYLDKVPEPG-VPTETIKD-MMFQLLRGLDFLHSHRVVHRDLKPQNILVTS---SGQIK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 166 LGGFGVA----IQLGESGLVAggrvgTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-----RLFE-- 234
Cdd:cd07862   151 LADFGLAriysFQMALTSVVV-----TLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDvdqlgKILDvi 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 235 ------------GIIKGKYKMNPRQ-----WSHISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd07862   226 glpgeedwprdvALPRQAFHSKSAQpiekfVTDIDELGKDLLLKCLTFNPAKRISAYSALSHPY 289
PLN02772 PLN02772
guanylate kinase
718-895 9.63e-19

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 89.51  E-value: 9.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 718 KTLVLLGAHGVGrrhiKNTLITK----HPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAM 793
Cdd:PLN02772  136 KPIVISGPSGVG----KGTLISMlmkeFPSMFGFSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFASVHGNL 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 794 YGTKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTITP--------GLNEDESLQ-RLQK-ESDVLQRT 863
Cdd:PLN02772  212 YGTSIEAVEVVTDSGKRCILDIDVQGARSVRASSLEAIFIFICPPSMEElekrlrarGTETEEQIQkRLRNaEAELEQGK 291
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1039796143 864 YAHYFDLTIINNEIDETIRHLEEAVELVCTAP 895
Cdd:PLN02772  292 SSGIFDHILYNDNLEECYKNLKKLLGLDGLAA 323
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
17-271 1.01e-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: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEGKRWISNLK---REASichmlKHPHIVELLETYSSDGML 93
Cdd:cd05588     2 VIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDD-----EDIDWVQTEKhvfETAS-----NHPFLVGLHSCFQTESRL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  94 YMVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAI 173
Cdd:cd05588    72 FFVIEFVNGGDLMFHMQRQRR----LPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGH---IKLTDYGMCK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 174 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF----------YGTKERLFEGIIKGKYKM 243
Cdd:cd05588   145 EGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgssdnpdQNTEDYLFQVILEKPIRI 224
                         250       260
                  ....*....|....*....|....*...
gi 1039796143 244 nPRQwshISESAKDLVRRMLMLDPAERI 271
Cdd:cd05588   225 -PRS---LSVKAASVLKGFLNKNPAERL 248
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
12-289 1.17e-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: 1.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTEGKRwisnLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd07850     2 YQNLKPIGSGAQGIVCAAYDTVTGQNVAIK-----KLSRPFQNVTHAKR----AYRELVLMKLVNHKNIIGLLNVFTPQK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 ML------YMVFEFMDgADLCFEIVKRADagfvysEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVK 165
Cdd:cd07850    73 SLeefqdvYLVMELMD-ANLCQVIQMDLD------HERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD---CTLK 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 166 LGGFGVAIQLGESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK---------------- 229
Cdd:cd07850   143 ILDFGLARTAGTSFMMT-PYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDhidqwnkiieqlgtps 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 230 ----ERLfeGIIKGKYKMN-PRQWSH---------------------ISESAKDLVRRMLMLDPAERITVYEALNHP--- 280
Cdd:cd07850   222 defmSRL--QPTVRNYVENrPKYAGYsfeelfpdvlfppdseehnklKASQARDLLSKMLVIDPEKRISVDDALQHPyin 299
                         330
                  ....*....|
gi 1039796143 281 -WLKERDRYA 289
Cdd:cd07850   300 vWYDPSEVEA 309
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
11-282 1.19e-18

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: 86.55  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  11 VYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTsspglstegkRW--ISNLKREASICHMLKHPH----IVELL 84
Cdd:cd14102     1 VYQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVT----------EWgtLNGVMVPLEIVLLKKVGSgfrgVIKLL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  85 ETYSS-DGMLyMVFEFMDGADLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKenSAP 163
Cdd:cd14102    71 DWYERpDGFL-IVMERPEPVKDLFDFITEKGA---LDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLR--TGE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 164 VKLGGFGVAIQLGESGLV--AGGRVGTPhfmaPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKErlfegIIKGK 240
Cdd:cd14102   145 LKLIDFGSGALLKDTVYTdfDGTRVYSP----PEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPFEQDEE-----ILRGR 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1039796143 241 YKMNPRqwshISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14102   216 LYFRRR----VSPECQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
12-282 1.37e-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: 88.55  E-value: 1.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTEGKRwisnLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd07876    23 YQQLKPIGSGAQGIVCAAFDTVLGINVAVK-----KLSRPFQNQTHAKR----AYRELVLLKCVNHKNIISLLNVFTPQK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 ML------YMVFEFMDgADLCFEIVKRADagfvysEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVK 165
Cdd:cd07876    94 SLeefqdvYLVMELMD-ANLCQVIHMELD------HERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS---DCTLK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 166 LGGFGVAiQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE--------------- 230
Cdd:cd07876   164 ILDFGLA-RTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHidqwnkvieqlgtps 242
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796143 231 -----RLFEGIikGKYKMNPRQ------------WSHISES---------AKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd07876   243 aefmnRLQPTV--RNYVENRPQypgisfeelfpdWIFPSESerdklktsqARDLLSKMLVIDPDKRISVDEALRHPYI 318
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
7-282 2.23e-18

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: 85.96  E-value: 2.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   7 LFEDVYElcevIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTEgkRWISNLKrEASICHMLKHPHIVELLET 86
Cdd:cd06607     2 IFEDLRE----IGHGSFGAVYYARNKRTSEVVAIK-----KMSYSGKQSTE--KWQDIIK-EVKFLRQLRHPNTIEYKGC 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYMVFEFMDG--ADLcFEIVKRAdagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPV 164
Cdd:cd06607    70 YLREHTAWLVMEYCLGsaSDI-VEVHKKP-----LQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTE---PGTV 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 165 KLGGFGVAiqlgesGLV--AGGRVGTPHFMAPEVV---KREPYGKPVDVWGCGVIlfillsgCLPFYGTKERLFegiikg 239
Cdd:cd06607   141 KLADFGSA------SLVcpANSFVGTPYWMAPEVIlamDEGQYDGKVDVWSLGIT-------CIELAERKPPLF------ 201
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 240 kyKMNPR--------------QWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd06607   202 --NMNAMsalyhiaqndsptlSSGEWSDDFRNFVDSCLQKIPQDRPSAEDLLKHPFV 256
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
18-282 2.27e-18

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: 86.60  E-value: 2.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTegkrwisnlkREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd07871    13 LGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAI----------REVSLLKNLKHANIVTLHDIIHTERCLTLVF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDgADLCFEIvkrADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGFGVAIQLGE 177
Cdd:cd07871    83 EYLD-SDLKQYL---DNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEK---GELKLADFGLARAKSV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 SGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGT--KERL---------------------- 232
Cdd:cd07871   156 PTKTYSNEVVTLWYRPPDVlLGSTEYSTPIDMWGVGCILYEMATGRPMFPGStvKEELhlifrllgtpteetwpgvtsne 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039796143 233 -FEGIIKGKYKMNP--RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd07871   236 eFRSYLFPQYRAQPliNHAPRLDTDGIDLLSSLLLYETKSRISAEAALRHSYF 288
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
12-261 3.08e-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: 87.79  E-value: 3.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglstegKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd05628     3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLE--------KEQVGHIRAERDILVEADSLWVVKMFYSFQDKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd05628    75 NLYLIMEFLPGGDMMTLLMKKD----TLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGH---VKLSDFGL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESG-----------------------------------LVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILF 216
Cdd:cd05628   148 CTGLKKAHrtefyrnlnhslpsdftfqnmnskrkaetwkrnrrQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMY 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039796143 217 ILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISESAKDLVRR 261
Cdd:cd05628   228 EMLIGYPPFCSeTPQETYKKVMNWKETLIFPPEVPISEKAKDLILR 273
SH3_MPP5 cd12036
Src Homology 3 domain of Membrane Protein, Palmitoylated 5 (or MAGUK p55 subfamily member 5); ...
599-659 3.81e-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: 3.81e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039796143 599 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQG--KLENSKNGTAGLIPSPE 659
Cdd:cd12036     1 HVRAHFDYDPEDDPYIPCRELGLSFQKGDILHVISQEDPNWWQAyrEGEEDNQSLAGLIPSKS 63
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
17-227 3.85e-18

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: 85.47  E-value: 3.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRetGQQFAVKIVdvakfTSSPglSTEGKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYMV 96
Cdd:cd14146     1 IIGVGGFGKVYRATWK--GQEVAVKAA-----RQDP--DEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMDGADLcfeivKRADAGFVYSEA----------VASHYMRQILEALRYCHDNN---IIHRDVKPHCVLLASK-EN-- 160
Cdd:cd14146    72 MEFARGGTL-----NRALAAANAAPGprrarripphILVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLLEKiEHdd 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 161 --SAPVKLGGFGVAIQLGESGLVAGGrvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 227
Cdd:cd14146   147 icNKTLKITDFGLAREWHRTTKMSAA--GTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRG 213
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
18-215 3.87e-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: 85.22  E-value: 3.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIvdvAKFTSSPGlstegkrwisNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKM---NTLSSNRA----------NMLREVQLMNRLSHPNILRFMGVCVHQGQLHALT 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLcfeiVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVA--IQL 175
Cdd:cd14155    68 EYINGGNL----EQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVVGDFGLAekIPD 143
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1039796143 176 GESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVIL 215
Cdd:cd14155   144 YSDGKEKLAVVGSPYWMAPEVLRGEPYNEKADVFSYGIIL 183
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
18-280 4.64e-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: 85.20  E-value: 4.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDvakftSSPGLSTEGKrwisNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLH-----SSPNCIEERK----ALLKEAEKMERARHSYVLPLLGVCVERRSLGLVM 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLcFEIVKRADAGFVYSeaVASHYMRQILEALRYCH--DNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQL 175
Cdd:cd13978    72 EYMENGSL-KSLLEREIQDVPWS--LRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILL---DNHFHVKISDFGLSKLG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GESGLVAGGRV-----GTPHFMAPEVVkREPYGKPV---DVWGCGVILFILLSGCLPFYGTKERL--FEGIIKGKYKM-- 243
Cdd:cd13978   146 MKSISANRRRGtenlgGTPIYMAPEAF-DDFNKKPTsksDVYSFAIVIWAVLTRKEPFENAINPLliMQIVSKGDRPSld 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039796143 244 ---NPRQWSHISEsAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd13978   225 digRLKQIENVQE-LISLMIRCWDGNPDARPTFLECLDRL 263
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
10-305 4.81e-18

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: 86.54  E-value: 4.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKivDVAKFTSSPGLSTEGKRWISNLKreasicHMlKHPHIVELLETYSS 89
Cdd:cd07880    15 DRYRDLKQVGSGAYGTVCSALDRRTGAKVAIK--KLYRPFQSELFAKRAYRELRLLK------HM-KHENVIGLLDVFTP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGML------YMVFEFMdGADLCfEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCvlLASKENsAP 163
Cdd:cd07880    86 DLSLdrfhdfYLVMPFM-GTDLG-KLMKHEK----LSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGN--LAVNED-CE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 164 VKLGGFGVAIQlGESGLVagGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFE------ 234
Cdd:cd07880   157 LKILDFGLARQ-TDSEMT--GYVVTRWYRAPEVIlNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDhlDQLMEimkvtg 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 235 ----------------GIIKGKYKMNPRQWSHI----SESAKDLVRRMLMLDPAERITVYEALNHPWLKErdryaykIHL 294
Cdd:cd07880   234 tpskefvqklqsedakNYVKKLPRFRKKDFRSLlpnaNPLAVNVLEKMLVLDAESRITAAEALAHPYFEE-------FHD 306
                         330
                  ....*....|.
gi 1039796143 295 PETVEQLRKFN 305
Cdd:cd07880   307 PEDETEAPPYD 317
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
8-282 6.32e-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: 86.22  E-value: 6.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELCEVIGKGPFSVVRRCINRETGQ-QFAVKIV-DVAKFTSSPGLSTEGKRWISNLKRE-ASICHMLKhphivell 84
Cdd:cd14214    11 LQERYEIVGDLGEGTFGKVVECLDHARGKsQVALKIIrNVGKYREAARLEINVLKKIKEKDKEnKFLCVLMS-------- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  85 ETYSSDGMLYMVFEFMDGAdlCFEIVKRADagFV-YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE---- 159
Cdd:cd14214    83 DWFNFHGHMCIAFELLGKN--TFEFLKENN--FQpYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVNSEfdtl 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 160 ------------NSAPVKLGGFGVAIQLGESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 227
Cdd:cd14214   159 ynesksceeksvKNTSIRVADFGSATFDHEHHTTI---VATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 228 TKER----LFEGII------------KGKY--------KMNPRQWSHISESAK-----------------DLVRRMLMLD 266
Cdd:cd14214   236 HENRehlvMMEKILgpipshmihrtrKQKYfykgslvwDENSSDGRYVSENCKplmsymlgdslehtqlfDLLRRMLEFD 315
                         330
                  ....*....|....*.
gi 1039796143 267 PAERITVYEALNHPWL 282
Cdd:cd14214   316 PALRITLKEALLHPFF 331
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
17-278 7.63e-18

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


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 84.69  E-value: 7.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKivdVAKFTSSPGLStEGKRWISNLKReasIChmlKHPHIVELL--ETYSSDGML- 93
Cdd:cd13985     7 QLGEGGFSYVYLAHDVNTGRRYALK---RMYFNDEEQLR-VAIKEIEIMKR---LC---GHPNIVQYYdsAILSSEGRKe 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  94 -YMVFEFMDGAdLCFEIVKRADAGFvySEAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLASKENsapVKLGGFG 170
Cdd:cd13985    77 vLLLMEYCPGS-LVDILEKSPPSPL--SEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGR---FKLCDFG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 171 VA------------IQLGESGLvagGRVGTPHFMAPEVV---KREPYGKPVDVWGCGVILFILLSGCLPFygtKERLFEG 235
Cdd:cd13985   151 SAttehypleraeeVNIIEEEI---QKNTTPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPF---DESSKLA 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039796143 236 IIKGKYKM--NPRQwshiSESAKDLVRRMLMLDPAERITVYEALN 278
Cdd:cd13985   225 IVAGKYSIpeQPRY----SPELHDLIRHMLTPDPAERPDIFQVIN 265
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
59-286 8.26e-18

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 85.80  E-value: 8.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  59 KRWISNLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYC 138
Cdd:PTZ00426   72 QKQVDHVFSERKILNYINHPFCVNLYGSFKDESYLYLVLEFVIGGEF-FTFLRRNKR---FPNDVGCFYAAQIVLIFEYL 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 139 HDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFIL 218
Cdd:PTZ00426  148 QSLNIVYRDLKPENLLL---DKDGFIKMTDFGFAKVVDTRTYTL---CGTPEYIAPEILLNVGHGKAADWWTLGIFIYEI 221
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796143 219 LSGCLPFYGTK-----ERLFEGIIkgkykMNPRqwsHISESAKDLVRRMLMLDPAERI-----TVYEALNHPWLKERD 286
Cdd:PTZ00426  222 LVGCPPFYANEplliyQKILEGII-----YFPK---FLDNNCKHLMKKLLSHDLTKRYgnlkkGAQNVKEHPWFGNID 291
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
12-282 8.27e-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: 85.11  E-value: 8.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKftssPGLSTEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14040     8 YLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNK----SWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLY-MVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLASKENSAPVKLGG 168
Cdd:cd14040    84 DTFcTVLEYCEGNDLDFYLKQHK----LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESGLVAGGR------VGTPHFMAPE--VVKREP--YGKPVDVWGCGVILFILLSGCLPF---YGTKERLFEG 235
Cdd:cd14040   160 FGLSKIMDDDSYGVDGMdltsqgAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFghnQSQQDILQEN 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1039796143 236 IIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14040   240 TILKATEVQFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
18-262 1.05e-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: 83.64  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRetGQQFAVKIVDVakftsspglSTEGKRWISNLKREASICHmlkhPHIVELLETYSSDGMLYMVF 97
Cdd:cd14058     1 VGRGSFGVVCKARWR--NQIVAVKIIES---------ESEKKAFEVEVRQLSRVDH----PNIIKLYGACSNQKPVCLVM 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLcFEIVKRADAGFVYSEAVASHYMRQILEALRYCH---DNNIIHRDVKPHCVLLASKENSapVKLGGFGVAIQ 174
Cdd:cd14058    66 EYAEGGSL-YNVLHGKEPKPIYTAAHAMSWALQCAKGVAYLHsmkPKALIHRDLKPPNLLLTNGGTV--LKICDFGTACD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 175 LgeSGLVAGGRvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF---------------YGTKERLFEGIIKG 239
Cdd:cd14058   143 I--STHMTNNK-GSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFdhiggpafrimwavhNGERPPLIKNCPKP 219
                         250       260
                  ....*....|....*....|....*.
gi 1039796143 240 KYKMNPRQWSHISE---SAKDLVRRM 262
Cdd:cd14058   220 IESLMTRCWSKDPEkrpSMKEIVKIM 245
PDZ_MPP5-like cd06798
PDZ domain of membrane palmitoylated protein 5 (MPP5), Drosophila Stardust, and related ...
495-575 1.61e-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: 1.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 495 RLVQFQKnTDEPMGITLKmNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIV 574
Cdd:cd06798     1 KIVRIEK-TREPLGATVR-NEGDSVIISRIVKGGAAEKSGLLHEGDEILEINGIEIRGKDVNEVCDLLADMHGTLTFLLI 78

                  .
gi 1039796143 575 P 575
Cdd:cd06798    79 P 79
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
17-225 1.82e-17

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: 83.11  E-value: 1.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRetGQQFAVKIVDVAKfTSSPGLSTEgkrwisNLKREASICHMLKHPHIVELLETYSSDGMLYMV 96
Cdd:cd14148     1 IIGVGGFGKVYKGLWR--GEEVAVKAARQDP-DEDIAVTAE------NVRQEARLFWMLQHPNIIALRGVCLNPPHLCLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMDGADLcfeivKRADAGFVYSEAVASHYMRQILEALRYCHDNN---IIHRDVKPHCVLLASK-EN----SAPVKLGG 168
Cdd:cd14148    72 MEYARGGAL-----NRALAGKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEPiENddlsGKTLKITD 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 169 FGVAIQLGESGLVAGGrvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF 225
Cdd:cd14148   147 FGLAREWHKTTKMSAA--GTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
SH3_MPP3 cd12039
Src Homology 3 domain of Membrane Protein, Palmitoylated 3 (or MAGUK p55 subfamily member 3); ...
599-657 2.08e-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: 2.08e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 599 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPS 657
Cdd:cd12039     1 FMRALFDYNPYEDRAIPCQEAGLPFKRRDILEVVSQDDPTWWQAKRVGDTNLRAGLIPS 59
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
10-284 2.76e-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: 84.32  E-value: 2.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftSSPGLST-EGKRwisnLKREASICHMLKHPHIVELLETYS 88
Cdd:cd07877    17 ERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKL------SRPFQSIiHAKR----TYRELRLLKHMKHENVIGLLDVFT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGML------YMVFEFMdGADLCfEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCvlLASKENsA 162
Cdd:cd07877    87 PARSLeefndvYLVTHLM-GADLN-NIVKCQK----LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSN--LAVNED-C 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 163 PVKLGGFGVAIQLGESglvAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE----------- 230
Cdd:cd07877   158 ELKILDFGLARHTDDE---MTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHidqlklilrlv 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796143 231 -----RLFEGI--------IKGKYKMNPRQWSHI----SESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd07877   235 gtpgaELLKKIssesarnyIQSLTQMPKMNFANVfigaNPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQ 305
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
9-283 2.95e-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: 83.18  E-value: 2.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEvIGKGPFSVVRRCINRETGQQFAVKIVdvakftSSPGLSTEGKRWISNLK--REASIChmlkhPHIVELLET 86
Cdd:cd06616     6 EDLKDLGE-IGRGAFGTVNKMLHKPSGTIMAVKRI------RSTVDEKEQKRLLMDLDvvMRSSDC-----PYIVKFYGA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYMVFEFMDGA-DLCFEIVKRADAGfVYSEAVASHYMRQILEALRYCHDN-NIIHRDVKPHCVLLASKENsapV 164
Cdd:cd06616    74 LFREGDCWICMELMDISlDKFYKYVYEVLDS-VIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGN---I 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 165 KLGGFGVAIQLGESglVAGGR-VGTPHFMAPEVV----KREPYGKPVDVWGCGVILFILLSGCLPFYGTKErLFEGI--- 236
Cdd:cd06616   150 KLCDFGISGQLVDS--IAKTRdAGCRPYMAPERIdpsaSRDGYDVRSDVWSLGITLYEVATGKFPYPKWNS-VFDQLtqv 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039796143 237 IKGKY-KMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLK 283
Cdd:cd06616   227 VKGDPpILSNSEEREFSPSFVNFVNLCLIKDESKRPKYKELLKHPFIK 274
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
14-227 3.16e-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: 82.77  E-value: 3.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  14 LCEVIGKGPFSVVRRCINRetGQQFAVKivdVAKFTSSPGLSTEGKrwisNLKREASICHMLKHPHIVELLETYSSDGML 93
Cdd:cd14147     7 LEEVIGIGGFGKVYRGSWR--GELVAVK---AARQDPDEDISVTAE----SVRQEARLFAMLAHPNIIALKAVCLEEPNL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  94 YMVFEFMDGADLcfeivKRADAGFVYSEAVASHYMRQILEALRYCHDNNI---IHRDVKPHCVLLASK-ENSA----PVK 165
Cdd:cd14147    78 CLVMEYAAGGPL-----SRALAGRRVPPHVLVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLLQPiENDDmehkTLK 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 166 LGGFGVAIQLGESGLVAGGrvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 227
Cdd:cd14147   153 ITDFGLAREWHKTTQMSAA--GTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRG 212
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
496-573 3.17e-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: 3.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 496 LVQFQKNTDEPMGITLKMNELNH---CIVARIMHGGMIHRQGtLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFK 572
Cdd:pfam00595   1 QVTLEKDGRGGLGFSLKGGSDQGdpgIFVSEVLPGGAAEAGG-LKVGDRILSINGQDVENMTHEEAVLALKGSGGKVTLT 79

                  .
gi 1039796143 573 I 573
Cdd:pfam00595  80 I 80
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
18-282 3.61e-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: 83.78  E-value: 3.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKivDVAKFTSSPGLStegKRwisnLKREASICHMLKHPHIVELLETYSSDGM-LYMV 96
Cdd:cd07856    18 VGMGAFGLVCSARDQLTGQNVAVK--KIMKPFSTPVLA---KR----TYRELKLLKHLRHENIISLSDIFISPLEdIYFV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMdGADLCFEIVKRAdagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLasKENsAPVKLGGFGVAiQLG 176
Cdd:cd07856    89 TELL-GTDLHRLLTSRP-----LEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILV--NEN-CDLKICDFGLA-RIQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 177 ESGLVagGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGcLPFYGTKERLFEGIIKGKYKMNP---------- 245
Cdd:cd07856   159 DPQMT--GYVSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEG-KPLFPGKDHVNQFSIITELLGTPpddvintics 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796143 246 ------------RQWSHISE-------SAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd07856   236 entlrfvqslpkRERVPFSEkfknadpDAIDLLEKMLVFDPKKRISAAEALAHPYL 291
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
18-215 3.61e-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: 3.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIvdvakftsspglsTEGKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKI-------------YKNDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPIL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLCfEIVKRADAGFVYSEAVAshYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGE 177
Cdd:cd14156    68 EYVSGGCLE-ELLAREELPLSWREKVE--LACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAVVTDFGLAREVGE 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1039796143 178 SGLVAGGR----VGTPHFMAPEVVKREPYGKPVDVWGCGVIL 215
Cdd:cd14156   145 MPANDPERklslVGSAFWMAPEMLRGEPYDRKVDVFSFGIVL 186
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1-286 7.08e-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: 82.80  E-value: 7.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   1 MADDDvlFEDVYELceviGKGPFSVVRRCINRETGQQFAVKIVDVakftsspglstEGKRWISN-LKREASICHMLKHPH 79
Cdd:cd06650     2 LKDDD--FEKISEL----GAGNGGVVFKVSHKPSGLVMARKLIHL-----------EIKPAIRNqIIRELQVLHECNSPY 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  80 IVELLETYSSDGMLYMVFEFMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHD-NNIIHRDVKPHCVLLASK 158
Cdd:cd06650    65 IVGFYGAFYSDGEISICMEHMDGGSLD-QVLKKAGR---IPEQILGKVSIAVIKGLTYLREkHKIMHRDVKPSNILVNSR 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 159 ensAPVKLGGFGVAIQLGESglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF----YGTKERLFE 234
Cdd:cd06650   141 ---GEIKLCDFGVSGQLIDS--MANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIpppdAKELELMFG 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 235 GIIKG-----------------KYKMNPRQWSHISE--------------------SAKDLVRRMLMLDPAERITVYEAL 277
Cdd:cd06650   216 CQVEGdaaetpprprtpgrplsSYGMDSRPPMAIFElldyivnepppklpsgvfslEFQDFVNKCLIKNPAERADLKQLM 295

                  ....*....
gi 1039796143 278 NHPWLKERD 286
Cdd:cd06650   296 VHAFIKRSD 304
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
12-282 7.17e-17

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: 83.64  E-value: 7.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAK-FTSSpglSTEGKRWISNLKREASICHMlkhpHIVELLETYSSD 90
Cdd:cd14224    67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKrFHRQ---AAEEIRILEHLKKQDKDNTM----NVIHMLESFTFR 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMDgADLcFEIVKRAD-AGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSApVKLGGF 169
Cdd:cd14224   140 NHICMTFELLS-MNL-YELIKKNKfQGF--SLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSG-IKVIDF 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GvaiqlgeSGLVAGGRVGT----PHFMAPEVVKREPYGKPVDVWGCGVILFILLSG--------------CL-------- 223
Cdd:cd14224   215 G-------SSCYEHQRIYTyiqsRFYRAPEVILGARYGMPIDMWSFGCILAELLTGyplfpgedegdqlaCMiellgmpp 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 224 -------------------PFYGTKERLFEGII--------KGKYKMNP--RQWSHISESAKD-----LVRRMLMLDPAE 269
Cdd:cd14224   288 qklletskraknfisskgyPRYCTVTTLPDGSVvlnggrsrRGKMRGPPgsKDWVTALKGCDDplfldFLKRCLEWDPAA 367
                         330
                  ....*....|...
gi 1039796143 270 RITVYEALNHPWL 282
Cdd:cd14224   368 RMTPSQALRHPWL 380
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
7-282 8.61e-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: 82.24  E-value: 8.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   7 LFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAK-FTSSpglsteGKRWISNLK--REASICHMLKHpHIVEL 83
Cdd:cd14136     7 VYNGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQhYTEA------ALDEIKLLKcvREADPKDPGRE-HVVQL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  84 LETYSSDGM----LYMVFEFMdGADLCFEIvKRADAGFVYSEAVAShYMRQILEALRYCHDN-NIIHRDVKPHCVLLASK 158
Cdd:cd14136    80 LDDFKHTGPngthVCMVFEVL-GPNLLKLI-KRYNYRGIPLPLVKK-IARQVLQGLDYLHTKcGIIHTDIKPENVLLCIS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 159 EnsAPVKLGGFGVA----------IQlgesglvaggrvgTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY-- 226
Cdd:cd14136   157 K--IEVKIADLGNAcwtdkhftedIQ-------------TRQYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFDph 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 227 -----------------------------GTKERLF------------------EGIIKGKYKMNPRQWSHISesakDLV 259
Cdd:cd14136   222 sgedysrdedhlaliiellgriprsiilsGKYSREFfnrkgelrhisklkpwplEDVLVEKYKWSKEEAKEFA----SFL 297
                         330       340
                  ....*....|....*....|...
gi 1039796143 260 RRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14136   298 LPMLEYDPEKRATAAQCLQHPWL 320
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
8-282 9.51e-17

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: 82.03  E-value: 9.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglsTEGKRWISNLKREASICHMLKHPHIVELLETY 87
Cdd:cd14041     4 LNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRD----EKKENYHKHACREYRIHKELDHPRIVKLYDYF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLY-MVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLASKENSAPV 164
Cdd:cd14041    80 SLDTDSFcTVLEYCEGNDLDFYLKQHK----LMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTACGEI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 165 KLGGFGVAIQLGES--GLVAGGRV-----GTPHFMAPE--VVKREP--YGKPVDVWGCGVILFILLSGCLPF---YGTKE 230
Cdd:cd14041   156 KITDFGLSKIMDDDsyNSVDGMELtsqgaGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFYQCLYGRKPFghnQSQQD 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 231 RLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14041   236 ILQENTILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
18-284 1.04e-16

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: 81.31  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEGKRWisnlKREASICHMLKHPHIVELLETYSS----DGML 93
Cdd:cd14031    18 LGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKA-----EQQRF----KEEAEMLKGLQHPNIVRFYDSWESvlkgKKCI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  94 YMVFEFMDGADLCfEIVKRADagfVYSEAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLASKENSapVKLGGFGV 171
Cdd:cd14031    89 VLVTELMTSGTLK-TYLKRFK---VMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTGS--VKIGDLGL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESglVAGGRVGTPHFMAPEVVKrEPYGKPVDVWGCGVILFILLSGCLPFYGTKE--RLFEGIIKGkykMNPRQWS 249
Cdd:cd14031   163 ATLMRTS--FAKSVIGTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPYSECQNaaQIYRKVTSG---IKPASFN 236
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039796143 250 HISE-SAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd14031   237 KVTDpEVKEIIEGCIRQNKSERLSIKDLLNHAFFAE 272
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
12-279 1.47e-16

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: 81.19  E-value: 1.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAkftsspglSTEGkrwISNLKREASICHMLKHPHIVELLET---YS 88
Cdd:cd13986     2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCH--------SKED---VKEAMREIENYRLFNHPNILRLLDSqivKE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDG--MLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNII---HRDVKPHCVLLAskENSAP 163
Cdd:cd13986    71 AGGkkEVYLLLPYYKRGSLQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLS--EDDEP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 164 VkLGGFGVAIQlgeSGLVAGGRV------------GTPHFMAPEVVKREPYG---KPVDVWGCGVILFILLSGCLPF--- 225
Cdd:cd13986   149 I-LMDLGSMNP---ARIEIEGRRealalqdwaaehCTMPYRAPELFDVKSHCtidEKTDIWSLGCTLYALMYGESPFeri 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 226 YGTKERLFEGIIKGKYKMnPRQwSHISESAKDLVRRMLMLDPAERITVYEALNH 279
Cdd:cd13986   225 FQKGDSLALAVLSGNYSF-PDN-SRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
9-286 1.53e-16

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


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 81.08  E-value: 1.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELcEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsspGLSTEGKRWISNlkrEASICHMLKHPHIVELLETYS 88
Cdd:cd06619     1 QDIQYQ-EILGHGNGGTVYKAYHLLTRRILAVKVIPL-------DITVELQKQIMS---ELEILYKCDSPYIIGFYGAFF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLcfEIVKRADAGFVYSEAVAshymrqILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGG 168
Cdd:cd06619    70 VENRISICTEFMDGGSL--DVYRKIPEHVLGRIAVA------VVKGLTYLWSLKILHRDVKPSNMLVNTR---GQVKLCD 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQLGESglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE--------RLFEGIIKGK 240
Cdd:cd06619   139 FGVSTQLVNS--IAKTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKnqgslmplQLLQCIVDED 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039796143 241 YKMNPRqwSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERD 286
Cdd:cd06619   217 PPVLPV--GQFSEKFVHFITQCMRKQPKERPAPENLMDHPFIVQYN 260
gmk PRK14737
guanylate kinase; Provisional
718-895 1.78e-16

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 78.50  E-value: 1.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 718 KTLVLLGAHGVGRRHIKNTLITKHPDrFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTK 797
Cdd:PRK14737    5 KLFIISSVAGGGKSTIIQALLEEHPD-FLFSISCTTRAPRPGDEEGKTYFFLTIEEFKKGIADGEFLEWAEVHDNYYGTP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 798 LETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFV-VFIAAPT--------ITPGLNEDES-LQRLQKESDVLQRtyAHY 867
Cdd:PRK14737   84 KAFIEDAFKEGRSAIMDIDVQGAKIIKEKFPERIVtIFIEPPSeeeweerlIHRGTDSEESiEKRIENGIIELDE--ANE 161
                         170       180
                  ....*....|....*....|....*...
gi 1039796143 868 FDLTIINNEIDETIRHLEeavELVCTAP 895
Cdd:PRK14737  162 FDYKIINDDLEDAIADLE---AIICGKK 186
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
10-298 1.82e-16

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: 81.19  E-value: 1.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTegkrwisnlkREASICHMLKHPHIVELLETYSS 89
Cdd:cd07872     6 ETYIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAI----------REVSLLKDLKHANIVTLHDIVHT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDgADLCFEIvkrADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGF 169
Cdd:cd07872    76 DKSLTLVFEYLD-KDLKQYM---DDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINER---GELKLADF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGT----------------KERL 232
Cdd:cd07872   149 GLARAKSVPTKTYSNEVVTLWYRPPDVlLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGStvedelhlifrllgtpTEET 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796143 233 FEGIIKG---------KYKMNP--RQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKErdrYAYKIH-LPETV 298
Cdd:cd07872   229 WPGISSNdefknynfpKYKPQPliNHAPRLDTEGIELLTKFLQYESKKRISAEEAMKHAYFRS---LGTRIHsLPESI 303
SH3_MPP6 cd12038
Src Homology 3 domain of Membrane Protein, Palmitoylated 6 (or MAGUK p55 subfamily member 6); ...
599-657 2.26e-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: 2.26e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 599 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKlENSKNGTAGLIPS 657
Cdd:cd12038     1 FVKCHFDYNPYNDNLIPCKEAGLKFSKGEILQIVNREDPNWWQAS-HVKEGGSAGLIPS 58
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
9-284 2.61e-16

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


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 80.09  E-value: 2.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsSPGLStegkrwISNLKREASICHMLKHPHIVELLETYS 88
Cdd:cd06645    10 QEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKL-----EPGED------FAVVQQEIIMMKDCKHSNIVAYFGSYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLcfeivkrADAGFV---YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVK 165
Cdd:cd06645    79 RRDKLWICMEFCGGGSL-------QDIYHVtgpLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLT---DNGHVK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 166 LGGFGVAIQLGESGLVAGGRVGTPHFMAPEVV---KREPYGKPVDVWGCGVILFILLSGCLP----------FYGTKERL 232
Cdd:cd06645   149 LADFGVSAQITATIAKRKSFIGTPYWMAPEVAaveRKGGYNQLCDIWAVGITAIELAELQPPmfdlhpmralFLMTKSNF 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 233 FEGIIKGKYKmnprqWSHiseSAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd06645   229 QPPKLKDKMK-----WSN---SFHHFVKMALTKNPKKRPTAEKLLQHPFVTQ 272
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
18-277 3.07e-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: 3.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTsspglstegKRWISNLKREASICHMLKHPHIVELlETYSSDGMLYMVF 97
Cdd:cd14049    14 LGKGGYGKVYKVRNKLDGQYYAIKKILIKKVT---------KRDCMKVLREVKVLAGLQHPNIVGY-HTAWMEHVQLMLY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADL-------------CFEIVKRADAGFVYSEaVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapV 164
Cdd:cd14049    84 IQMQLCELslwdwivernkrpCEEEFKSAPYTPVDVD-VTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDIH--V 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 165 KLGGFGVAIQL------------GESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSgclPFYGTKER- 231
Cdd:cd14049   161 RIGDFGLACPDilqdgndsttmsRLNGLTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELFQ---PFGTEMERa 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039796143 232 -LFEGIIKGKYKMN-PRQWSHISESAKDLVRRmlmlDPAERITVYEAL 277
Cdd:cd14049   238 eVLTQLRNGQIPKSlCKRWPVQAKYIKLLTST----EPSERPSASQLL 281
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
8-283 3.98e-16

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: 80.59  E-value: 3.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELceviGKGPFSVVRRCINRETGQQFAVKIVDVAKftsspglstegKRWISNLKREASICHMLKHPHIVELLETY 87
Cdd:cd07854     7 YMDLRPL----GCGSNGLVFSAVDSDCDKRVAVKKIVLTD-----------PQSVKHALREIKIIRRLDHDNIVKVYEVL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDG--------------MLYMVFEFMDgADLCFEIVKRAdagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCV 153
Cdd:cd07854    72 GPSGsdltedvgsltelnSVYIVQEYME-TDLANVLEQGP-----LSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANV 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 154 LLASKEnsAPVKLGGFGVAIQL----GESGLVAGGRVgTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGT 228
Cdd:cd07854   146 FINTED--LVLKIGDFGLARIVdphySHKGYLSEGLV-TKWYRSPRLLlSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGA 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 229 KE-RLFEGIIK---------------------GKYKMNPRQ-----WSHISESAKDLVRRMLMLDPAERITVYEALNHPW 281
Cdd:cd07854   223 HElEQMQLILEsvpvvreedrnellnvipsfvRNDGGEPRRplrdlLPGVNPEALDFLEQILTFNPMDRLTAEEALMHPY 302

                  ..
gi 1039796143 282 LK 283
Cdd:cd07854   303 MS 304
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
67-225 4.57e-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: 78.69  E-value: 4.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  67 REASICHM--LKHPHIVELLETYSSDGMLYMVFEFMDGADLcFEIVKradAGFVYSEAVASHYMRQILEALRYCHDNNII 144
Cdd:cd14059    28 KETDIKHLrkLNHPNIIKFKGVCTQAPCYCILMEYCPYGQL-YEVLR---AGREITPSLLVDWSKQIASGMNYLHLHKII 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 145 HRDVKPHCVLLASKENsapVKLGGFGVAIQLGESGlVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLP 224
Cdd:cd14059   104 HRDLKSPNVLVTYNDV---LKISDFGTSKELSEKS-TKMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIP 179

                  .
gi 1039796143 225 F 225
Cdd:cd14059   180 Y 180
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
10-284 6.94e-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: 79.28  E-value: 6.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTegkrwisnlkREASICHMLKHPHIVELLETYSS 89
Cdd:cd07873     2 ETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTAI----------REVSLLKDLKHANIVTLHDIIHT 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDgADLCFEIvkrADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKensAPVKLGGF 169
Cdd:cd07873    72 EKSLTLVFEYLD-KDLKQYL---DDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINER---GELKLADF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGT----------------KERL 232
Cdd:cd07873   145 GLARAKSIPTKTYSNEVVTLWYRPPDIlLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGStveeqlhfifrilgtpTEET 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 233 FEGIIKG---------KYKMNPRQwSH---ISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd07873   225 WPGILSNeefksynypKYRADALH-NHaprLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFHS 287
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
12-275 7.49e-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: 7.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVD----------VAKFTSSPGLSTEGKRWIS----NLKREASICHMLKH 77
Cdd:cd13977     2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRcnapenvelaLREFWALSSIQRQHPNVIQleecVLQRDGLAQRMSHG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  78 PHI----VELLET---------YSSDGMLYMVFEFMDGADLCFEIVKRADagfvySEAVASHYMRQILEALRYCHDNNII 144
Cdd:cd13977    82 SSKsdlyLLLVETslkgercfdPRSACYLWFVMEFCDGGDMNEYLLSRRP-----DRQTNTSFMLQLSSALAFLHRNQIV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 145 HRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGRV-----------GTPHFMAPEVVKREpYGKPVDVWGCGV 213
Cdd:cd13977   157 HRDLKPDNILISHKRGEPILKVADFGLSKVCSGSGLNPEEPAnvnkhflssacGSDFYMAPEVWEGH-YTAKADIFALGI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 214 ILFILLSGCLPFYG-TKERLFEGIIKGKYKM---------NPRQWSHI--------SESAKDLVRRMLMLDPAERITVYE 275
Cdd:cd13977   236 IIWAMVERITFRDGeTKKELLGTYIQQGKEIvplgealleNPKLELQIplkkkksmNDDMKQLLRDMLAANPQERPDAFQ 315
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
18-286 7.60e-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: 80.46  E-value: 7.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIvdvakFTSSPGLSTEGKRWISNlkrEASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd05600    19 VGQGGYGSVFLARKKDTGEICALKI-----MKKKVLFKLNEVNHVLT---ERDILTTTNSPWLVKLLYAFQDPENVYLAM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLcfeivkRA---DAGfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVA-- 172
Cdd:cd05600    91 EYVPGGDF------RTllnNSG-ILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDS---SGHIKLTDFGLAsg 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 173 -----------IQLGESGLVAGGR------------------------VGTPHFMAPEVVKREPYGKPVDVWGCGVILFI 217
Cdd:cd05600   161 tlspkkiesmkIRLEEVKNTAFLEltakerrniyramrkedqnyansvVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFE 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 218 LLSGCLPFYG-TKERLFEGIIKGKYKM------NPRQWSHISESAKDLVRRMLMlDPAERITVYEAL-NHPWLKERD 286
Cdd:cd05600   241 CLVGFPPFSGsTPNETWANLYHWKKTLqrpvytDPDLEFNLSDEAWDLITKLIT-DPQDRLQSPEQIkNHPFFKNID 316
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
18-284 7.61e-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: 7.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVdvakftSSPGLSTEGKRwisNLKREASICHMLKHPHIVELLETYSSDGML---- 93
Cdd:cd07878    23 VGSGAYGSVCSAYDTRLRQKVAVKKL------SRPFQSLIHAR---RTYRELRLLKHMKHENVIGLLDVFTPATSIenfn 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  94 --YMVFEFMdGADLCfEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVllASKENsAPVKLGGFGV 171
Cdd:cd07878    94 evYLVTNLM-GADLN-NIVKCQK----LSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNV--AVNED-CELRILDFGL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESglvAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYGTK-----ERLFEGI--------- 236
Cdd:cd07878   165 ARQADDE---MTGYVATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDyidqlKRIMEVVgtpspevlk 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 237 ----------IKGKYKMNPRQWSHISESAK----DLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd07878   242 kisseharkyIQSLPHMPQQDLKKIFRGANplaiDLLEKMLVLDSDKRISASEALAHPYFSQ 303
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
12-213 9.34e-16

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: 78.53  E-value: 9.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVakftsSPGLStegkrwISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd06646    11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIKL-----EPGDD------FSLIQQEIFMVKECKHCNIVAYFGSYLSRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcfeivkrADAGFV---YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGG 168
Cdd:cd06646    80 KLWICMEYCGGGSL-------QDIYHVtgpLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLT---DNGDVKLAD 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039796143 169 FGVAIQLGESGLVAGGRVGTPHFMAPEVVKREP---YGKPVDVWGCGV 213
Cdd:cd06646   150 FGVAAKITATIAKRKSFIGTPYWMAPEVAAVEKnggYNQLCDIWAVGI 197
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
14-273 1.53e-15

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: 77.89  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  14 LCEVIGKGPFSVVRR--CINRETGQQFAVKIVDVAKFTSSPGLStegkrwiSNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd05049     9 LKRELGEGAFGKVFLgeCYNLEPEQDKMLVAVKTLKDASSPDAR-------KDFEREAELLTNLQHENIVKFYGVCTEGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCfEIVKR--ADAGFVYSEAVAS---------HYMRQILEALRYCHDNNIIHRDVKPHCVLLASKen 160
Cdd:cd05049    82 PLLMVFEYMEHGDLN-KFLRShgPDAAFLASEDSAPgeltlsqllHIAVQIASGMVYLASQHFVHRDLATRNCLVGTN-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 161 sAPVKLGGFGVA--IQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYG-TKERLFEGI 236
Cdd:cd05049   159 -LVVKIGDFGMSrdIYSTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWeIFTYGKQPWFQlSNTEVIECI 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1039796143 237 IKGKYKMNPRqwshiseSAKDLVRRmLML-----DPAERITV 273
Cdd:cd05049   238 TQGRLLQRPR-------TCPSEVYA-VMLgcwkrEPQQRLNI 271
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
18-225 2.12e-15

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: 77.65  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAkftsspgLSTEGK-RWIsnlkREASICHMLKHPHIVELLET-----YSSDG 91
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKSCRLE-------LSVKNKdRWC----HEIQIMKKLNHPNVVKACDVpeemnFLVND 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGV 171
Cdd:cd14039    70 VPLLAMEYCSGGDL-RKLLNKPENCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVHKIIDLGY 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 172 AIQLgESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF 225
Cdd:cd14039   149 AKDL-DQGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
SH3_MPP4 cd12034
Src Homology 3 domain of Membrane Protein, Palmitoylated 4 (or MAGUK p55 subfamily member 4); ...
599-657 2.33e-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: 2.33e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 599 YVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPS 657
Cdd:cd12034     1 YVRAMVDYWPQQDPSIPCADAGLPFRKGDILQIVDQNDSLWWQARKLSDLAACAGLIPS 59
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
18-288 3.17e-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: 78.25  E-value: 3.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVK-IVDV-AKFTSSpglstegKRWISNLKREASICH--------MLKHPHIVELLEty 87
Cdd:cd07853     8 IGYGAFGVVWSVTDPRDGKRVALKkMPNVfQNLVSC-------KRVFRELKMLCFFKHdnvlsaldILQPPHIDPFEE-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 ssdgmLYMVFEFMDgADLCFEIVKradagfvySEAVASHYMR----QILEALRYCHDNNIIHRDVKPHCVLLASkenSAP 163
Cdd:cd07853    79 -----IYVVTELMQ-SDLHKIIVS--------PQPLSSDHVKvflyQILRGLKYLHSAGILHRDIKPGNLLVNS---NCV 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 164 VKLGGFGVA-IQLGESGLVAGGRVGTPHFMAPEVVKREP-YGKPVDVWGCGVILFILLSGCLPF---------------Y 226
Cdd:cd07853   142 LKICDFGLArVEEPDESKHMTQEVVTQYYRAPEILMGSRhYTSAVDIWSVGCIFAELLGRRILFqaqspiqqldlitdlL 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 227 GTK--ERLF---EG----IIKGKYKMNPRQW-----SHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE-RDRY 288
Cdd:cd07853   222 GTPslEAMRsacEGarahILRGPHKPPSLPVlytlsSQATHEAVHLLCRMLVFDPDKRISAADALAHPYLDEgRLRY 298
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
12-271 3.72e-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: 3.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd05633     7 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMK-----QGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGV 171
Cdd:cd05633    82 KLCFILDLMNGGDLHYHLSQHG----VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL---DEHGHVRISDLGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGgrVGTPHFMAPEVVKR-EPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSH 250
Cdd:cd05633   155 ACDFSKKKPHAS--VGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELPDS 232
                         250       260
                  ....*....|....*....|.
gi 1039796143 251 ISESAKDLVRRMLMLDPAERI 271
Cdd:cd05633   233 FSPELKSLLEGLLQRDVSKRL 253
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
12-271 3.78e-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: 3.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd14223     2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMK-----QGETLALNERIMLSLVSTGDCPFIVCMSYAFHTPD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGV 171
Cdd:cd14223    77 KLSFILDLMNGGDLHYHLSQHG----VFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILL---DEFGHVRISDLGL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGgrVGTPHFMAPEVVKRE-PYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSH 250
Cdd:cd14223   150 ACDFSKKKPHAS--VGTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDS 227
                         250       260
                  ....*....|....*....|.
gi 1039796143 251 ISESAKDLVRRMLMLDPAERI 271
Cdd:cd14223   228 FSPELRSLLEGLLQRDVNRRL 248
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
3-311 4.01e-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: 77.37  E-value: 4.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   3 DDDVLFEDVYElcevIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTEgkRWiSNLKREASICHMLKHPHIVE 82
Cdd:cd06634    12 DPEKLFSDLRE----IGHGSFGAVYFARDVRNNEVVAIK-----KMSYSGKQSNE--KW-QDIIKEVKFLQKLRHPNTIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  83 LLETYSSDGMLYMVFEFMDGA--DLcFEIVKRAdagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASken 160
Cdd:cd06634    80 YRGCYLREHTAWLVMEYCLGSasDL-LEVHKKP-----LQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTE--- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 161 SAPVKLGGFGVAIQLGEsglvAGGRVGTPHFMAPEVV---KREPYGKPVDVWGCGVIlfillsgCLPFYGTKERLFE-GI 236
Cdd:cd06634   151 PGLVKLGDFGSASIMAP----ANSFVGTPYWMAPEVIlamDEGQYDGKVDVWSLGIT-------CIELAERKPPLFNmNA 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 237 IKGKYKMNPR-----QWSHISESAKDLVRRMLMLDPAERITVYEALNHPWL-KERDRYAYKIHLPETVEQLRKFN--ARR 308
Cdd:cd06634   220 MSALYHIAQNespalQSGHWSEYFRNFVDSCLQKIPQDRPTSDVLLKHRFLlRERPPTVIMDLIQRTKDAVRELDnlQYR 299

                  ...
gi 1039796143 309 KLK 311
Cdd:cd06634   300 KMK 302
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
68-221 4.44e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 78.11  E-value: 4.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  68 EASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAgfvYSEAVASHymRQILEALRYCHDNNIIHRD 147
Cdd:PHA03212  133 EAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKTDLYCYLAAKRNIA---ICDILAIE--RSVLRAIQYLHENRIIHRD 207
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 148 VKPHCVLLaskENSAPVKLGGFGVA---IQLGESGLVagGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSG 221
Cdd:PHA03212  208 IKAENIFI---NHPGDVCLGDFGAAcfpVDINANKYY--GWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATC 279
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
18-215 5.36e-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: 76.15  E-value: 5.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKivDVAKFtsspglSTEGKRwisNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMK--ELIRF------DEETQR---TFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFIT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLcFEIVKRADAGFVYSEAVAshYMRQILEALRYCHDNNIIHRDVKPHCVLLasKENSAPVkLGGFGVA-IQLG 176
Cdd:cd14221    70 EYIKGGTL-RGIIKSMDSHYPWSQRVS--FAKDIASGMAYLHSMNIIHRDLNSHNCLV--RENKSVV-VADFGLArLMVD 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 177 ESGLVAGGR-------------VGTPHFMAPEVVKREPYGKPVDVWGCGVIL 215
Cdd:cd14221   144 EKTQPEGLRslkkpdrkkrytvVGNPYWMAPEMINGRSYDEKVDVFSFGIVL 195
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
18-286 1.21e-14

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


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 76.48  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKivDVAKFTSSPGLSTEGKRWISNLKreasicHMlKHPHIVELLETYSS----DGM- 92
Cdd:cd07879    23 VGSGAYGSVCSAIDKRTGEKVAIK--KLSRPFQSEIFAKRAYRELTLLK------HM-QHENVIGLLDVFTSavsgDEFq 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  93 -LYMVFEFMDgADLcfeivkRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCvlLASKENsAPVKLGGFGV 171
Cdd:cd07879    94 dFYLVMPYMQ-TDL------QKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGN--LAVNED-CELKILDFGL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESglvAGGRVGTPHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYGTK--------------------E 230
Cdd:cd07879   164 ARHADAE---MTGYVVTRWYRAPEVIlNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDyldqltqilkvtgvpgpefvQ 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039796143 231 RLFEGIIKGKYKMNPRQ--------WSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE-RD 286
Cdd:cd07879   241 KLEDKAAKSYIKSLPKYprkdfstlFPKASPQAVDLLEKMLELDVDKRLTATEALEHPYFDSfRD 305
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
18-243 1.28e-14

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: 75.99  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTsspglstegkRWISNLKREASICHMLKHPHIVELL--ETYSSDGMLYM 95
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFM----------RPLDVQMREFEVLKKLNHKNIVKLFaiEEELTTRHKVL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLcFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPV-KLGGFGVAIQ 174
Cdd:cd13988    71 VMELCPCGSL-YTVLEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVyKLTDFGAARE 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 175 LGESGLVAgGRVGTPHFMAPEVVKR--------EPYGKPVDVWGCGVILFILLSGCLPFygtkeRLFEGIIKGKYKM 243
Cdd:cd13988   150 LEDDEQFV-SLYGTEEYLHPDMYERavlrkdhqKKYGATVDLWSIGVTFYHAATGSLPF-----RPFEGPRRNKEVM 220
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
496-574 1.41e-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: 1.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 496 LVQFQKNTDEPMGITLK--MNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKI 573
Cdd:cd00136     1 TVTLEKDPGGGLGFSIRggKDGGGGIFVSRVEPGGPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELLKSAGGEVTLTV 80

                  .
gi 1039796143 574 V 574
Cdd:cd00136    81 R 81
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
67-282 1.59e-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: 1.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  67 REASICHMLKHPHIVELLETYSSDGML------YMVFEFMDgADLCFEIVKRADagfvysEAVASHYMRQILEALRYCHD 140
Cdd:cd07874    65 RELVLMKCVNHKNIISLLNVFTPQKSLeefqdvYLVMELMD-ANLCQVIQMELD------HERMSYLLYQMLCGIKHLHS 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 141 NNIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVIL----- 215
Cdd:cd07874   138 AGIIHRDLKPSNIVVKS---DCTLKILDFGLARTAGTSFMMT-PYVVTRYYRAPEVILGMGYKENVDIWSVGCIMgemvr 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 216 -FILLSG-----------------CLPFYGTKERLFEGIIKGKYK-------------MNPRQWSH---ISESAKDLVRR 261
Cdd:cd07874   214 hKILFPGrdyidqwnkvieqlgtpCPEFMKKLQPTVRNYVENRPKyagltfpklfpdsLFPADSEHnklKASQARDLLSK 293
                         250       260
                  ....*....|....*....|.
gi 1039796143 262 MLMLDPAERITVYEALNHPWL 282
Cdd:cd07874   294 MLVIDPAKRISVDEALQHPYI 314
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
17-278 2.04e-14

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: 74.22  E-value: 2.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRetGQQFAVKIVDvaKFTSSpglstegkrwiSNLKREASICHMLKHPHIVELLETYSSDGMLYMV 96
Cdd:cd14068     1 LLGDGGFGSVYRAVYR--GEDVAVKIFN--KHTSF-----------RLLRQELVVLSHLHHPSLVALLAAGTAPRMLVME 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMDGADLCFEivkRADAGFvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAS-KENSAPV-KLGGFGVAIQ 174
Cdd:cd14068    66 LAPKGSLDALLQ---QDNASL--TRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTlYPNCAIIaKIADYGIAQY 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 175 LGESGLVAGgrVGTPHFMAPEVVKRE-PYGKPVDVWGCGVILFILLSGclpfygtKERLFEGI----------IKGK--- 240
Cdd:cd14068   141 CCRMGIKTS--EGTPGFRAPEVARGNvIYNQQADVYSFGLLLYDILTC-------GERIVEGLkfpnefdelaIQGKlpd 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039796143 241 ----YKMNPrqWSHISEsakdLVRRMLMLDPAER---ITVYEALN 278
Cdd:cd14068   212 pvkeYGCAP--WPGVEA----LIKDCLKENPQCRptsAQVFDILN 250
L27 pfam02828
L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.
412-462 2.47e-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: 2.47e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 412 VQRAKEVLEEISCYPE-NNDAKELKRILTQPHFMALLQTHDVVAHEVYSDEA 462
Cdd:pfam02828   1 VELVLELLEDLQPLSEaSEDLAELQKLLQSPHLQALLEAHDKVAQKVYEPPS 52
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
18-286 2.63e-14

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: 74.72  E-value: 2.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVdvakftSSPGLSTEGKRWISNLkREASICHmlKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd06618    23 IGSGTCGQVYKMRHKKTGHVMAVKQM------RRSGNKEENKRILMDL-DVVLKSH--DCPYIVKCYGYFITDSDVFICM 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDgadLCFEIVKRADAGFVySEAVASHYMRQILEALRYCHDN-NIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLG 176
Cdd:cd06618    94 ELMS---TCLDKLLKRIQGPI-PEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILLDESGN---VKLCDFGISGRLV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 177 ESglVAGGR-VGTPHFMAPEVVKREPYGK---PVDVWGCGVILFILLSGCLPFYGTKERlFEGIIK----GKYKMNPRQw 248
Cdd:cd06618   167 DS--KAKTRsAGCAAYMAPERIDPPDNPKydiRADVWSLGISLVELATGQFPYRNCKTE-FEVLTKilneEPPSLPPNE- 242
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1039796143 249 sHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERD 286
Cdd:cd06618   243 -GFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRYE 279
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
8-282 2.98e-14

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: 75.05  E-value: 2.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYELCEVIGKGPFSVVRRCIN-RETGQQFAVKIV-DVAKFTSSPGLSTEGKRWISNLKRE-ASIChmlkhphiVELL 84
Cdd:cd14215    10 LQERYEIVSTLGEGTFGRVVQCIDhRRGGARVALKIIkNVEKYKEAARLEINVLEKINEKDPEnKNLC--------VQMF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  85 ETYSSDGMLYMVFEFMdgADLCFEIVKRADAgFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE----- 159
Cdd:cd14215    82 DWFDYHGHMCISFELL--GLSTFDFLKENNY-LPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSDyelty 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 160 -----------NSAPVKLGGFGVAIQLGESGLVAggrVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT 228
Cdd:cd14215   159 nlekkrdersvKSTAIRVVDFGSATFDHEHHSTI---VSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTH 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 229 KER----LFEGII------------KGKYKMNPR-QWS-------HISESAK-----------------DLVRRMLMLDP 267
Cdd:cd14215   236 DNRehlaMMERILgpipsrmirktrKQKYFYHGRlDWDentsagrYVRENCKplrryltseaeehhqlfDLIESMLEYEP 315
                         330
                  ....*....|....*
gi 1039796143 268 AERITVYEALNHPWL 282
Cdd:cd14215   316 SKRLTLAAALKHPFF 330
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
9-284 3.01e-14

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: 74.00  E-value: 3.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVYELCEvIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGlSTEGKRWISNL--KREASIChmlkhPHIVELLET 86
Cdd:cd06617     1 DDLEVIEE-LGRGAYGVVDKMRHVPTGTIMAVK-----RIRATVN-SQEQKRLLMDLdiSMRSVDC-----PYTVTFYGA 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYMVFEFMDGA-DLCFEIVKraDAGFVYSEAVASHYMRQILEALRYCHDN-NIIHRDVKPHCVLLASKENsapV 164
Cdd:cd06617    69 LFREGDVWICMEVMDTSlDKFYKKVY--DKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQ---V 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 165 KLGGFGVAIQLGESgLVAGGRVGTPHFMAPEVV--KREPYGKPV--DVWGCGVILFILLSGCLPF--YGTKERLFEGIIK 238
Cdd:cd06617   144 KLCDFGISGYLVDS-VAKTIDAGCKPYMAPERInpELNQKGYDVksDVWSLGITMIELATGRFPYdsWKTPFQQLKQVVE 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039796143 239 GKYKMNPRQwsHISESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd06617   223 EPSPQLPAE--KFSPEFQDFVNKCLKKNYKERPNYPELLQHPFFEL 266
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
16-279 3.32e-14

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: 73.86  E-value: 3.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVakfTSSPGLSTegkrwisnLKREASICHMLK-HPHIVELLE---TYSSDG 91
Cdd:cd14037     9 KYLAEGGFAHVYLVKTSNGGNRAALKRVYV---NDEHDLNV--------CKREIEIMKRLSgHKNIVGYIDssaNRSGNG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 M--LYMVFEFMDGADLCFEIVKRADAGFVYSEAVasHYMRQILEALRYCH--DNNIIHRDVKPHCVLLASKENsapVKLG 167
Cdd:cd14037    78 VyeVLLLMEYCKGGGVIDLMNQRLQTGLTESEIL--KIFCDVCEAVAAMHylKPPLIHRDLKVENVLISDSGN---YKLC 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVA------------IQLGESGLVaggRVGTPHFMAPEVVkrEPY-GKPV----DVWGCGVILFILLSGCLPFygtKE 230
Cdd:cd14037   153 DFGSAttkilppqtkqgVTYVEEDIK---KYTTLQYRAPEMI--DLYrGKPIteksDIWALGCLLYKLCFYTTPF---EE 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039796143 231 RLFEGIIKGKYKM--NPRQwshiSESAKDLVRRMLMLDPAERITVYEALNH 279
Cdd:cd14037   225 SGQLAILNGNFTFpdNSRY----SKRLHKLIRYMLEEDPEKRPNIYQVSYE 271
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
3-298 3.58e-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: 74.70  E-value: 3.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   3 DDDVLFEDVYElcevIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTEgkRWiSNLKREASICHMLKHPHIVE 82
Cdd:cd06635    22 DPEKLFSDLRE----IGHGSFGAVYFARDVRTSEVVAIK-----KMSYSGKQSNE--KW-QDIIKEVKFLQRIKHPNSIE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  83 LLETYSSDGMLYMVFEFMDGA--DLcFEIVKRAdagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASken 160
Cdd:cd06635    90 YKGCYLREHTAWLVMEYCLGSasDL-LEVHKKP-----LQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTE--- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 161 SAPVKLGGFGVAIQLGEsglvAGGRVGTPHFMAPEVV---KREPYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEG 235
Cdd:cd06635   161 PGQVKLADFGSASIASP----ANSFVGTPYWMAPEVIlamDEGQYDGKVDVWSLGITCIELAERKPPLFNMNamSALYHI 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 236 IIKGKYKMNPRQWshiSESAKDLVRRMLMLDPAERITVYEALNHPW-LKERdryaykihlPETV 298
Cdd:cd06635   237 AQNESPTLQSNEW---SDYFRNFVDSCLQKIPQDRPTSEELLKHMFvLRER---------PETV 288
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1-236 3.77e-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: 74.70  E-value: 3.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   1 MADDDvlFEDVYELceviGKGPFSVVRRCINRETGQQFAVKIVDVakftsspglstEGKRWISN-LKREASICHMLKHPH 79
Cdd:cd06649     2 LKDDD--FERISEL----GAGNGGVVTKVQHKPSGLIMARKLIHL-----------EIKPAIRNqIIRELQVLHECNSPY 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  80 IVELLETYSSDGMLYMVFEFMDGADLCfEIVKRADAgfvYSEAVASHYMRQILEALRYCHD-NNIIHRDVKPHCVLLASK 158
Cdd:cd06649    65 IVGFYGAFYSDGEISICMEHMDGGSLD-QVLKEAKR---IPEEILGKVSIAVLRGLAYLREkHQIMHRDVKPSNILVNSR 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796143 159 ensAPVKLGGFGVAIQLGESglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGI 236
Cdd:cd06649   141 ---GEIKLCDFGVSGQLIDS--MANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKELEAI 213
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
18-282 4.34e-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: 4.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRE---TGQQFAV---------KIVDVAKFTSSPGLSTEGKRwisnLKREASICHMLKHPHIVELLE 85
Cdd:cd07875    15 IGDSTFTVLKRYQNLKpigSGAQGIVcaaydaileRNVAIKKLSRPFQNQTHAKR----AYRELVLMKCVNHKNIIGLLN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  86 TYSSDGML------YMVFEFMDgADLCFEIVKRADagfvysEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASke 159
Cdd:cd07875    91 VFTPQKSLeefqdvYIVMELMD-ANLCQVIQMELD------HERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKS-- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 160 nSAPVKLGGFGVAIQLGESGLVAgGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTK---------E 230
Cdd:cd07875   162 -DCTLKILDFGLARTAGTSFMMT-PYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDhidqwnkviE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 231 RLFEGIIKGKYKMNPRQWSHI------------------------------SESAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd07875   240 QLGTPCPEFMKKLQPTVRTYVenrpkyagysfeklfpdvlfpadsehnklkASQARDLLSKMLVIDASKRISVDEALQHP 319

                  ..
gi 1039796143 281 WL 282
Cdd:cd07875   320 YI 321
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
64-229 4.85e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 74.88  E-value: 4.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  64 NLKREASICHMLKHPHIVELLETYSSDGMLYMVFEfmdgadlcfeiVKRADAgFVYSEAVASHYMRQI-------LEALR 136
Cdd:PHA03207  132 TPGREIDILKTISHRAIINLIHAYRWKSTVCMVMP-----------KYKCDL-FTYVDRSGPLPLEQAitiqrrlLEALA 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 137 YCHDNNIIHRDVKPHCVLLASKENSApvkLGGFGVAIQLGESGLVAG--GRVGTPHFMAPEVVKREPYGKPVDVWGCGVI 214
Cdd:PHA03207  200 YLHGRGIIHRDVKTENIFLDEPENAV---LGDFGAACKLDAHPDTPQcyGWSGTLETNSPELLALDPYCAKTDIWSAGLV 276
                         170
                  ....*....|....*
gi 1039796143 215 LFILLSGCLPFYGTK 229
Cdd:PHA03207  277 LFEMSVKNVTLFGKQ 291
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
61-216 4.99e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 75.31  E-value: 4.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  61 WISNLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDgADLCFEIVKRADA-GFVYSEAVAshymRQILEALRYCH 139
Cdd:PHA03211  203 WYASSVHEARLLRRLSHPAVLALLDVRVVGGLTCLVLPKYR-SDLYTYLGARLRPlGLAQVTAVA----RQLLSAIDYIH 277
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 140 DNNIIHRDVKPHCVLLASKENsapVKLGGFGVA--IQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILF 216
Cdd:PHA03211  278 GEGIIHRDIKTENVLVNGPED---ICLGDFGAAcfARGSWSTPFHYGIAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIF 353
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
68-220 1.31e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 73.37  E-value: 1.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  68 EASICHMLKHPHIVELLETYSSDGMLYMVFEFMDgADLCFEIVKR------ADAGFVyseavashyMRQILEALRYCHDN 141
Cdd:PHA03209  107 EAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYS-SDLYTYLTKRsrplpiDQALII---------EKQILEGLRYLHAQ 176
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 142 NIIHRDVKPHCVLLASKENsapVKLGGFGVAiQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLS 220
Cdd:PHA03209  177 RIIHRDVKTENIFINDVDQ---VCIGDLGAA-QFPVVAPAFLGLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEMLA 251
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
18-215 1.36e-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: 72.16  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKivDVAKFtsspglSTEGKRwisNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVMVMK--ELIRF------DEEAQR---NFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLIT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLcFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGE 177
Cdd:cd14154    70 EYIPGGTL-KDVLKDMARPLPWAQRV--RFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKT---VVVADFGLARLIVE 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796143 178 SGLVAGGR--------------------VGTPHFMAPEVVKREPYGKPVDVWGCGVIL 215
Cdd:cd14154   144 ERLPSGNMspsetlrhlkspdrkkrytvVGNPYWMAPEMLNGRSYDEKVDIFSFGIVL 201
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
493-575 1.46e-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: 66.63  E-value: 1.46e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  493 RVRLVQFQKNTdEPMGITLKMN--ELNHCIVARIMHGGMIHRQGtLHVGDEIREINGISVANQTVEQLQKMLREMRGSIT 570
Cdd:smart00228   1 EPRLVELEKGG-GGLGFSLVGGkdEGGGVVVSSVVPGSPAAKAG-LRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKVT 78

                   ....*
gi 1039796143  571 FKIVP 575
Cdd:smart00228  79 LTVLR 83
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
18-279 1.78e-13

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: 71.57  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETgqqfavkIVDVAKFTSSPGLSTEGKRwiSNLKREASICHMLKHPHIVELLETYSS----DGML 93
Cdd:cd14033     9 IGRGSFKTVYRGLDTET-------TVEVAWCELQTRKLSKGER--QRFSEEVEMLKGLQHPNIVRFYDSWKStvrgHKCI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  94 YMVFEFMDGADLCFEIVKRADAGFvyseAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLASKenSAPVKLGGFGV 171
Cdd:cd14033    80 ILVTELMTSGTLKTYLKRFREMKL----KLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITGP--TGSVKIGDLGL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQlgESGLVAGGRVGTPHFMAPEVVKrEPYGKPVDVWGCGVILFILLSGCLPFYGTKE--RLFEGIIKGkykMNPRQWS 249
Cdd:cd14033   154 ATL--KRASFAKSVIGTPEFMAPEMYE-EKYDEAVDVYAFGMCILEMATSEYPYSECQNaaQIYRKVTSG---IKPDSFY 227
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1039796143 250 HIS-ESAKDLVRRMLMLDPAERITVYEALNH 279
Cdd:cd14033   228 KVKvPELKEIIEGCIRTDKDERFTIQDLLEH 258
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
16-280 2.03e-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: 2.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKivdvakftsspglstEGKRWISNLKREASICHML-------KHPHIVELLETYS 88
Cdd:cd14051     6 EKIGSGEFGSVYKCINRLDGCVYAIK---------------KSKKPVAGSVDEQNALNEVyahavlgKHPHVVRYYSAWA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEN--SAPVKL 166
Cdd:cd14051    71 EDDHMIIQNEYCNGGSLADAISENEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNpvSSEEEE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFG----------VAIQLGESGLVAggRVGTPH-------FMAPEVVkREPYGK--PVDVWGCGVILFILLSG-CLPFY 226
Cdd:cd14051   151 EDFEgeednpesneVTYKIGDLGHVT--SISNPQveegdcrFLANEIL-QENYSHlpKADIFALALTVYEAAGGgPLPKN 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 227 GTKerlFEGIIKGKYKMNPrqwsHISESAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd14051   228 GDE---WHEIRQGNLPPLP----QCSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
SH3_DLG-like cd11861
Src Homology 3 domain of Disks large homolog proteins; The DLG-like proteins are scaffolding ...
599-657 2.88e-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: 2.88e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039796143 599 YVRAQFEYDPAKDDLIPCKeaGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTA--GLIPS 657
Cdd:cd11861     1 YVRALFDYDPSRDSGLPSQ--GLSFKFGDILHVTNASDDEWWQARRVTPNGEEEevGVIPS 59
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
32-227 3.34e-13

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: 70.76  E-value: 3.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  32 RETGQQFAVKIVDVAKFTSSPGL----------STEGKRWISNLKREASICHMLKHPHIVELLEtyssdgmlymvfefMD 101
Cdd:cd14067    14 RYQGQPVAVKRFHIKKCKKRTDGsadtmlkhlrAADAMKNFSEFRQEASMLHSLQHPCIVYLIG--------------IS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 102 GADLCF--EIVKRADAGFVYSE-AVASHYM-----------RQILEALRYCHDNNIIHRDVKPHCVLLASKE--NSAPVK 165
Cdd:cd14067    80 IHPLCFalELAPLGSLNTVLEEnHKGSSFMplghmltfkiaYQIAAGLAYLHKKNIIFCDLKSDNILVWSLDvqEHINIK 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 166 LGGFGVAIQLGESGLVagGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG 227
Cdd:cd14067   160 LSDYGISRQSFHEGAL--GVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRPSLG 219
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
57-296 4.56e-13

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: 69.98  E-value: 4.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  57 EGKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGAdlCFEIVKRADAGFVYSEAVASHYMrQILEALR 136
Cdd:cd05112    38 EGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHG--CLSDYLRTQRGLFSAETLLGMCL-DVCEGMA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 137 YCHDNNIIHRDVKPHCVLLAskENSApVKLGGFGVA-IQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVIL 215
Cdd:cd05112   115 YLEEASVIHRDLAARNCLVG--ENQV-VKVSDFGMTrFVLDDQYTSSTGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLM 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 216 FILLS-GCLPFYG-TKERLFEGIIKGKYKMNPRQWSHisesakdlvrrmlmldpaeriTVYEALNHPWlKER--DRYAYK 291
Cdd:cd05112   192 WEVFSeGKIPYENrSNSEVVEDINAGFRLYKPRLAST---------------------HVYEIMNHCW-KERpeDRPSFS 249

                  ....*
gi 1039796143 292 IHLPE 296
Cdd:cd05112   250 LLLRQ 254
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
18-264 1.31e-12

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: 68.89  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRciNRETGQqFAVKIVDVAKFTSSPglstegkrwISNLKREASICHMLKHPHIVeLLETYSSDGMLYMVF 97
Cdd:cd14150     8 IGTGSFGTVFR--GKWHGD-VAVKILKVTEPTPEQ---------LQAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIIT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLC---------FEIVKRADAGfvyseavashymRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGG 168
Cdd:cd14150    75 QWCEGSSLYrhlhvtetrFDTMQLIDVA------------RQTAQGMDYLHAKNIIHRDLKSNNIFL---HEGLTVKIGD 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVA-IQLGESGlvaGGRVGTPH----FMAPEVVKRE---PYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGK 240
Cdd:cd14150   140 FGLAtVKTRWSG---SQQVEQPSgsilWMAPEVIRMQdtnPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQIIFMVGR 216
                         250       260
                  ....*....|....*....|....
gi 1039796143 241 YKMNPrQWSHISESAKDLVRRMLM 264
Cdd:cd14150   217 GYLSP-DLSKLSSNCPKAMKRLLI 239
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
16-215 1.40e-12

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: 68.91  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCI-NRETGQ--QFAVKIVdvakftSSPGLSTEGKrwISNLKREASICHMLKHPHIVELLETYSSDGM 92
Cdd:cd05040     1 EKLGDGSFGVVRRGEwTTPSGKviQVAVKCL------KSDVLSQPNA--MDDFLKEVNAMHSLDHPNLIRLYGVVLSSPL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  93 LyMVFEFMDGADLcFEIVKRADAGFVYSeaVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVA 172
Cdd:cd05040    73 M-MVTELAPLGSL-LDRLRKDQGHFLIS--TLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDK---VKIGDFGLM 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 173 IQLGEsglvagGR---VGTPH------FMAPEVVKREPYGKPVDVWGCGVIL 215
Cdd:cd05040   146 RALPQ------NEdhyVMQEHrkvpfaWCAPESLKTRKFSHASDVWMFGVTL 191
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
12-282 1.84e-12

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: 69.49  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRE-TGQQFAVKIV-DVAKFTSSPGLSTEGKRWISNLKREASIchmlkhpHIVELLETYSS 89
Cdd:cd14213    14 YEIVDTLGEGAFGKVVECIDHKmGGMHVAVKIVkNVDRYREAARSEIQVLEHLNTTDPNSTF-------RCVQMLEWFDH 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLCFeIVKRADAGFVYSEAVASHYmrQILEALRYCHDNNIIHRDVKPHCVLLASKE---------- 159
Cdd:cd14213    87 HGHVCIVFELLGLSTYDF-IKENSFLPFPIDHIRNMAY--QICKSVNFLHHNKLTHTDLKPENILFVQSDyvvkynpkmk 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 160 ------NSAPVKLGGFGVAIQLGE--SGLVAggrvgTPHFMAPEVVKREPYGKPVDVW--GCGVILFILLSGCLPFYGTK 229
Cdd:cd14213   164 rdertlKNPDIKVVDFGSATYDDEhhSTLVS-----TRHYRAPEVILALGWSQPCDVWsiGCILIEYYLGFTVFQTHDSK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 230 ERL--FEGII------------KGKYKMNPR-QWSHISESAK------------------------DLVRRMLMLDPAER 270
Cdd:cd14213   239 EHLamMERILgplpkhmiqktrKRKYFHHDQlDWDEHSSAGRyvrrrckplkefmlsqdvdheqlfDLIQKMLEYDPAKR 318
                         330
                  ....*....|..
gi 1039796143 271 ITVYEALNHPWL 282
Cdd:cd14213   319 ITLDEALKHPFF 330
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
32-282 1.96e-12

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: 68.89  E-value: 1.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  32 RETGQQFAVKIVDvaKFTSSPGLSTEGKRWISNLKREASicHM--LKHPHIVELLETY-SSDGMLYMVFEFMDgADLCFE 108
Cdd:cd14011    18 KSTKQEVSVFVFE--KKQLEEYSKRDREQILELLKRGVK--QLtrLRHPRILTVQHPLeESRESLAFATEPVF-ASLANV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 109 IVKRAD--------AGFVYSEAVASHYMRQILEALRYCHDN-NIIHRDVKPHCVLLaskeNSAPV-KLGGFGVAIQL--- 175
Cdd:cd14011    93 LGERDNmpspppelQDYKLYDVEIKYGLLQISEALSFLHNDvKLVHGNICPESVVI----NSNGEwKLAGFDFCISSeqa 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 -GESGLVAGGRVGTPH-------FMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEgiikgkYKMNPRQ 247
Cdd:cd14011   169 tDQFPYFREYDPNLPPlaqpnlnYLAPEYILSKTCDPASDMFSLGVLIYAIYNKGKPLFDCVNNLLS------YKKNSNQ 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1039796143 248 WSHISESA--------KDLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14011   243 LRQLSLSLlekvpeelRDHVKTLLNVTPEVRPDAEQLSKIPFF 285
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
413-461 2.47e-12

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


Pssm-ID: 197794  Cd Length: 53  Bit Score: 62.14  E-value: 2.47e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039796143  413 QRAKEVLEEISCYPE-NNDAKELKRILTQPHFMALLQTHDVVAHEVYSDE 461
Cdd:smart00569   1 QRLLELLEELQSLLSpSEDLQELRRLLQSPHLQALLKIHDKVAETELDPP 50
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
18-284 2.51e-12

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: 68.54  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstEGKRWisnlKREASICHMLKHPHIVELLETYSS----DGML 93
Cdd:cd14030    33 IGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKS-----ERQRF----KEEAGMLKGLQHPNIVRFYDSWEStvkgKKCI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  94 YMVFEFMDGADLCfEIVKRADagfVYSEAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLASKENSapVKLGGFGV 171
Cdd:cd14030   104 VLVTELMTSGTLK-TYLKRFK---VMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTGS--VKIGDLGL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESglVAGGRVGTPHFMAPEVVKrEPYGKPVDVWGCGVILFILLSGCLPFYGTKE--RLFEGIIKGkykMNPRQWS 249
Cdd:cd14030   178 ATLKRAS--FAKSVIGTPEFMAPEMYE-EKYDESVDVYAFGMCMLEMATSEYPYSECQNaaQIYRRVTSG---VKPASFD 251
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039796143 250 HIS-ESAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd14030   252 KVAiPEVKEIIEGCIRQNKDERYAIKDLLNHAFFQE 287
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
13-280 3.11e-12

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: 67.76  E-value: 3.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  13 ELCEVIGKGPFSVVRRCINRetGQQFAVKIV-DVAKFTSSpglstegkrwisnLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd05039     9 KLGELIGKGEFGDVMLGDYR--GQKVAVKCLkDDSTAAQA-------------FLAEASVMTTLRHPNLVQLLGVVLEGN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRADAgfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSApvKLGGFGV 171
Cdd:cd05039    74 GLYIVTEYMAKGSLVDYLRSRGRA--VITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLV-SEDNVA--KVSDFGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AiQLGESGLvAGGRVgtP-HFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPF--YGTKErLFEGIIKGkYKMNPrq 247
Cdd:cd05039   149 A-KEASSNQ-DGGKL--PiKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYprIPLKD-VVPHVEKG-YRMEA-- 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039796143 248 wshiSESAKDLVRRMLM----LDPAERIT---VYEALNHP 280
Cdd:cd05039   221 ----PEGCPPEVYKVMKncweLDPAKRPTfkqLREKLEHI 256
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
10-280 5.36e-12

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: 67.36  E-value: 5.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELcEVIGKGPFSVVRRCINRETGQQFAVKivdvakfTSSPGLSteGKRWISNLKREASICHML-KHPHIVELLETYS 88
Cdd:cd14138     6 EFHEL-EKIGSGEFGSVFKCVKRLDGCIYAIK-------RSKKPLA--GSVDEQNALREVYAHAVLgQHSHVVRYYSAWA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE--NSAPVK- 165
Cdd:cd14138    76 EDDHMLIQNEYCNGGSLADAISENYRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSipNAASEEg 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 166 ----LGGFGVAIQLGESGLVAggRVGTPH-------FMAPEVVKrEPYG--KPVDVWGCGVILfILLSGCLPFYGTKERL 232
Cdd:cd14138   156 dedeWASNKVIFKIGDLGHVT--RVSSPQveegdsrFLANEVLQ-ENYThlPKADIFALALTV-VCAAGAEPLPTNGDQW 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039796143 233 FEgIIKGKYkmnPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd14138   232 HE-IRQGKL---PRIPQVLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
16-280 5.38e-12

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: 67.26  E-value: 5.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKivdvakftsspglstEGKRWISNLKREASICHML-------KHPHIVELLETYS 88
Cdd:cd14139     6 EKIGVGEFGSVYKCIKRLDGCVYAIK---------------RSMRPFAGSSNEQLALHEVyahavlgHHPHVVRYYSAWA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASK---------- 158
Cdd:cd14139    71 EDDHMIIQNEYCNGGSLQDAISENTKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFICHKmqsssgvgee 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 159 -ENSAPVKLGGfGVAIQLGESGLVAG-----GRVGTPHFMAPEVVKREPYGKP-VDVWGCGVILfILLSGCLPFyGTKER 231
Cdd:cd14139   151 vSNEEDEFLSA-NVVYKIGDLGHVTSinkpqVEEGDSRFLANEILQEDYRHLPkADIFALGLTV-ALAAGAEPL-PTNGA 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1039796143 232 LFEGIIKGKYKMNPRQwshISESAKDLVRRMLMLDPAERITVYEALNHP 280
Cdd:cd14139   228 AWHHIRKGNFPDVPQE---LPESFSSLLKNMIQPDPEQRPSATALARHT 273
pknD PRK13184
serine/threonine-protein kinase PknD;
12-295 6.53e-12

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 69.80  E-value: 6.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIV--DVAKFtssPGLStegKRWIsnlkREASICHMLKHPHIVELLETYSS 89
Cdd:PRK13184    4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIreDLSEN---PLLK---KRFL----REAKIAADLIHPGIVPVYSICSD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADL---------CfEIVKRADAgfvYSEAVAShYMR---QILEALRYCHDNNIIHRDVKPHCVLL-- 155
Cdd:PRK13184   74 GDPVYYTMPYIEGYTLksllksvwqK-ESLSKELA---EKTSVGA-FLSifhKICATIEYVHSKGVLHRDLKPDNILLgl 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 156 ----------------ASKENSAPVKLGGFGVaiqLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILL 219
Cdd:PRK13184  149 fgevvildwgaaifkkLEEEDLLDIDVDERNI---CYSSMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQML 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 220 SGCLPFYGTKER--LFEGIIKGKYKMNPrqWSHISESAKDLVRRMLMLDPAERITVYEALN---HPWLKERDRYAYKIHL 294
Cdd:PRK13184  226 TLSFPYRRKKGRkiSYRDVILSPIEVAP--YREIPPFLSQIAMKALAVDPAERYSSVQELKqdlEPHLQGSPEWTVKATL 303

                  .
gi 1039796143 295 P 295
Cdd:PRK13184  304 M 304
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
9-231 8.97e-12

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: 66.68  E-value: 8.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   9 EDVyELCEVIGKGPFSVVRRCI-NRETGQQFAVKiVDVAKFTSSPglsTEGKRWISnlkrEASICHMLKHPHIVELLETY 87
Cdd:cd05056     6 EDI-TLGRCIGEGQFGDVYQGVyMSPENEKIAVA-VKTCKNCTSP---SVREKFLQ----EAYIMRQFDHPHIVKLIGVI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMlYMVFEFMDGADLCFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLG 167
Cdd:cd05056    77 TENPV-WIVMELAPLGELRSYLQVNKYS---LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDC---VKLG 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796143 168 GFGVAIQLGESGLVAGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYGTKER 231
Cdd:cd05056   150 DFGLSRYMEDESYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWeILMLGVKPFQGVKNN 215
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
13-272 1.21e-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: 66.74  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  13 ELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVaKFTSSPGLSTEGKRWISNLKreaSICHMLKHPHIVELLETYSSDGM 92
Cdd:cd05055    38 SFGKTLGAGAFGKVVEATAYGLSKSDAVMKVAV-KMLKPTAHSSEREALMSELK---IMSHLGNHENIVNLLGACTIGGP 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  93 LYMVFEFMDGADLCFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVA 172
Cdd:cd05055   114 ILVITEYCCYGDLLNFLRRKRESFLTLEDLL--SFSYQVAKGMAFLASKNCIHRDLAARNVLLT---HGKIVKICDFGLA 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 173 IQ-LGESGLVAGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYGTK-ERLFEGIIKGKYKMNprQW 248
Cdd:cd05055   189 RDiMNDSNYVVKGNARLPvKWMAPESIFNCVYTFESDVWSYGILLWEIFSlGSNPYPGMPvDSKFYKLIKEGYRMA--QP 266
                         250       260
                  ....*....|....*....|....
gi 1039796143 249 SHISESAKDLVRRMLMLDPAERIT 272
Cdd:cd05055   267 EHAPAEIYDIMKTCWDADPLKRPT 290
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
18-284 1.21e-11

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: 66.25  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSspglsTEGKRWisnlKREASICHMLKHPHIVELLETYSSDGM----L 93
Cdd:cd14032     9 LGRGSFKTVYKGLDTETWVEVAWCELQDRKLTK-----VERQRF----KEEAEMLKGLQHPNIVRFYDFWESCAKgkrcI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  94 YMVFEFMDGADLCfEIVKRADagfVYSEAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLASKENSapVKLGGFGV 171
Cdd:cd14032    80 VLVTELMTSGTLK-TYLKRFK---VMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPTGS--VKIGDLGL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESglVAGGRVGTPHFMAPEVVKrEPYGKPVDVWGCGVILFILLSGCLPFYGTKE--RLFEGIIKGkykMNPRQWS 249
Cdd:cd14032   154 ATLKRAS--FAKSVIGTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPYSECQNaaQIYRKVTCG---IKPASFE 227
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039796143 250 HISE-SAKDLVRRMLMLDPAERITVYEALNHPWLKE 284
Cdd:cd14032   228 KVTDpEIKEIIGECICKNKEERYEIKDLLSHAFFAE 263
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
18-167 1.46e-11

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: 62.84  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAkftsspglSTEGKRWISNLKREASIChMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDDV--------NNEEGEDLESEMDILRRL-KGLELNIPKVLVTEDVDGPNILLM 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLCFEIVKRADagfvySEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLG 167
Cdd:cd13968    72 ELVKGGTLIAYTQEEEL-----DEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
12-301 1.75e-11

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 67.37  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKivdvaKFTSSPGLSTegkrwisnlkREASICHMLKHPHIVELLETYSSDG 91
Cdd:PTZ00036   68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIK-----KVLQDPQYKN----------RELLIMKNLNHINIIFLKDYYYTEC 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 M--------LYMVFEFMDgadlcfEIVKRADAGFVYSEA-----VASHYMRQILEALRYCHDNNIIHRDVKPHCVLLasK 158
Cdd:PTZ00036  133 FkkneknifLNVVMEFIP------QTVHKYMKHYARNNHalplfLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLI--D 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 159 ENSAPVKLGGFGVAiqlgeSGLVAGGR----VGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYG------ 227
Cdd:PTZ00036  205 PNTHTLKLCDFGSA-----KNLLAGQRsvsyICSRFYRAPELmLGATNYTTHIDLWSLGCIIAEMILGYPIFSGqssvdq 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 228 -----------TKERLFEgiikgkykMNPrQWSHIS------------------ESAKDLVRRMLMLDPAERITVYEALN 278
Cdd:PTZ00036  280 lvriiqvlgtpTEDQLKE--------MNP-NYADIKfpdvkpkdlkkvfpkgtpDDAINFISQFLKYEPLKRLNPIEALA 350
                         330       340
                  ....*....|....*....|....
gi 1039796143 279 HPWLKE-RDRYaykIHLPETVEQL 301
Cdd:PTZ00036  351 DPFFDDlRDPC---IKLPKYIDKL 371
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
599-657 1.94e-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: 1.94e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143  599 YVRAQFEYDPAKDDlipckeaGIRFRVGDIIQIISKDDHNWWQGKLensKNGTAGLIPS 657
Cdd:smart00326   4 QVRALYDYTAQDPD-------ELSFKKGDIITVLEKSDDGWWKGRL---GRGKEGLFPS 52
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
12-172 2.08e-11

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: 65.17  E-value: 2.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakftsspglSTEGKRwiSNLKREASICHMLK-HPHIVELLETYSSD 90
Cdd:cd14016     2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIE-----------KKDSKH--PQLEYEAKVYKLLQgGPGIPRLYWFGQEG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GMLYMVFEFMdGADL--CFEIVKR----------ADagfvyseavashymrQILEALRYCHDNNIIHRDVKPHCVLLASK 158
Cdd:cd14016    69 DYNVMVMDLL-GPSLedLFNKCGRkfslktvlmlAD---------------QMISRLEYLHSKGYIHRDIKPENFLMGLG 132
                         170
                  ....*....|....
gi 1039796143 159 ENSAPVKLGGFGVA 172
Cdd:cd14016   133 KNSNKVYLIDFGLA 146
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
129-231 2.42e-11

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: 65.11  E-value: 2.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 129 RQILEALRYCHDNNIIHRDVKPHCVLLASkenSAPVKLGGFGVAI--QLGESGLVAGGRVGTPHFMAPEVVK---REPYG 203
Cdd:cd14062    96 RQTAQGMDYLHAKNIIHRDLKSNNIFLHE---DLTVKIGDFGLATvkTRWSGSQQFEQPTGSILWMAPEVIRmqdENPYS 172
                          90       100
                  ....*....|....*....|....*...
gi 1039796143 204 KPVDVWGCGVILFILLSGCLPFYGTKER 231
Cdd:cd14062   173 FQSDVYAFGIVLYELLTGQLPYSHINNR 200
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
16-270 2.89e-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: 64.64  E-value: 2.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETgqqfavkiVDVAKFTSSPGLSTEGK-RWISnlkrEASICHMLKHPHIVELLETYSSDGMLY 94
Cdd:cd05085     2 ELLGKGNFGEVYKGTLKDK--------TPVAVKTCKEDLPQELKiKFLS----EARILKQYDHPNIVKLIGVCTQRQPIY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  95 MVFEFMDGADLCFEIVKRADagfvysEAVASHYMRQILEA---LRYCHDNNIIHRDVKPHCVLLAskENSApVKLGGFGV 171
Cdd:cd05085    70 IVMELVPGGDFLSFLRKKKD------ELKTKQLVKFSLDAaagMAYLESKNCIHRDLAARNCLVG--ENNA-LKISDFGM 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYG-TKERLFEGIIKGkYKMNPRQw 248
Cdd:cd05085   141 SRQEDDGVYSSSGLKQIPiKWTAPEALNYGRYSSESDVWSFGILLWETFSlGVCPYPGmTNQQAREQVEKG-YRMSAPQ- 218
                         250       260
                  ....*....|....*....|..
gi 1039796143 249 sHISESAKDLVRRMLMLDPAER 270
Cdd:cd05085   219 -RCPEDIYKIMQRCWDYNPENR 239
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
17-278 2.93e-11

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: 65.22  E-value: 2.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEgkrwisnlkreasICHMLK---HPHIVELLE--TYSSDG 91
Cdd:cd14036     7 VIAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNKAIIQE-------------INFMKKlsgHPNIVQFCSaaSIGKEE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLC----FEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLAskeNSAPVK 165
Cdd:cd14036    74 SDQGQAEYLLLTELCkgqlVDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIG---NQGQIK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 166 LGGFGVAIQL----------GESGLVAG--GRVGTPHFMAPEVV---KREPYGKPVDVWGCGVILFILLSGCLPFY-GTK 229
Cdd:cd14036   151 LCDFGSATTEahypdyswsaQKRSLVEDeiTRNTTPMYRTPEMIdlySNYPIGEKQDIWALGCILYLLCFRKHPFEdGAK 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039796143 230 ERlfegIIKGKYKM--NPRQWSHISesakDLVRRMLMLDPAERITVYEALN 278
Cdd:cd14036   231 LR----IINAKYTIppNDTQYTVFH----DLIRSTLKVNPEERLSITEIVE 273
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
18-282 3.18e-11

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: 64.65  E-value: 3.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglstegkrwisnlkrEASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd13995    12 IPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPS----------------DVEIQACFRHENIAELYGALLWEETVHLFM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGAdlcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskenSAPVKLGGFGVAIQLGE 177
Cdd:cd13995    76 EAGEGG----SVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFM----STKAVLVDFGLSVQMTE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 SGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNPrQWSHISESAK 256
Cdd:cd13995   148 DVYVPKDLRGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRsAYPSYLYIIHKQAP-PLEDIAQDCS 226
                         250       260       270
                  ....*....|....*....|....*....|
gi 1039796143 257 DLVRRM----LMLDPAERITVYEALNHPWL 282
Cdd:cd13995   227 PAMRELleaaLERNPNHRSSAAELLKHEAL 256
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
18-272 4.48e-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: 64.67  E-value: 4.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVV-----RRCINRETGQQFAVKIVDVAkftsspglSTEGKRwISNLKrEASICHMLKHPHIVELLETYSSDGM 92
Cdd:cd05032    14 LGQGSFGMVyeglaKGVVKGEPETRVAIKTVNEN--------ASMRER-IEFLN-EASVMKEFNCHHVVRLLGVVSTGQP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  93 LYMVFEFMDGADLCFEIVKR---ADAGFVYSEAVASHYMR---QILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKL 166
Cdd:cd05032    84 TLVVMELMAKGDLKSYLRSRrpeAENNPGLGPPTLQKFIQmaaEIADGMAYLAAKKFVHRDLAARNCMVAEDLT---VKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 167 GGFGVAIQLGESGLV--AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYG-TKERLFEGIIKGKYk 242
Cdd:cd05032   161 GDFGMTRDIYETDYYrkGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWeMATLAEQPYQGlSNEEVLKFVIDGGH- 239
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1039796143 243 MN-----PRQWshisesaKDLVRRMLMLDPAERIT 272
Cdd:cd05032   240 LDlpencPDKL-------LELMRMCWQYNPKMRPT 267
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
4-270 5.16e-11

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: 64.64  E-value: 5.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   4 DDVLFEDVyelcevIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglsTEGKRWISNLKreaSICHMLKHPHIVEL 83
Cdd:cd05089     2 EDIKFEDV------IGEGNFGQVIKAMIKKDGLKMNAAIKMLKEFASE----NDHRDFAGELE---VLCKLGHHPNIINL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  84 LETYSSDGMLYMVFEFMDGADLcFEIVKRA-----DAGFVYSEAVASHYM-RQILE-------ALRYCHDNNIIHRDVKP 150
Cdd:cd05089    69 LGACENRGYLYIAIEYAPYGNL-LDFLRKSrvletDPAFAKEHGTASTLTsQQLLQfasdvakGMQYLSEKQFIHRDLAA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 151 HCVLLAskENSApVKLGGFGVAiqLGESGLVAG--GRVGTpHFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYG 227
Cdd:cd05089   148 RNVLVG--ENLV-SKIADFGLS--RGEEVYVKKtmGRLPV-RWMAIESLNYSVYTTKSDVWSFGVLLWEIVSlGGTPYCG 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1039796143 228 -TKERLFEGIIKGKYKMNPRqwsHISESAKDLVRRMLMLDPAER 270
Cdd:cd05089   222 mTCAELYEKLPQGYRMEKPR---NCDDEVYELMRQCWRDRPYER 262
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
58-220 5.17e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 66.26  E-value: 5.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  58 GKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDgadlcFEIVKradagFVYSEAV----------ASHY 127
Cdd:PHA03210  203 GSRAAIQLENEILALGRLNHENILKIEEILRSEANTYMITQKYD-----FDLYS-----FMYDEAFdwkdrpllkqTRAI 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 128 MRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLgESGLVAG--GRVGTPHFMAPEVVKREPYGKP 205
Cdd:PHA03210  273 MKQLLCAVEYIHDKKLIHRDIKLENIFL---NCDGKIVLGDFGTAMPF-EKEREAFdyGWVGTVATNSPEILAGDGYCEI 348
                         170
                  ....*....|....*
gi 1039796143 206 VDVWGCGVILFILLS 220
Cdd:PHA03210  349 TDIWSCGLILLDMLS 363
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
12-253 7.45e-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: 63.82  E-value: 7.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKivdvakftsspglsTEGKRWISN-LKREASIC-HMLKHPHIVELLETYSS 89
Cdd:cd14017     2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMK--------------VESKSQPKQvLKMEVAVLkKLQGKPHFCRLIGCGRT 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMdGADLcFEIVKRADAGFvYSEAVASHYMRQILEALRYCHDNNIIHRDVKP-HCVLLASKENSAPVKLGG 168
Cdd:cd14017    68 ERYNYIVMTLL-GPNL-AELRRSQPRGK-FSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPsNFAIGRGPSDERTVYILD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 169 FGVAIQ-LGESGLV------AGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKY 241
Cdd:cd14017   145 FGLARQyTNKDGEVerpprnAAGFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKLKDKEEVGKMKEKI 224
                         250       260
                  ....*....|....*....|..
gi 1039796143 242 KMN------PRQ----WSHISE 253
Cdd:cd14017   225 DHEellkglPKEffqiLKHIRS 246
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
62-225 8.47e-11

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: 65.03  E-value: 8.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  62 ISNLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDN 141
Cdd:cd05626    45 VAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGGDMMSLLIRME----VFPEVLARFYIAELTLAIESVHKM 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 142 NIIHRDVKPHCVLLaskENSAPVKLGGFGVAI-----------QLGE----------------SGLVAGGR--------- 185
Cdd:cd05626   121 GFIHRDIKPDNILI---DLDGHIKLTDFGLCTgfrwthnskyyQKGShirqdsmepsdlwddvSNCRCGDRlktleqrat 197
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039796143 186 -----------VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF 225
Cdd:cd05626   198 kqhqrclahslVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQPPF 248
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
57-220 8.49e-11

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: 63.96  E-value: 8.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  57 EGKRWISNLKREASICHMLKHPHIVELLE-TYSSDGMLYMVFEFMdGADLCFEIVKRADAGF-VYSEAVASHYMRQILEA 134
Cdd:cd14001    44 QRSLYQERLKEEAKILKSLNHPNIVGFRAfTKSEDGSLCLAMEYG-GKSLNDLIEERYEAGLgPFPAATILKVALSIARA 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 135 LRYCH-DNNIIHRDVKPHCVLLASKENSapVKLGGFGVAIQLGESGLVA----GGRVGTPHFMAPEVVKRepyGKPV--- 206
Cdd:cd14001   123 LEYLHnEKKILHGDIKSGNVLIKGDFES--VKLCDFGVSLPLTENLEVDsdpkAQYVGTEPWKAKEALEE---GGVItdk 197
                         170
                  ....*....|....*
gi 1039796143 207 -DVWGCGVILFILLS 220
Cdd:cd14001   198 aDIFAYGLVLWEMMT 212
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
62-286 1.00e-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: 64.68  E-value: 1.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  62 ISNLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDN 141
Cdd:cd05625    45 VAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMG----VFPEDLARFYIAELTCAVESVHKM 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 142 NIIHRDVKPHCVLLaskENSAPVKLGGFGVAI-----------QLGE----------------SGLVAGGR--------- 185
Cdd:cd05625   121 GFIHRDIKPDNILI---DRDGHIKLTDFGLCTgfrwthdskyyQSGDhlrqdsmdfsnewgdpENCRCGDRlkplerraa 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 186 -----------VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHISE 253
Cdd:cd05625   198 rqhqrclahslVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAqTPLETQMKVINWQTSLHIPPQAKLSP 277
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039796143 254 SAKDLVRRmLMLDPAERI---TVYEALNHPWLKERD 286
Cdd:cd05625   278 EASDLIIK-LCRGPEDRLgknGADEIKAHPFFKTID 312
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
13-279 1.09e-10

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: 63.08  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  13 ELCEVIGKGPFSVVRrcINRETGQQFAVKIVDVakftsspglSTEGKRWISnlkrEASICHMLKHPHIVELLETYSSD-G 91
Cdd:cd05082     9 KLLQTIGKGEFGDVM--LGDYRGNKVAVKCIKN---------DATAQAFLA----EASVMTQLRHSNLVQLLGVIVEEkG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCFEIVKRADAgfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSApvKLGGFGV 171
Cdd:cd05082    74 GLYIVTEYMAKGSLVDYLRSRGRS--VLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLV-SEDNVA--KVSDFGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQLGESGLVAGGRVgtpHFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYGTKERLFEGIIKGKYKMNPRqwSH 250
Cdd:cd05082   149 TKEASSTQDTGKLPV---KWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYPRIPLKDVVPRVEKGYKMDAP--DG 223
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1039796143 251 ISESAKDLVRRMLMLDPAERIT---VYEALNH 279
Cdd:cd05082   224 CPPAVYDVMKNCWHLDAAMRPSflqLREQLEH 255
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
18-272 1.17e-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: 63.41  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCI----NRETGQQFAVKivdvakfTSSPGlstEGKRWISNLKREASICHMLKHPHIVELLETYSSDG-- 91
Cdd:cd05079    12 LGEGHFGKVELCRydpeGDNTGEQVAVK-------SLKPE---SGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGgn 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLCfEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGV 171
Cdd:cd05079    82 GIKLIMEFLPSGSLK-EYLPRNKNKINLKQQL--KYAVQICKGMDYLGSRQYVHRDLAARNVLV---ESEHQVKIGDFGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 --AIQLGESGLVAGGRVGTPHF-MAPEVVKREPYGKPVDVWGCGVILFILLSGCL--------------PFYG--TKERL 232
Cdd:cd05079   156 tkAIETDKEYYTVKDDLDSPVFwYAPECLIQSKFYIASDVWSFGVTLYELLTYCDsesspmtlflkmigPTHGqmTVTRL 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039796143 233 FEGIIKGKYKMNPrqwSHISESAKDLVRRMLMLDPAERIT 272
Cdd:cd05079   236 VRVLEEGKRLPRP---PNCPEEVYQLMRKCWEFQPSKRTT 272
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
18-225 1.21e-10

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: 63.29  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINREtgqqfavKIVDVAKFTSSPGLSTEGKRwiSNLKREASICHMLKHPHIVELLeTYSSDG-MLYMV 96
Cdd:cd14158    23 LGEGGFGVVFKGYIND-------KNVAVKKLAAMVDISTEDLT--KQFEQEIQVMAKCQHENLVELL-GYSCDGpQLCLV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMDGADL-----CFE----IVKRADAGFVYSEAVASHYMrqilealrycHDNNIIHRDVKPHCVLLasKENSAPvKLG 167
Cdd:cd14158    93 YTYMPNGSLldrlaCLNdtppLSWHMRCKIAQGTANGINYL----------HENNHIHRDIKSANILL--DETFVP-KIS 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 168 GFGVAIQLGESGLVAGGR--VGTPHFMAPEVVKREPYGKpVDVWGCGVILFILLSGCLPF 225
Cdd:cd14158   160 DFGLARASEKFSQTIMTEriVGTTAYMAPEALRGEITPK-SDIFSFGVVLLEIITGLPPV 218
L27 smart00569
domain in receptor targeting proteins Lin-2 and Lin-7;
354-407 1.23e-10

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


Pssm-ID: 197794  Cd Length: 53  Bit Score: 57.52  E-value: 1.23e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039796143  354 SQVLDSLEEIHALTDCSEkDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNP 407
Cdd:smart00569   1 QRLLELLEELQSLLSPSE-DLQELRRLLQSPHLQALLKIHDKVAETELDPPLPE 53
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
599-657 1.31e-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: 57.09  E-value: 1.31e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 599 YVRAQFEYDPAKDDLIPckeagirFRVGDIIQIISKDDHNWWQGKLENSKngtAGLIPS 657
Cdd:cd00174     1 YARALYDYEAQDDDELS-------FKKGDIITVLEKDDDGWWEGELNGGR---EGLFPA 49
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
12-243 1.42e-10

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: 62.84  E-value: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETgQQFAVKIVDVAKFTSSPGLSTEgkrwISNLKReasichmLKHPHIVELLETYSSDG 91
Cdd:cd05148     8 FTLERKLGSGYFGEVWEGLWKNR-VRVAIKILKSDDLLKQQDFQKE----VQALKR-------LRHKHLISLFAVCSVGE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGADLcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskENSApVKLGGFGV 171
Cdd:cd05148    76 PVYIITELMEKGSL--LAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVG--EDLV-CKVADFGL 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 172 AIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYG-TKERLFEGIIKGkYKM 243
Cdd:cd05148   151 ARLIKEDVYLSSDKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGmNNHEVYDQITAG-YRM 223
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
18-233 1.59e-10

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: 62.65  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQQFAVKivDVAKFTSSpglsTEgkrwiSNLKREASICHMLKHPHIVELLETYSSDGMLYMVF 97
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMK--ELIRCDEE----TQ-----KTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLcfEIVKRADAGFVYSEAVAshYMRQILEALRYCHDNNIIHRDVKPHCVLlaskensapVKLGGFGVAIQLGE 177
Cdd:cd14222    70 EFIEGGTL--KDFLRADDPFPWQQKVS--FAKGIASGMAYLHSMSIIHRDLNSHNCL---------IKLDKTVVVADFGL 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 178 SGLVAGGR--------------------------VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLS------GCLPF 225
Cdd:cd14222   137 SRLIVEEKkkpppdkpttkkrtlrkndrkkrytvVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEIIGqvyadpDCLPR 216
                         250
                  ....*....|.
gi 1039796143 226 ---YGTKERLF 233
Cdd:cd14222   217 tldFGLNVRLF 227
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
55-246 3.50e-10

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: 61.91  E-value: 3.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  55 STEGKRwiSNLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLC-FEIVKRADA-------GFVYSEAVASH 126
Cdd:cd05092    46 ATESAR--QDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMRHGDLNrFLRSHGPDAkildggeGQAPGQLTLGQ 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 127 YMR---QILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQLGESGLV-AGGRVGTP-HFMAPEVVKREP 201
Cdd:cd05092   124 MLQiasQIASGMVYLASLHFVHRDLATRNCLVG---QGLVVKIGDFGMSRDIYSTDYYrVGGRTMLPiRWMPPESILYRK 200
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1039796143 202 YGKPVDVWGCGVILF-ILLSGCLPFYG-TKERLFEGIIKGKYKMNPR 246
Cdd:cd05092   201 FTTESDIWSFGVVLWeIFTYGKQPWYQlSNTEAIECITQGRELERPR 247
PDZ3_DLG5-like cd06767
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
495-573 4.81e-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: 4.81e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 495 RLVQFQKnTDEPMGITLKMNELNHCIVARIMHGGMIHRQGtLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKI 573
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 ...
501-563 5.25e-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: 5.25e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 501 KNTDEPMGITLKMN-ELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLR 563
Cdd:cd06670    10 VKGNSSLGITVSADkDGNGCIVKSIIHGGAVSRDGRISVGDFIVSINNESLRNVTNAQARAILR 73
SH3_DLG3 cd12029
Src Homology 3 domain of Disks Large homolog 3; DLG3, also called synapse-associated protein ...
596-662 5.45e-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: 56.25  E-value: 5.45e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 596 RQIYVRAQFEYDPAKDDLIPCKeaGIRFRVGDIIQIISKDDHNWWQGKL--ENSKNGTAGLIPSPELQE 662
Cdd:cd12029     1 RSLYVRALFDYDRTRDSCLPSQ--GLSFSYGDILHVINASDDEWWQARLvtPHGESEQIGVIPSKKRVE 67
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
18-229 5.45e-10

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 60.83  E-value: 5.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRETGQqfavKIVDVAKFTSSPGLSTEGKRwisNLKREASICHMLKHPHIVELLETYSSDGMLyMVF 97
Cdd:cd05060     3 LGHGNFGSVRKGVYLMKSG----KEVEVAVKTLKQEHEKAGKK---EFLREASVMAQLDHPCIVRLIGVCKGEPLM-LVM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV--AIQL 175
Cdd:cd05060    75 ELAPLGPLLKYLKKRRE----IPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQ---AKISDFGMsrALGA 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796143 176 GESGLVA--GGRvgTP-HFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYGTK 229
Cdd:cd05060   148 GSDYYRAttAGR--WPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGEMK 203
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
13-227 5.47e-10

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: 61.24  E-value: 5.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  13 ELCEVIGKGPFSVVRR-----CINRETGQQFAVKIVdvaKFTSSPGLSTEgkrwisnLKREASICHMLKHPHIVELLETY 87
Cdd:cd05048     8 RFLEELGEGAFGKVYKgellgPSSEESAISVAIKTL---KENASPKTQQD-------FRREAELMSDLQHPNIVCLLGVC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  88 SSDGMLYMVFEFMDGADLCFEIVKRA---DAGFVYSEAVASHYMR---------QILEALRYCHDNNIIHRDVKPHCVLL 155
Cdd:cd05048    78 TKEQPQCMLFEYMAHGDLHEFLVRHSphsDVGVSSDDDGTASSLDqsdflhiaiQIAAGMEYLSSHHYVHRDLAARNCLV 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796143 156 ASKENsapVKLGGFGVA--IQLGESGLVAGGRVGTPHFMAPEVVKrepYGK---PVDVWGCGVILFILLS-GCLPFYG 227
Cdd:cd05048   158 GDGLT---VKISDFGLSrdIYSSDYYRVQSKSLLPVRWMPPEAIL---YGKfttESDVWSFGVVLWEIFSyGLQPYYG 229
SH3_DLG1 cd12031
Src Homology 3 domain of Disks Large homolog 1; DLG1, also called synapse-associated protein ...
596-657 6.48e-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: 6.48e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 596 RQIYVRAQFEYDPAKDDLIPCKeaGIRFRVGDIIQIISKDDHNWWQGK--LENSKNGTAGLIPS 657
Cdd:cd12031     1 RSLYVRALFDYDKTKDSGLPSQ--GLNFKFGDILHVVNASDDEWWQARqvTADGESEEIGVIPS 62
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
16-270 6.95e-10

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: 60.82  E-value: 6.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSpglsTEGKRWISNLKreaSICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd05047     1 DVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASK----DDHRDFAGELE---VLCKLGHHPNIINLLGACEHRGYLYL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLcFEIVKRA-----DAGFVYSEAVAS--------HYMRQILEALRYCHDNNIIHRDVKPHCVLLAskENSA 162
Cdd:cd05047    74 AIEYAPHGNL-LDFLRKSrvletDPAFAIANSTAStlssqqllHFAADVARGMDYLSQKQFIHRDLAARNILVG--ENYV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 163 pVKLGGFGVAiqLGESGLVAG--GRVGTpHFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYG-TKERLFEGIIK 238
Cdd:cd05047   151 -AKIADFGLS--RGQEVYVKKtmGRLPV-RWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGmTCAELYEKLPQ 226
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1039796143 239 GKYKMNPRqwsHISESAKDLVRRMLMLDPAER 270
Cdd:cd05047   227 GYRLEKPL---NCDDEVYDLMRQCWREKPYER 255
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
3-231 7.49e-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: 60.85  E-value: 7.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   3 DDDVLFEDVYELCEVIGKGPFSVVRRciNRETGQqFAVKIVDVAKFTSspglstegkRWISNLKREASICHMLKHPHIVe 82
Cdd:cd14151     1 DDWEIPDGQITVGQRIGSGSFGTVYK--GKWHGD-VAVKMLNVTAPTP---------QQLQAFKNEVGVLRKTRHVNIL- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  83 LLETYSSDGMLYMVFEFMDGADLC---------FEIVKRADAGfvyseavashymRQILEALRYCHDNNIIHRDVKPHCV 153
Cdd:cd14151    68 LFMGYSTKPQLAIVTQWCEGSSLYhhlhiietkFEMIKLIDIA------------RQTAQGMDYLHAKSIIHRDLKSNNI 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 154 LLaskENSAPVKLGGFGVA-IQLGESGLVAGGRV-GTPHFMAPEVVK---REPYGKPVDVWGCGVILFILLSGCLPFYGT 228
Cdd:cd14151   136 FL---HEDLTVKIGDFGLAtVKSRWSGSHQFEQLsGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYELMTGQLPYSNI 212

                  ...
gi 1039796143 229 KER 231
Cdd:cd14151   213 NNR 215
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
4-245 7.70e-10

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: 61.09  E-value: 7.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   4 DDVLFEDVYELCEVIGKGPFSVVRRC---INRETGQQFAVKIVDVAKFTSSPglstegkrwISNLKREASICHMLKHPHI 80
Cdd:cd05074     3 DVLIQEQQFTLGRMLGKGEFGSVREAqlkSEDGSFQKVAVKMLKADIFSSSD---------IEEFLREAACMKEFDHPNV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  81 VELLETY---SSDGML---YMVFEFMDGADL-CFEIVKR-ADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHC 152
Cdd:cd05074    74 IKLIGVSlrsRAKGRLpipMVILPFMKHGDLhTFLLMSRiGEEPFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 153 VLLASKENsapVKLGGFGVAIQLGESGLVAGGRVGT-P-HFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYGTK 229
Cdd:cd05074   154 CMLNENMT---VCVADFGLSKKIYSGDYYRQGCASKlPvKWLALESLADNVYTTHSDVWAFGVTMWeIMTRGQTPYAGVE 230
                         250
                  ....*....|....*..
gi 1039796143 230 E-RLFEGIIKGKYKMNP 245
Cdd:cd05074   231 NsEIYNYLIKGNRLKQP 247
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
17-227 8.94e-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: 60.51  E-value: 8.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRCINRETGQQfaVKI---VDVAKFTSSPGLSTEgkrwisnLKREASICHMLKHPHIVELLETYSSDGML 93
Cdd:cd05057    14 VLGSGAFGTVYKGVWIPEGEK--VKIpvaIKVLREETGPKANEE-------ILDEAYVMASVDHPHLVRLLGICLSSQVQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  94 yMVFEFMDGADLcFEIVkRADAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAI 173
Cdd:cd05057    85 -LITQLMPLGCL-LDYV-RNHRDNIGSQLLLN-WCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNH---VKITDFGLAK 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 174 QLG---ESGLVAGGRVgtP-HFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYG 227
Cdd:cd05057   158 LLDvdeKEYHAEGGKV--PiKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYEG 214
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
67-279 8.99e-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: 60.51  E-value: 8.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  67 REASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLcFEIVKRADAGFVysEAVASHYM-RQILEALRYCHDNNIIH 145
Cdd:cd05052    51 KEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNL-LDYLRECNREEL--NAVVLLYMaTQIASAMEYLEKKNFIH 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 146 RDVKPHCVLLAskENSApVKLGGFGVAIQLGESGLVAGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCL 223
Cdd:cd05052   128 RDLAARNCLVG--ENHL-VKVADFGLSRLMTGDTYTAHAGAKFPiKWTAPESLAYNKFSIKSDVWAFGVLLWeIATYGMS 204
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 224 PFYGTKERLFEGIIKGKYKMNprQWSHISESAKDLVRRMLMLDPAERIT---VYEALNH 279
Cdd:cd05052   205 PYPGIDLSQVYELLEKGYRME--RPEGCPPKVYELMRACWQWNPSDRPSfaeIHQALET 261
SH3_DLG2 cd12032
Src Homology 3 domain of Disks Large homolog 2; DLG2, also called postsynaptic density-93 ...
596-657 9.02e-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: 55.86  E-value: 9.02e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 596 RQIYVRAQFEYDPAKDDLIPCKeaGIRFRVGDIIQIISKDDHNWWQGK--LENSKNGTAGLIPS 657
Cdd:cd12032     4 RSLYVRAMFDYEKSKDSGLPSQ--GLSFRYGDILHVINASDDEWWQARrvTPDGDSEEMGVIPS 65
gmk PRK14738
guanylate kinase; Provisional
720-882 1.27e-09

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 58.97  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 720 LVLLGAHGVGRRHIKNTLITKHPDrFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLE 799
Cdd:PRK14738   16 VVISGPSGVGKDAVLARMRERKLP-FHFVVTATTRPKRPGEIDGVDYHFVTPEEFREMISQNELLEWAEVYGNYYGVPKA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 800 TIRKIHEQGLIAILDVEPQALKVLRtaEFAPFVVFI-AAPtitPGLNE------------DESL-QRLQKESDVLQRTYA 865
Cdd:PRK14738   95 PVRQALASGRDVIVKVDVQGAASIK--RLVPEAVFIfLAP---PSMDEltrrlelrrtesPEELeRRLATAPLELEQLPE 169
                         170
                  ....*....|....*....
gi 1039796143 866 hyFDLTIIN--NEIDETIR 882
Cdd:PRK14738  170 --FDYVVVNpeDRLDEAVA 186
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
65-239 1.65e-09

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 59.82  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  65 LKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLcFEIVKRADAGFvyseAVASHYMRQILEALRYCHDNNII 144
Cdd:cd14027    38 LLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNL-MHVLKKVSVPL----SVKGRIILEIIEGMAYLHGKGVI 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 145 HRDVKPHCVLLaskENSAPVKLGGFGVAIQLGESGL-------------VAGGRVGTPHFMAPEVVkREPYGKPV---DV 208
Cdd:cd14027   113 HKDLKPENILV---DNDFHIKIADLGLASFKMWSKLtkeehneqrevdgTAKKNAGTLYYMAPEHL-NDVNAKPTeksDV 188
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1039796143 209 WGCGVILFILLSGCLPFYG--TKERLFEGIIKG 239
Cdd:cd14027   189 YSFAIVLWAIFANKEPYENaiNEDQIIMCIKSG 221
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
18-226 2.07e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 59.70  E-value: 2.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRC----INRETGQQFAVKIVDvakfTSSPGLStegkrwISNLKREASICHMLKHPHIVELLETYSSDGM- 92
Cdd:cd05038    12 LGEGHFGSVELCrydpLGDNTGEQVAVKSLQ----PSGEEQH------MSDFKREIEILRTLDHEYIVKYKGVCESPGRr 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  93 -LYMVFEFMDGAdlCFEIVKRADAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 171
Cdd:cd05038    82 sLRLIMEYLPSG--SLRDYLQRHRDQIDLKRLLL-FASQICKGMEYLGSQRYIHRDLAARNILVESEDL---VKISDFGL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039796143 172 A--IQLGESGLVAGGRVGTPHF-MAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFY 226
Cdd:cd05038   156 AkvLPEDKEYYYVKEPGESPIFwYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQ 213
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
19-277 2.32e-09

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: 58.82  E-value: 2.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  19 GKGPFSVVRRCINRETGQQFAVKIvdvakftsspglstegkrwISNLKREASICHMLKHPHIVE------------LLET 86
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKK-------------------LLKIEKEAEILSVLSHRNIIQfygaileapnygIVTE 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  87 YSSDGMLYmvfEFMDGADlcfeivkradagfvySEAV-ASHYM---RQILEALRYCHDN---NIIHRDVKPHCVLLASke 159
Cdd:cd14060    63 YASYGSLF---DYLNSNE---------------SEEMdMDQIMtwaTDIAKGMHYLHMEapvKVIHRDLKSRNVVIAA-- 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 160 nSAPVKLGGFGVAIQLGESGLVAggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGtkerlFEG---- 235
Cdd:cd14060   123 -DGVLKICDFGASRFHSHTTHMS--LVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKG-----LEGlqva 194
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039796143 236 ---IIKGKYKMNPrqwSHISESAKDLVRRMLMLDPAERITVYEAL 277
Cdd:cd14060   195 wlvVEKNERPTIP---SSCPRSFAELMRRCWEADVKERPSFKQII 236
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
16-222 2.37e-09

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 59.60  E-value: 2.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCiNRETGQQFAVkiVDVAKFTSSPGL-------STEGKRWISNLKREASICHMLKHPHIVELLETYS 88
Cdd:cd05097    11 EKLGEGQFGEVHLC-EAEGLAEFLG--EGAPEFDGQPVLvavkmlrADVTKTARNDFLKEIKIMSRLKNPNIIRLLGVCV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  89 SDGMLYMVFEFMDGADLCFEIVKRA-DAGFVYSEAVAS-------HYMRQILEALRYCHDNNIIHRDVKPHCVLLaskEN 160
Cdd:cd05097    88 SDDPLCMITEYMENGDLNQFLSQREiESTFTHANNIPSvsianllYMAVQIASGMKYLASLNFVHRDLATRNCLV---GN 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 161 SAPVKLGGFGVAIQL--GESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGC 222
Cdd:cd05097   165 HYTIKIADFGMSRNLysGDYYRIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLC 228
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
18-231 3.20e-09

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: 58.89  E-value: 3.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRciNRETGQqFAVKIVDVAKFTSSPglstegkrwISNLKREASICHMLKHPHIVeLLETYSSDGMLYMVF 97
Cdd:cd14149    20 IGSGSFGTVYK--GKWHGD-VAVKILKVVDPTPEQ---------FQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  98 EFMDGADLcFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVA-IQLG 176
Cdd:cd14149    87 QWCEGSSL-YKHLHVQETKFQMFQLI--DIARQTAQGMDYLHAKNIIHRDMKSNNIFL---HEGLTVKIGDFGLAtVKSR 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 177 ESGLVAGGR-VGTPHFMAPEVVKRE---PYGKPVDVWGCGVILFILLSGCLPFYGTKER 231
Cdd:cd14149   161 WSGSQQVEQpTGSILWMAPEVIRMQdnnPFSFQSDVYSYGIVLYELMTGELPYSHINNR 219
L27 pfam02828
L27 domain; The L27 domain is found in receptor targeting proteins Lin-2 and Lin-7.
353-400 3.22e-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: 3.22e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1039796143 353 VSQVLDSLEEIHALTDCSEkDLDFLHSVFQDQHLHTLLDLYDKINTKS 400
Cdd:pfam02828   1 VELVLELLEDLQPLSEASE-DLAELQKLLQSPHLQALLEAHDKVAQKV 47
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
16-226 3.44e-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: 58.99  E-value: 3.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRciNRETGQQFAVKIVDVAkftsspglstEGKRWIsnlkREASICH--MLKHPHIVELL---ETYSSD 90
Cdd:cd13998     1 EVIGKGRFGEVWK--ASLKNEPVAVKIFSSR----------DKQSWF----REKEIYRtpMLKHENILQFIaadERDTAL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  91 GM-LYMVFEFMDGADLCfEIVKRADAGFVYSEAVASHYMRqileALRYCHDN---------NIIHRDVKPHCVLLasKEN 160
Cdd:cd13998    65 RTeLWLVTAFHPNGSL*-DYLSLHTIDWVSLCRLALSVAR----GLAHLHSEipgctqgkpAIAHRDLKSKNILV--KND 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 161 SAPVkLGGFGVAIQL----GESGLVAGGRVGTPHFMAPEV------VKREPYGKPVDVWGCGVILFILLSGC-------- 222
Cdd:cd13998   138 GTCC-IADFGLAVRLspstGEEDNANNGQVGTKRYMAPEVlegainLRDFESFKRVDIYAMGLVLWEMASRCtdlfgive 216

                  ....*..
gi 1039796143 223 ---LPFY 226
Cdd:cd13998   217 eykPPFY 223
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
13-272 3.56e-09

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: 58.90  E-value: 3.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  13 ELCEVIGKGPFSVVRRciNRETGQqFAVKIVDVAkftsspGLSTEGkrwISNLKREASICHMLKHPHIVELLETYSSDGM 92
Cdd:cd14063     3 EIKEVIGKGRFGRVHR--GRWHGD-VAIKLLNID------YLNEEQ---LEAFKEEVAAYKNTRHDNLVLFMGACMDPPH 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  93 LYMVFEFMDGADLcFEIVKRADAGFVYSEAVasHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVkLGGFGVa 172
Cdd:cd14063    71 LAIVTSLCKGRTL-YSLIHERKEKFDFNKTV--QIAQQICQGMGYLHAKGIIHKDLKSKNIFL---ENGRVV-ITDFGL- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 173 iqLGESGLVAGGR----VGTPH----FMAPEVVK----------REPYGKPVDVWGCGVILFILLSGCLPFygtKERLFE 234
Cdd:cd14063   143 --FSLSGLLQPGRredtLVIPNgwlcYLAPEIIRalspdldfeeSLPFTKASDVYAFGTVWYELLAGRWPF---KEQPAE 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1039796143 235 GII--KGKYKMNPRQWSHISESAKDLVRRMLMLDPAERIT 272
Cdd:cd14063   218 SIIwqVGCGKKQSLSQLDIGREVKDILMQCWAYDPEKRPT 257
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
16-220 3.92e-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: 58.54  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQqfavKIVDVAKFTSSPGlSTEGKRWisNLKREASICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd05033    10 KVIGGGEFGEVCSGSLKLPGK----KEIDVAIKTLKSG-YSDKQRL--DFLTEASIMGQFDHPNVIRLEGVVTKSRPVMI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLcFEIVKRADAGFVYSEAVAshYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQL 175
Cdd:cd05033    83 VTEYMENGSL-DKFLRENDGKFTVTQLVG--MLRGIASGMKYLSEMNYVHRDLAARNILVNSDLV---CKVSDFGLSRRL 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039796143 176 GESG---LVAGGRVGTpHFMAPEVVKREPYGKPVDVWGCGVILFILLS 220
Cdd:cd05033   157 EDSEatyTTKGGKIPI-RWTAPEAIAYRKFTSASDVWSFGIVMWEVMS 203
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
131-270 4.69e-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: 4.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 131 ILEALRYCHDNNIIHRDVKPHCVLLaSKENSApvKLGGFGVAIqlgESGLVAGGRVGTPHFMAPEVVKREpYGKPVDVWG 210
Cdd:cd13975   111 VVEGIRFLHSQGLVHRDIKLKNVLL-DKKNRA--KITDLGFCK---PEAMMSGSIVGTPIHMAPELFSGK-YDNSVDVYA 183
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796143 211 CGVILFILLSGC--LPF----YGTKERLFEGIIKGkykMNPRQWSHISESAKDLVRRMLMLDPAER 270
Cdd:cd13975   184 FGILFWYLCAGHvkLPEafeqCASKDHLWNNVRKG---VRPERLPVFDEECWNLMEACWSGDPSQR 246
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
16-222 5.90e-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: 58.11  E-value: 5.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVV--RRCINRETgqqfAVKIVDVAKFTSspglstegkrWIsNLKREASICHMlKHPHIVELL----ETYSS 89
Cdd:cd14053     1 EIKARGRFGAVwkAQYLNRLV----AVKIFPLQEKQS----------WL-TEREIYSLPGM-KHENILQFIgaekHGESL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGMLYMVFEFMDGADLCfEIVKradaGFVYSEAVASHYMRQILEALRYCHDN----------NIIHRDVKPHCVLLasKE 159
Cdd:cd14053    65 EAEYWLITEFHERGSLC-DYLK----GNVISWNELCKIAESMARGLAYLHEDipatngghkpSIAHRDFKSKNVLL--KS 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 160 NSAPVkLGGFGVAIQLgESGLVAG---GRVGTPHFMAPEVV------KREPYgKPVDVWGCGVILFILLSGC 222
Cdd:cd14053   138 DLTAC-IADFGLALKF-EPGKSCGdthGQVGTRRYMAPEVLegainfTRDAF-LRIDMYAMGLVLWELLSRC 206
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
130-278 5.92e-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: 5.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 130 QILEALRYCHDNNIIHRDVKPHCVLLASKENSAPV-KLGGFGVAIQLGESGL--------VAGGrvGTPHFMAPEVVKRE 200
Cdd:cd14018   146 QLLEGVDHLVRHGIAHRDLKSDNILLELDFDGCPWlVIADFGCCLADDSIGLqlpfsswyVDRG--GNACLMAPEVSTAV 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 201 P-------YGKpVDVWGCGVILFILLSGCLPFYGTKERLFEgiiKGKYKMN--PRQWSHISESAKDLVRRMLMLDPAERI 271
Cdd:cd14018   224 PgpgvvinYSK-ADAWAVGAIAYEIFGLSNPFYGLGDTMLE---SRSYQESqlPALPSAVPPDVRQVVKDLLQRDPNKRV 299

                  ....*..
gi 1039796143 272 TVYEALN 278
Cdd:cd14018   300 SARVAAN 306
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
62-244 6.57e-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: 6.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  62 ISNLKREASICHML-KHPHIVELLETYSSDGMLYMVFEFMD--------------GADLCFEIVKRADAGFVYSEAVASH 126
Cdd:cd05101    73 LSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYVIVEYASkgnlreylrarrppGMEYSYDINRVPEEQMTFKDLVSCT 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 127 YmrQILEALRYCHDNNIIHRDVKPHCVLLAskENSApVKLGGFGVAIQLGESGL---VAGGRVGTpHFMAPEVVKREPYG 203
Cdd:cd05101   153 Y--QLARGMEYLASQKCIHRDLAARNVLVT--ENNV-MKIADFGLARDINNIDYykkTTNGRLPV-KWMAPEALFDRVYT 226
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1039796143 204 KPVDVWGCGVILF-ILLSGCLPFYGTK-ERLFEgIIKGKYKMN 244
Cdd:cd05101   227 HQSDVWSFGVLMWeIFTLGGSPYPGIPvEELFK-LLKEGHRMD 268
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
18-253 6.84e-09

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 57.84  E-value: 6.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRCINRetGQ-QFAVKIVDvakftsspglstEGKRWISNLKREASICHMLKHPHIVELLETYSSDGMLYMV 96
Cdd:cd05059    12 LGSGQFGVVHLGKWR--GKiDVAIKMIK------------EGSMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  97 FEFMdgADLCFEIVKRADAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKP-HCvlLASKENSapVKLGGFGVAIQL 175
Cdd:cd05059    78 TEYM--ANGCLLNYLRERRGKFQTEQLLE-MCKDVCEAMEYLESNGFIHRDLAArNC--LVGEQNV--VKVSDFGLARYV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 176 GESGLVAGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYGTK-----ERLFEGIIKGKYKMNPRQ- 247
Cdd:cd05059   151 LDDEYTSSVGTKFPvKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSnsevvEHISQGYRLYRPHLAPTEv 230
                         250
                  ....*....|...
gi 1039796143 248 -------WSHISE 253
Cdd:cd05059   231 ytimyscWHEKPE 243
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
45-246 7.07e-09

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: 57.74  E-value: 7.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  45 VAKFTSSPGLSTegkrwISNLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLcFEIVKRADAGFVYSEAVA 124
Cdd:cd05072    34 VAVKTLKPGTMS-----VQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGSL-LDFLKSDEGGKVLLPKLI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 125 ShYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGGFGVAIQLGESGLVAGGRVGTP-HFMAPEVVKREPYG 203
Cdd:cd05072   108 D-FSAQIAEGMAYIERKNYIHRDLRAANVLVS---ESLMCKIADFGLARVIEDNEYTAREGAKFPiKWTAPEAINFGSFT 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039796143 204 KPVDVWGCGVILF-ILLSGCLPFYGTKERLFEGIIKGKYKMnPR 246
Cdd:cd05072   184 IKSDVWSFGILLYeIVTYGKIPYPGMSNSDVMSALQRGYRM-PR 226
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
16-244 7.21e-09

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: 57.99  E-value: 7.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPF-SVVRRCI---NRETGQQFAVKIVDvakftsspglSTEGKRWISNLKREASICHMLKHPHIVELLETYSSDG 91
Cdd:cd05080    10 RDLGEGHFgKVSLYCYdptNDGTGEMVAVKALK----------ADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 --MLYMVFEFMDGADLCFEIVKRAdagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGF 169
Cdd:cd05080    80 gkSLQLIMEYVPLGSLRDYLPKHS-----IGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLL---DNDRLVKIGDF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 170 GVAIQLGESGLVAggRVG----TPHF-MAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMN 244
Cdd:cd05080   152 GLAKAVPEGHEYY--RVRedgdSPVFwYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQSPPTKFLEMIGIAQGQMT 229
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
128-282 7.30e-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: 7.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 128 MRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLGGFGVAIQLgesglvaggRVGT----------PHFMAPEV- 196
Cdd:cd14013   126 MRQILVALRKLHSTGIVHRDVKPQNIIVSEGDGQ--FKIIDLGAAADL---------RIGInyipkeflldPRYAPPEQy 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 197 -----VKREP--------------YGKP--VDVWGCGVilfILLSGCLPfygtKERLFEGIIKGKYKMNPRQW------- 248
Cdd:cd14013   195 imstqTPSAPpapvaaalspvlwqMNLPdrFDMYSAGV---ILLQMAFP----NLRSDSNLIAFNRQLKQCDYdlnawrm 267
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039796143 249 ---SHISESAK--------------DLVRRMLMLDPAERITVYEALNHPWL 282
Cdd:cd14013   268 lvePRASADLRegfeildlddgagwDLVTKLIRYKPRGRLSASAALAHPYF 318
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
10-230 7.33e-09

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 58.56  E-value: 7.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  10 DVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakfTSSPGLSTEGKRWISNLKReasichmlkhphivelLETYSS 89
Cdd:cd14227    15 NTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKIL-----KNHPSYARQGQIEVSILAR----------------LSTESA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  90 DGM----LYMVFEFMDGADLCFEIVKRADAGFVYSEAVAS---HYMRQILE----ALRYCHDNNIIHRDVKPHCVLLASK 158
Cdd:cd14227    74 DDYnfvrAYECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPlplKYIRPILQqvatALMKLKSLGLIHADLKPENIMLVDP 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039796143 159 ENSA-PVKLGGFGVAIQLGESglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE 230
Cdd:cd14227   154 SRQPyRVKVIDFGSASHVSKA--VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASE 224
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
16-278 7.86e-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: 57.45  E-value: 7.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQQFAVKivdvakfTSSPGLSTEGKRwisNLKREASICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd05041     1 EKIGRGNFGDVYRGVLKPDNTEVAVK-------TCRETLPPDLKR---KFLQEARILKQYDHPNIVKLIGVCVQKQPIMI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLCFEIVKRADAGFVyseavaSHYMRQILEA---LRYCHDNNIIHRDVKP-HCvlLASKENSapVKLGGFGV 171
Cdd:cd05041    71 VMELVPGGSLLTFLRKKGARLTV------KQLLQMCLDAaagMEYLESKNCIHRDLAArNC--LVGENNV--LKISDFGM 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 172 AIQlGESGL--VAGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYG-TKERLFEGIIKGkYKMNPr 246
Cdd:cd05041   141 SRE-EEDGEytVSDGLKQIPiKWTAPEALNYGRYTSESDVWSFGILLWeIFSLGATPYPGmSNQQTREQIESG-YRMPA- 217
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039796143 247 qwshiSESAKDLVRRMLML----DPAERITVYEALN 278
Cdd:cd05041   218 -----PELCPEAVYRLMLQcwayDPENRPSFSEIYN 248
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
65-225 1.09e-08

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: 57.69  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  65 LKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMD-GAdlCFEIVKRAdagFVY--SEAVASHYMRQILEALRYCHDN 141
Cdd:cd08216    46 LQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAyGS--CRDLLKTH---FPEglPELAIAFILRDVLNALEYIHSK 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 142 NIIHRDVKPHCVLLASkenSAPVKLGGFGVAIQLGESglvaGGRVGTPHF-----------MAPEVVKR--EPYGKPVDV 208
Cdd:cd08216   121 GYIHRSVKASHILISG---DGKVVLSGLRYAYSMVKH----GKRQRVVHDfpksseknlpwLSPEVLQQnlLGYNEKSDI 193
                         170
                  ....*....|....*..
gi 1039796143 209 WGCGVILFILLSGCLPF 225
Cdd:cd08216   194 YSVGITACELANGVVPF 210
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
18-250 1.09e-08

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: 57.67  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  18 IGKGPFSVVRRC----INRETGQQFAVKIVDVAKFTSSpglstegKRWISNLKREASICHML-KHPHIVELLETYSSDGM 92
Cdd:cd05099    20 LGEGCFGQVVRAeaygIDKSRPDQTVTVAVKMLKDNAT-------DKDLADLISEMELMKLIgKHKNIINLLGVCTQEGP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  93 LYMVFEFMD--------------GADLCFEIVKRADAGFVYSEAVASHYmrQILEALRYCHDNNIIHRDVKPHCVLLASK 158
Cdd:cd05099    93 LYVIVEYAAkgnlreflrarrppGPDYTFDITKVPEEQLSFKDLVSCAY--QVARGMEYLESRRCIHRDLAARNVLVTED 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 159 EnsaPVKLGGFGVAI---QLGESGLVAGGRVGTpHFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYGTK-ERLF 233
Cdd:cd05099   171 N---VMKIADFGLARgvhDIDYYKKTSNGRLPV-KWMAPEALFDRVYTHQSDVWSFGILMWeIFTLGGSPYPGIPvEELF 246
                         250
                  ....*....|....*..
gi 1039796143 234 EGIIKGKYKMNPRQWSH 250
Cdd:cd05099   247 KLLREGHRMDKPSNCTH 263
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
4-229 1.43e-08

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 56.88  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   4 DDVLFEDVyELceviGKGPFSVVRRCINRETGQQFAVKIvDVAKFTSSPGLSTEgkrwisnLKREASICHMLKHPHIVEL 83
Cdd:cd05115     3 DNLLIDEV-EL----GSGNFGCVKKGVYKMRKKQIDVAI-KVLKQGNEKAVRDE-------MMREAQIMHQLDNPYIVRM 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  84 LETYSSDGMLyMVFEFMDGADLCFEIVKRADAgfVYSEAVAsHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAP 163
Cdd:cd05115    70 IGVCEAEALM-LVMEMASGGPLNKFLSGKKDE--ITVSNVV-ELMHQVSMGMKYLEEKNFVHRDLAARNVLLV---NQHY 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 164 VKLGGFGVAIQLGESGLVAGGRVGTP---HFMAPEVVKREPYGKPVDVWGCGVILFILLSgclpfYGTK 229
Cdd:cd05115   143 AKISDFGLSKALGADDSYYKARSAGKwplKWYAPECINFRKFSSRSDVWSYGVTMWEAFS-----YGQK 206
SH3_GRB2_C cd11949
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical ...
599-657 1.60e-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: 1.60e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039796143 599 YVRAQFEYDPAKDDlipckEAGirFRVGDIIQIISKDDHNWWQGKLenskNGTAGLIPS 657
Cdd:cd11949     1 YVQALFDFDPQEDG-----ELG--FRRGDFIEVMDNSDPNWWKGAC----HGQTGMFPR 48
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
62-250 2.11e-08

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 56.95  E-value: 2.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  62 ISNLKREASICHML-KHPHIVELLETYSSDGMLYMVFEFMD--------------GADLCFEIVKRADAGFVYSEAVASH 126
Cdd:cd05100    61 LSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYVLVEYASkgnlreylrarrppGMDYSFDTCKLPEEQLTFKDLVSCA 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 127 YmrQILEALRYCHDNNIIHRDVKPHCVLLaSKENSapVKLGGFGVAI---QLGESGLVAGGRVGTpHFMAPEVVKREPYG 203
Cdd:cd05100   141 Y--QVARGMEYLASQKCIHRDLAARNVLV-TEDNV--MKIADFGLARdvhNIDYYKKTTNGRLPV-KWMAPEALFDRVYT 214
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1039796143 204 KPVDVWGCGVILF-ILLSGCLPFYGTK-ERLFEGIIKGKYKMNPRQWSH 250
Cdd:cd05100   215 HQSDVWSFGVLLWeIFTLGGSPYPGIPvEELFKLLKEGHRMDKPANCTH 263
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
16-245 2.11e-08

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB 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: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 56.42  E-value: 2.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQqfavKIVDVAKFTSSPGLSTEGKRwisNLKREASICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd05065    10 EVIGAGEFGEVCRGRLKLPGK----REIFVAIKTLKSGYTEKQRR---DFLSEASIMGQFDHPNIIHLEGVVTKSRPVMI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLCfEIVKRADAGFVYSEAVAshYMRQILEALRYCHDNNIIHRDVKPHCVLLaskeNSAPV-KLGGFGVAIQ 174
Cdd:cd05065    83 ITEFMENGALD-SFLRQNDGQFTVIQLVG--MLRGIAAGMKYLSEMNYVHRDLAARNILV----NSNLVcKVSDFGLSRF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 175 LGE--------SGLvaGGRVGTpHFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYGTKERLFEGIIKGKYKMNP 245
Cdd:cd05065   156 LEDdtsdptytSSL--GGKIPI-RWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWDMSNQDVINAIEQDYRLPP 232
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
64-270 2.18e-08

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: 56.51  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  64 NLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADL--CFEIVKRADAGFVYSEAVASH--------------- 126
Cdd:cd05045    49 DLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLrsFLRESRKVGPSYLGSDGNRNSsyldnpderaltmgd 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 127 ---YMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESGLV---AGGRVGTpHFMAPEVVKRE 200
Cdd:cd05045   129 lisFAWQISRGMQYLAEMKLVHRDLAARNVLVAEGRK---MKISDFGLSRDVYEEDSYvkrSKGRIPV-KWMAIESLFDH 204
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039796143 201 PYGKPVDVWGCGVILFILLS-GCLPFYG-TKERLFEgIIKGKYKMNprQWSHISESAKDLVRRMLMLDPAER 270
Cdd:cd05045   205 IYTTQSDVWSFGVLLWEIVTlGGNPYPGiAPERLFN-LLKTGYRME--RPENCSEEMYNLMLTCWKQEPDKR 273
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
12-230 2.26e-08

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 57.02  E-value: 2.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakfTSSPGLSTEGKRWISNLKREASichmlKHPHIVELLETYSsdg 91
Cdd:cd14228    17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKIL-----KNHPSYARQGQIEVSILSRLSS-----ENADEYNFVRSYE--- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 mlymVFEFMDGADLCFEIVKRADAGFVYSEAVAS---HYMRQILE----ALRYCHDNNIIHRDVKPHCVLLASK-ENSAP 163
Cdd:cd14228    84 ----CFQHKNHTCLVFEMLEQNLYDFLKQNKFSPlplKYIRPILQqvatALMKLKSLGLIHADLKPENIMLVDPvRQPYR 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 164 VKLGGFGVAIQLGESglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE 230
Cdd:cd14228   160 VKVIDFGSASHVSKA--VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASE 224
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
601-657 2.30e-08

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


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 50.66  E-value: 2.30e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039796143 601 RAQFEYDPAKDDLIPckeagirFRVGDIIQIISKDDHNWWQGKLensKNGTAGLIPS 657
Cdd:pfam00018   1 VALYDYTAQEPDELS-------FKKGDIIIVLEKSEDGWWKGRN---KGGKEGLIPS 47
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
59-227 2.83e-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: 56.17  E-value: 2.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  59 KRWiSNLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKR---ADAGFVYSE--AVAS-------- 125
Cdd:cd05090    49 QQW-NEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLHEFLIMRsphSDVGCSSDEdgTVKSsldhgdfl 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 126 HYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQLGESGL--VAGGRVGTPHFMAPEVVKREPYG 203
Cdd:cd05090   128 HIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLH---VKISDLGLSREIYSSDYyrVQNKSLLPIRWMPPEAIMYGKFS 204
                         170       180
                  ....*....|....*....|....*
gi 1039796143 204 KPVDVWGCGVILFILLS-GCLPFYG 227
Cdd:cd05090   205 SDSDIWSFGVVLWEIFSfGLQPYYG 229
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
16-226 2.96e-08

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 55.75  E-value: 2.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRCINRETGQqfavKIVDVAKFTSSPGLsTEGKRwiSNLKREASICHMLKHPHIVELLETYSSDGMLYM 95
Cdd:cd05063    11 KVIGAGEFGEVFRGILKMPGR----KEVAVAIKTLKPGY-TEKQR--QDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  96 VFEFMDGADLCfEIVKRADAGFVYSEAVAshYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQL 175
Cdd:cd05063    84 ITEYMENGALD-KYLRDHDGEFSSYQLVG--MLRGIAAGMKYLSDMNYVHRDLAARNILV---NSNLECKVSDFGLSRVL 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796143 176 GE----SGLVAGGRVGTpHFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFY 226
Cdd:cd05063   158 EDdpegTYTTSGGKIPI-RWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPYW 212
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
8-222 3.66e-08

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: 56.10  E-value: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143   8 FEDVYeLCEVIGKGPFSVVRRCINRETGQQF--AVKIVdvakftsSPGLSTEGKrwiSNLKREASICHMLKHPHIVELLE 85
Cdd:cd05096    18 FGEVH-LCEVVNPQDLPTLQFPFNVRKGRPLlvAVKIL-------RPDANKNAR---NDFLKEVKILSRLKDPNIIRLLG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  86 TYSSDGMLYMVFEFMDGADL---------------CFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKP 150
Cdd:cd05096    87 VCVDEDPLCMITEYMENGDLnqflsshhlddkeenGNDAVPPAHCLPAISYSSLLHVALQIASGMKYLSSLNFVHRDLAT 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039796143 151 HCVLLASKENsapVKLGGFGVAIQL--GESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGC 222
Cdd:cd05096   167 RNCLVGENLT---IKIADFGMSRNLyaGDYYRIQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEILMLC 237
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
12-226 4.11e-08

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 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: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 56.19  E-value: 4.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  12 YELCEVIGKGPFSVVRRCINRETGQQFAVKIVdvakfTSSPGLSTEGKRWISNLKREASicHMLKHPHIVELLETYSSDG 91
Cdd:cd14229     2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKIL-----KNHPSYARQGQIEVGILARLSN--ENADEFNFVRAYECFQHRN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  92 MLYMVFEFMDGAdlCFEIVKRADAGFVYSEAVAShYMRQILEALRYCHDNNIIHRDVKPHCVLLASK-ENSAPVKLGGFG 170
Cdd:cd14229    75 HTCLVFEMLEQN--LYDFLKQNKFSPLPLKVIRP-ILQQVATALKKLKSLGLIHADLKPENIMLVDPvRQPYRVKVIDFG 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039796143 171 VAIQLGESglVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGcLPFY 226
Cdd:cd14229   152 SASHVSKT--VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG-WPLY 204
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
16-222 4.98e-08

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, 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 TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 55.46  E-value: 4.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  16 EVIGKGPFSVVRRC-INRETGQQF---AVKIVDVAKFTSspglstegkrWisnlKREASICHM--LKHPHIVE------- 82
Cdd:cd14055     1 KLVGKGRFAEVWKAkLKQNASGQYetvAVKIFPYEEYAS----------W----KNEKDIFTDasLKHENILQfltaeer 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  83 ---------LLETYSSDGML--YMVFEFMDGADLCfEIVKRADAGFVY--SEAVAShymrqilealrYCHDNNIIHRDVK 149
Cdd:cd14055    67 gvgldrqywLITAYHENGSLqdYLTRHILSWEDLC-KMAGSLARGLAHlhSDRTPC-----------GRPKIPIAHRDLK 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 150 PHCVLLASKENSApvkLGGFGVAIQLGES----GLVAGGRVGTPHFMAPEVVKR-------EPYgKPVDVWGCGVILFIL 218
Cdd:cd14055   135 SSNILVKNDGTCV---LADFGLALRLDPSlsvdELANSGQVGTARYMAPEALESrvnledlESF-KQIDVYSMALVLWEM 210

                  ....
gi 1039796143 219 LSGC 222
Cdd:cd14055   211 ASRC 214
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
17-222 5.63e-08

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 55.28  E-value: 5.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  17 VIGKGPFSVVRRC----INRETGQQFAVKivdvakftsspGLSTEGKRWISNLKREASICHMLKHPHIVELLETYSSDGM 92
Cdd:cd05081    11 QLGKGNFGSVELCrydpLGDNTGALVAVK-----------QLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  93 --LYMVFEFMDGADLcFEIVKRADAGFVYSEAVAshYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFG 170
Cdd:cd05081    80 rsLRLVMEYLPSGCL-RDFLQRHRARLDASRLLL--YSSQICKGMEYLGSRRCVHRDLAARNILVESEAH---VKIADFG 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039796143 171 VA--IQLGESGLVAGGRVGTPHF-MAPEVVKREPYGKPVDVWGCGVILFILLSGC 222
Cdd:cd05081   154 LAklLPLDKDYYVVREPGQSPIFwYAPESLSDNIFSRQSDVWSFGVVLYELFTYC 208
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
63-246 5.69e-08

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 55.43  E-value: 5.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143  63 SNLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLC-FEIVKRADAGFV--------YSEAVASHYMRQILE 133
Cdd:cd05093    52 KDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNkFLRAHGPDAVLMaegnrpaeLTQSQMLHIAQQIAA 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039796143 134 ALRYCHDNNIIHRDVKPHCVLLAskENSApVKLGGFGVAIQLGESGLV-AGGRVGTP-HFMAPEVVKREPYGKPVDVWGC 211
Cdd:cd05093   132 GMVYLASQHFVHRDLATRNCLVG--ENLL-VKIGDFGMSRDVYSTDYYrVGGHTMLPiRWMPPESIMYRKFTTESDVWSL 208
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1039796143 212 GVILF-ILLSGCLPFYG-TKERLFEGIIKGKYKMNPR 246
Cdd:cd05093   209 GVVLWeIFTYGKQPWYQlSNNEVIECITQGRVLQRPR 245
 
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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