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Conserved domains on  [gi|528504250|ref|XP_005158227|]
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casein kinase II subunit alpha isoform X1 [Danio rerio]

Protein Classification

casein kinase II subunit alpha/alpha'( domain architecture ID 10197591)

casein kinase II subunit alpha/alpha' is the catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
20-325 0e+00

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: 599.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  20 PREYWDYESHVVDWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLLD 99
Cdd:cd14132    1 PPEYWDYENLNVEWGSQDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKPVKKKKIKREIKILQNLRGGPNIVKLLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 100 IIKDPVSRTPALVFEHVNNTDFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLA 179
Cdd:cd14132   81 VVKDPQSKTPSLIFEYVNNTDFKTLYPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRKLRLIDWGLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 180 EFYHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYID 259
Cdd:cd14132  161 EFYHPGQEYNVRVASRYYKGPELLVDYQYYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVKIAKVLGTDDLYAYLD 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 260 KYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYFY 325
Cdd:cd14132  241 KYGIELPPRLNDILGRHSKKPWERFVNSENQHLVTPEALDLLDKLLRYDHQERITAKEAMQHPYFD 306
 
Name Accession Description Interval E-value
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
20-325 0e+00

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: 599.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  20 PREYWDYESHVVDWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLLD 99
Cdd:cd14132    1 PPEYWDYENLNVEWGSQDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKPVKKKKIKREIKILQNLRGGPNIVKLLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 100 IIKDPVSRTPALVFEHVNNTDFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLA 179
Cdd:cd14132   81 VVKDPQSKTPSLIFEYVNNTDFKTLYPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRKLRLIDWGLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 180 EFYHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYID 259
Cdd:cd14132  161 EFYHPGQEYNVRVASRYYKGPELLVDYQYYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVKIAKVLGTDDLYAYLD 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 260 KYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYFY 325
Cdd:cd14132  241 KYGIELPPRLNDILGRHSKKPWERFVNSENQHLVTPEALDLLDKLLRYDHQERITAKEAMQHPYFD 306
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
39-324 1.53e-63

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 203.92  E-value: 1.53e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250    39 YQLVRKLGRGKYSEVFEAINITNNEK----VVVKILKPVKKKKIKREIKILENLRGgPNIITLLDIIKDPVSRTpaLVFE 114
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLvaikVIKKKKIKKDRERILREIKILKKLKH-PNIVRLYDVFEDEDKLY--LVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250   115 HVNNTDFKQL---YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHPNQEYNVR 191
Cdd:smart00220  78 YCEGGDLFDLlkkRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH-VKLADFGLARQLDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250   192 VASRYFKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPFfhghDNYDQLVRIAKVLGTEDLYDYIDKYNIeldprfnd 271
Cdd:smart00220 157 VGTPEYMAPEVL-LGKGYGKAVDIWSLGVILYELLTGKPPF----PGDDQLLELFKKIGKPKPPFPPPEWDI-------- 223
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 528504250   272 ilgrhsrkrwerfvhsenqhlvSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:smart00220 224 ----------------------SPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
39-324 1.97e-41

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 145.46  E-value: 1.97e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250   39 YQLVRKLGRGKYSEVFEAINITNNEK-----VVVKILKPVKKKKIKREIKILENLRGgPNIITLLDIIKDPVSRTpaLVF 113
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIvaikkIKKEKIKKKKDKNILREIKILKKLNH-PNIVRLYDAFEDKDNLY--LVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  114 EHVNNTDFKQLYQ---TLSDYDIRFYMYEILKALDychsmgimhrdvkphnvmidhehrklrlidwglaefyhPNQEYNV 190
Cdd:pfam00069  78 EYVEGGSLFDLLSekgAFSEREAKFIMKQILEGLE--------------------------------------SGSSLTT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  191 RVASRYFKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNydqlvriakvlgtedlydyiDKYNIELDprfn 270
Cdd:pfam00069 120 FVGTPWYMAPEVL-GGNPYGPKVDVWSLGCILYELLTGKPPFPGINGN--------------------EIYELIID---- 174
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528504250  271 dilgrhsrkrwERFVHSENQHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:pfam00069 175 -----------QPYAFPELPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
37-324 4.84e-38

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 138.80  E-value: 4.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKK-----KKIKREIKILENLRGGpNIITLLDIIKDpvSRTPAL 111
Cdd:PLN00009   2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEdegvpSTAIREISLLKEMQHG-NIVRLQDVVHS--EKRLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 VFEHVNnTDFKQLYQTLSDYD-----IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAE-FYHPN 185
Cdd:PLN00009  79 VFEYLD-LDLKKHMDSSPDFAknprlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNALKLADFGLARaFGIPV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 186 QEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIel 265
Cdd:PLN00009 158 RTFTHEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQK-PLFPGDSEIDELFKIFRILGTPNEETWPGVTSL-- 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528504250 266 dPRFNDILGRHSRKRWERFVHSenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:PLN00009 235 -PDYKSAFPKWPPKDLATVVPT-----LEPAGVDLLSKMLRLDPSKRITARAALEHEYF 287
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
37-395 3.07e-26

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 109.72  E-value: 3.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRKLGRGKYSEVFEAINITNNEK------VVVKILKPVKKKKIKREIKILENLRGgPNIITLLDIIKDpvSRTPA 110
Cdd:COG0515    7 GRYRILRLLGRGGMGVVYLARDLRLGRPvalkvlRPELAADPEARERFRREARALARLNH-PNIVRVYDVGEE--DGRPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFKQLYQT---LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHPNQ- 186
Cdd:COG0515   84 LVMEYVEGESLADLLRRrgpLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGR-VKLIDFGIARALGGATl 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 187 -EYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPfFHGHDNYDQLVRIAkvlgtEDLYDYIDKYNIEL 265
Cdd:COG0515  163 tQTGTVVGTPGYMAPEQARG-EPVDPRSDVYSLGVTLYELLTGRPP-FDGDSPAELLRAHL-----REPPPPPSELRPDL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 266 DPRFNDILGR-HSRKRWERFvhsenqhlvsTEALDFLDKLLRYDHQ--ARLTAREAMDHSYFYPIVKDQGRGAPAAGMAA 342
Cdd:COG0515  236 PPALDAIVLRaLAKDPEERY----------QSAAELAAALRAVLRSlaAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 305
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528504250 343 SSTPVSSSSLMAGIASMTPSTQPNIANISAGSPVIPAPNTMATQVPTAAGAQP 395
Cdd:COG0515  306 AAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAAL 358
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
136-167 2.15e-09

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 59.04  E-value: 2.15e-09
                         10        20        30
                 ....*....|....*....|....*....|..
gi 528504250 136 YMYEILKALDYCHSMGIMHRDVKPHNVMIDHE 167
Cdd:NF033483 112 IMIQILSALEHAHRNGIVHRDIKPQNILITKD 143
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
92-178 4.55e-09

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: 58.32  E-value: 4.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250    92 PNIITLLDIIKDPVSRTPAlVFEHVNNTDFKQLYQT---LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMI---- 164
Cdd:TIGR03903   38 PNIVALLDSGEAPPGLLFA-VFEYVPGRTLREVLAAdgaLPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVsqtg 116
                           90
                   ....*....|....
gi 528504250   165 DHEHRKlrLIDWGL 178
Cdd:TIGR03903  117 VRPHAK--VLDFGI 128
 
Name Accession Description Interval E-value
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
20-325 0e+00

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: 599.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  20 PREYWDYESHVVDWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLLD 99
Cdd:cd14132    1 PPEYWDYENLNVEWGSQDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKPVKKKKIKREIKILQNLRGGPNIVKLLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 100 IIKDPVSRTPALVFEHVNNTDFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLA 179
Cdd:cd14132   81 VVKDPQSKTPSLIFEYVNNTDFKTLYPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRKLRLIDWGLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 180 EFYHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYID 259
Cdd:cd14132  161 EFYHPGQEYNVRVASRYYKGPELLVDYQYYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVKIAKVLGTDDLYAYLD 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 260 KYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYFY 325
Cdd:cd14132  241 KYGIELPPRLNDILGRHSKKPWERFVNSENQHLVTPEALDLLDKLLRYDHQERITAKEAMQHPYFD 306
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
39-324 5.04e-74

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: 230.97  E-value: 5.04e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVV--VKILKPVKKKKIKREIKILENLR---GGPNIITLLDIIKDPVSRTPALVF 113
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAikKIKNDFRHPKAALREIKLLKHLNdveGHPNIVKLLDVFEHRGGNHLCLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 114 EHVNnTDFKQLYQT----LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPnQEYN 189
Cdd:cd05118   81 ELMG-MNLYELIKDyprgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQLKLADFGLARSFTS-PPYT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 190 VRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRkEPFFHGHDNYDQLVRIAKVLGTEdlydyidkynieldprf 269
Cdd:cd05118  159 PYVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTG-RPLFPGDSEVDQLAKIVRLLGTP----------------- 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 270 ndilgrhsrkrwerfvhsenqhlvstEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd05118  221 --------------------------EALDLLSKMLKYDPAKRITASQALAHPYF 249
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
39-324 1.53e-63

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 203.92  E-value: 1.53e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250    39 YQLVRKLGRGKYSEVFEAINITNNEK----VVVKILKPVKKKKIKREIKILENLRGgPNIITLLDIIKDPVSRTpaLVFE 114
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLvaikVIKKKKIKKDRERILREIKILKKLKH-PNIVRLYDVFEDEDKLY--LVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250   115 HVNNTDFKQL---YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHPNQEYNVR 191
Cdd:smart00220  78 YCEGGDLFDLlkkRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH-VKLADFGLARQLDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250   192 VASRYFKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPFfhghDNYDQLVRIAKVLGTEDLYDYIDKYNIeldprfnd 271
Cdd:smart00220 157 VGTPEYMAPEVL-LGKGYGKAVDIWSLGVILYELLTGKPPF----PGDDQLLELFKKIGKPKPPFPPPEWDI-------- 223
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 528504250   272 ilgrhsrkrwerfvhsenqhlvSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:smart00220 224 ----------------------SPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
39-324 2.97e-60

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: 196.55  E-value: 2.97e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVKILKpvkkkkikreikiLENLRGG-----------------PNIITLLDII 101
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIR-------------LDNEEEGipstalreisllkelkhPNIVKLLDVI 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 102 KDPvsRTPALVFEHVNNtDFKQL----YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEhRKLRLIDWG 177
Cdd:cd07829   68 HTE--NKLYLVFEYCDQ-DLKKYldkrPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRD-GVLKLADFG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 178 LA-EFYHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIfRKEPFFHGHDNYDQLVRIAKVLGT--EDL 254
Cdd:cd07829  144 LArAFGIPLRTYTHEVVTLWYRAPEILLGSKHYSTAVDIWSVGCIFAELI-TGKPLFPGDSEIDQLFKIFQILGTptEES 222
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 255 YDYIDKYnieldPRFNDILGRHSRKRWERFVHSENQhlvstEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07829  223 WPGVTKL-----PDYKPTFPKWPKNDLEKVLPRLDP-----EGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
92-324 1.90e-54

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: 181.55  E-value: 1.90e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTP----ALVFEHVNNT------DFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHN 161
Cdd:cd14137   57 PNIVKLKYFFYSSGEKKDevylNLVMEYMPETlyrvirHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQN 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 162 VMIDHEHRKLRLIDWGLAEFYHPNQEyNVR-VASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIfRKEPFFHGHDNYD 240
Cdd:cd14137  137 LLVDPETGVLKLCDFGSAKRLVPGEP-NVSyICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELL-LGQPLFPGESSVD 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 241 QLVRIAKVLGT---EDLYDYIDKYnieLDPRFNDIlgrhSRKRWERFVHsenqHLVSTEALDFLDKLLRYDHQARLTARE 317
Cdd:cd14137  215 QLVEIIKVLGTptrEQIKAMNPNY---TEFKFPQI----KPHPWEKVFP----KRTPPDAIDLLSKILVYNPSKRLTALE 283

                 ....*..
gi 528504250 318 AMDHSYF 324
Cdd:cd14137  284 ALAHPFF 290
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
38-325 9.71e-53

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: 177.14  E-value: 9.71e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  38 DYQLVRKLGRGKYSEVFEAINITNNEK-----VVVKILKPVKKKKIKREIKILENLRGGPNIITLLDIIKDPVSRTpaLV 112
Cdd:cd07832    1 RYKILGRIGEGAHGIVFKAKDRETGETvalkkVALRKLEGGIPNQALREIKALQACQGHPYVVKLRDVFPHGTGFV--LV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 113 FEHVNNTdfkqLYQTLSDYD-------IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPN 185
Cdd:cd07832   79 FEYMLSS----LSEVLRDEErplteaqVKRYMRMLLKGVAYMHANRIMHRDLKPANLLIS-STGVLKIADFGLARLFSEE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 186 QE--YNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIfRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNI 263
Cdd:cd07832  154 DPrlYSHQVATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELL-NGSPLFPGENDIEQLAIVLRTLGTPNEKTWPELTSL 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528504250 264 eldPRFNDILGRHS-RKRWERFVHSEnqhlvSTEALDFLDKLLRYDHQARLTAREAMDHSYFY 325
Cdd:cd07832  233 ---PDYNKITFPESkGIRLEEIFPDC-----SPEAIDLLKGLLVYNPKKRLSAEEALRHPYFF 287
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
39-324 8.18e-51

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: 172.36  E-value: 8.18e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVKILKpvkkkkikreikiLENLRGG-----------------PNIITLLDII 101
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIR-------------MENEKEGfpitaireikllqkldhPNVVRLKEIV 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 102 kdpVSRTPA-------LVFEHVNNtDFKQL----YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRk 170
Cdd:cd07840   68 ---TSKGSAkykgsiyMVFEYMDH-DLTGLldnpEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGV- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 171 LRLIDWGLAEFYHP--NQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKV 248
Cdd:cd07840  143 LKLADFGLARPYTKenNADYTNRVITLWYRPPELLLGATRYGPEVDMWSVGCILAEL-FTGKPIFQGKTELEQLEKIFEL 221
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 249 LG--TEDLYDYIDKYnieldPRFNDILGRHSRKRWERFVHSenqHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07840  222 CGspTEENWPGVSDL-----PWFENLKPKKPYKRRLREVFK---NVIDPSALDLLDKLLTLDPKKRISADQALQHEYF 291
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
92-324 5.31e-50

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: 170.19  E-value: 5.31e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKdpVSRTPALVFEHVNNTDFKQL--YQTLSDYD-IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEH 168
Cdd:cd07833   60 ENIVNLKEAFR--RKGRLYLVFEYVERTLLELLeaSPGGLPPDaVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVS-ES 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 RKLRLIDWGLAEFYH--PNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIfRKEPFFHGHDNYDQLVRIA 246
Cdd:cd07833  137 GVLKLCDFGFARALTarPASPLTDYVATRWYRAPELLVGDTNYGKPVDVWAIGCIMAELL-DGEPLFPGDSDIDQLYLIQ 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 247 KVLGTedlydyIDKYNIEL---DPRFN-----DILGRHSRKRweRFvhsenQHLVSTEALDFLDKLLRYDHQARLTAREA 318
Cdd:cd07833  216 KCLGP------LPPSHQELfssNPRFAgvafpEPSQPESLER--RY-----PGKVSSPALDFLKACLRMDPKERLTCDEL 282

                 ....*.
gi 528504250 319 MDHSYF 324
Cdd:cd07833  283 LQHPYF 288
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
92-324 9.85e-46

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: 160.00  E-value: 9.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTpalvFEHVN------NTDFKQLY---QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:cd07834   59 ENIIGLLDILRPPSPEE----FNDVYivtelmETDLHKVIkspQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNI 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 163 MIDHEHrKLRLIDWGLAEFYHPNQ------EYnvrVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGH 236
Cdd:cd07834  135 LVNSNC-DLKICDFGLARGVDPDEdkgfltEY---VVTRWYRAPELLLSSKKYTKAIDIWSVGCIFAELLTRK-PLFPGR 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 237 DNYDQLVRIAKVLGT---EDLyDYIDKYNIeldPRFNDILGRHSRKRWERFVhsenqHLVSTEALDFLDKLLRYDHQARL 313
Cdd:cd07834  210 DYIDQLNLIVEVLGTpseEDL-KFISSEKA---RNYLKSLPKKPKKPLSEVF-----PGASPEAIDLLEKMLVFNPKKRI 280
                        250
                 ....*....|.
gi 528504250 314 TAREAMDHSYF 324
Cdd:cd07834  281 TADEALAHPYL 291
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
92-324 9.92e-46

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: 159.27  E-value: 9.92e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDII--KDPVSrtpaLVFEHVNnTDFKQLYQ----TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMID 165
Cdd:cd07841   62 PNIIGLLDVFghKSNIN----LVFEFME-TDLEKVIKdksiVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIA 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 166 hEHRKLRLIDWGLAEFY-HPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQLVR 244
Cdd:cd07841  137 -SDGVLKLADFGLARSFgSPNRKMTHQVVTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRV-PFLPGDSDIDQLGK 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 245 IAKVLGT--ED-------LYDYIdKYNIELDPRFNDIlgrhsrkrwerFVHsenqhlVSTEALDFLDKLLRYDHQARLTA 315
Cdd:cd07841  215 IFEALGTptEEnwpgvtsLPDYV-EFKPFPPTPLKQI-----------FPA------ASDDALDLLQRLLTLNPNKRITA 276

                 ....*....
gi 528504250 316 REAMDHSYF 324
Cdd:cd07841  277 RQALEHPYF 285
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
92-324 1.77e-45

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: 157.84  E-value: 1.77e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDpvSRTPALVFEHVNnTDFKQLYQTLSDYD-----IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDH 166
Cdd:cd07835   58 PNIVRLLDVVHS--ENKLYLVFEFLD-LDLKKYMDSSPLTGldpplIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDT 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 167 EHrKLRLIDWGLAE-FYHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQLVRI 245
Cdd:cd07835  135 EG-ALKLADFGLARaFGVPVRTYTHEVVTLWYRAPEILLGSKHYSTPVDIWSVGCIFAEMVTRR-PLFPGDSEIDQLFRI 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 246 AKVLGT--EDLYDYIDKYnieldPRFNDILGRHSRKRWERFVHSenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd07835  213 FRTLGTpdEDVWPGVTSL-----PDYKPTFPKWARQDLSKVVPS-----LDEDGLDLLSQMLVYDPAKRISAKAALQHPY 282

                 .
gi 528504250 324 F 324
Cdd:cd07835  283 F 283
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
39-324 3.47e-45

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: 157.05  E-value: 3.47e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEK----VVVKILKPVKKKKIKREIKILENLRGGPNIITLLDIIKDPVSRTPALVFE 114
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSRKTGKYyaikCMKKHFKSLEQVNNLREIQALRRLSPHPNILRLIEVLFDRKTGRLALVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 115 --HVNNTDF-KQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrkLRLIDWGLAEFYHPNQEYNVR 191
Cdd:cd07831   81 lmDMNLYELiKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDI--LKLADFGSCRGIYSKPPYTEY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 192 VASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQLVRIAKVLGTEDLydyidkyniELDPRFnd 271
Cdd:cd07831  159 ISTRWYRAPECLLTDGYYGPKMDIWAVGCVFFEILSLF-PLFPGTNELDQIAKIHDVLGTPDA---------EVLKKF-- 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528504250 272 ilgRHSRKRWERFVHSENQ------HLVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07831  227 ---RKSRHMNYNFPSKKGTglrkllPNASAEGLDLLKKLLAYDPDERITAKQALRHPYF 282
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
39-323 5.46e-43

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: 152.94  E-value: 5.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREI-------KILENLRGGPNIITLLDI-IKDPVSRTPA 110
Cdd:cd07857    2 YELIKELGQGAYGIVCSARNAETSEEETVAIKKITNVFSKKILAkralrelKLLRHFRGHKNITCLYDMdIVFPGNFNEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFKQLY---QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYHPNQE 187
Cdd:cd07857   82 YLYEELMEADLHQIIrsgQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADC-ELKICDFGLARGFSENPG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 188 YNVR-----VASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQLVRIAKVLGTEDlydyidkyn 262
Cdd:cd07857  161 ENAGfmteyVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGRK-PVFKGKDYVDQLNQILQVLGTPD--------- 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504250 263 ieldprfNDILGRHSRKRWERFVHSENQHL----------VSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd07857  231 -------EETLSRIGSPKAQNYIRSLPNIPkkpfesifpnANPLALDLLEKLLAFDPTKRISVEEALEHPY 294
Pkinase pfam00069
Protein kinase domain;
39-324 1.97e-41

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 145.46  E-value: 1.97e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250   39 YQLVRKLGRGKYSEVFEAINITNNEK-----VVVKILKPVKKKKIKREIKILENLRGgPNIITLLDIIKDPVSRTpaLVF 113
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIvaikkIKKEKIKKKKDKNILREIKILKKLNH-PNIVRLYDAFEDKDNLY--LVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  114 EHVNNTDFKQLYQ---TLSDYDIRFYMYEILKALDychsmgimhrdvkphnvmidhehrklrlidwglaefyhPNQEYNV 190
Cdd:pfam00069  78 EYVEGGSLFDLLSekgAFSEREAKFIMKQILEGLE--------------------------------------SGSSLTT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  191 RVASRYFKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNydqlvriakvlgtedlydyiDKYNIELDprfn 270
Cdd:pfam00069 120 FVGTPWYMAPEVL-GGNPYGPKVDVWSLGCILYELLTGKPPFPGINGN--------------------EIYELIID---- 174
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528504250  271 dilgrhsrkrwERFVHSENQHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:pfam00069 175 -----------QPYAFPELPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
39-324 6.94e-41

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: 145.75  E-value: 6.94e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEK----VVVKILKPVKKKKIKREIKILENLRGGPNIITLLDIIKDpvSRTPALVFE 114
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELvaikKMKKKFYSWEECMNLREVKSLRKLNEHPNIVKLKEVFRE--NDELYFVFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 115 HVNNTdfkqLYQTLSDYD--------IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQ 186
Cdd:cd07830   79 YMEGN----LYQLMKDRKgkpfsesvIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVS-GPEVVKIADFGLAREIRSRP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 187 EYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELD 266
Cdd:cd07830  154 PYTDYVSTRWYRAPEILLRSTSYSSPVDIWALGCIMAEL-YTLRPLFPGSSEIDQLYKICSVLGTPTKQDWPEGYKLASK 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504250 267 PRFndilgrhsrkRWERFVHSENQHLV---STEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07830  233 LGF----------RFPQFAPTSLHQLIpnaSPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
38-321 1.36e-40

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: 144.54  E-value: 1.36e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  38 DYQLVRKLGRGKYSEVFEAINITNNEKVV--VKILKPVKKKKIKREIKILENLRG--GPNIITLLDIIKDPvsRTPALVF 113
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAvkIIDKKKLKSEDEEMLRREIEILKRldHPNIVKLYEVFEDD--KNLYLVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 114 EHVNNTD-FKQL--YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHR--KLRLIDWGLAEFYHPNQEY 188
Cdd:cd05117   79 ELCTGGElFDRIvkKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPdsPIKIIDFGLAKIFEEGEKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 189 NVRVASRYFKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDnydqlvriakvlgtEDLYDYIDKYNIELDPr 268
Cdd:cd05117  159 KTVCGTPYYVAPEVL-KGKGYGKKCDIWSLGVILYILLCGYPPFYGETE--------------QELFEKILKGKYSFDS- 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528504250 269 fndilgrhsrKRWerfvhsenqHLVSTEALDFLDKLLRYDHQARLTAREAMDH 321
Cdd:cd05117  223 ----------PEW---------KNVSEEAKDLIKRLLVVDPKKRLTAAEALNH 256
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
37-324 1.49e-40

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: 144.29  E-value: 1.49e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILK--------PVKKKKIKREIKILENLRGGPNIITLLDII--KDPVs 106
Cdd:cd14019    1 NKYRIIEKIGEGTFSSVYKAEDKLHDLYDRNKGRLvalkhiypTSSPSRILNELECLERLGGSNNVSGLITAFrnEDQV- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 107 rtpALVFEHVNNTDFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYH--P 184
Cdd:cd14019   80 ---VAVLPYIEHDDFRDFYRKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKGVLVDFGLAQREEdrP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 185 NQEYNvRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYdyidkynie 264
Cdd:cd14019  157 EQRAP-RAGTRGFRAPEVLFKCPHQTTAIDIWSAGVILLSILSGRFPFFFSSDDIDALAEIATIFGSDEAY--------- 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 265 ldprfndilgrhsrkrwerfvhsenqhlvstealDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14019  227 ----------------------------------DLLDKLLELDPSKRITAEEALKHPFF 252
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
92-331 1.70e-40

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: 146.36  E-value: 1.70e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVsrtpalvfehvNNTDFKQLY-----------------QTLSDYDIRFYMYEILKALDYCHSMGIMH 154
Cdd:cd07855   64 DNIIAIRDILRPKV-----------PYADFKDVYvvldlmesdlhhiihsdQPLTLEHIRYFLYQLLRGLKYIHSANVIH 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 155 RDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYNVR-----VASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRK 229
Cdd:cd07855  133 RDLKPSNLLVN-ENCELKIGDFGMARGLCTSPEEHKYfmteyVATRWYRAPELMLSLPEYTQAIDMWSVGCIFAEMLGRR 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 230 EpFFHGHDNYDQLVRIAKVLGTEDlYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHlvsteALDFLDKLLRYDH 309
Cdd:cd07855  212 Q-LFPGKNYVHQLQLILTVLGTPS-QAVINAIGADRVRRYIQNLPNKQPVPWETLYPKADQQ-----ALDLLSQMLRFDP 284
                        250       260
                 ....*....|....*....|....
gi 528504250 310 QARLTAREAMDHSYF--YPIVKDQ 331
Cdd:cd07855  285 SERITVAEALQHPFLakYHDPDDE 308
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
85-324 2.58e-40

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: 145.78  E-value: 2.58e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  85 LENLRGGPNIITLLDIIKDPVSRTPALVFEHVNnTDFKQLYQT--LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:cd07852   60 LQELNDHPNIIKLLNVIRAENDKDIYLVFEYME-TDLHAVIRAniLEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNI 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 163 MIDHEHRkLRLIDWGLA------EFYHPNQ---EYnvrVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFF 233
Cdd:cd07852  139 LLNSDCR-VKLADFGLArslsqlEEDDENPvltDY---VATRWYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGK-PLF 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 234 HGHDNYDQLVRIAKVLGTedlydyidkynieldPRFNDILGRHSRKRW---ERFVHSENQHLV------STEALDFLDKL 304
Cdd:cd07852  214 PGTSTLNQLEKIIEVIGR---------------PSAEDIESIQSPFAAtmlESLPPSRPKSLDelfpkaSPDALDLLKKL 278
                        250       260
                 ....*....|....*....|
gi 528504250 305 LRYDHQARLTAREAMDHSYF 324
Cdd:cd07852  279 LVFNPNKRLTAEEALRHPYV 298
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
39-324 1.31e-39

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: 142.52  E-value: 1.31e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVKILKpvkkkkikreikiLENLRGGP----------------NIITLLDIIK 102
Cdd:cd07844    2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIR-------------LEHEEGAPftaireasllkdlkhaNIVTLHDIIH 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 103 dpVSRTPALVFEHVNnTDFKQLYQT----LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGL 178
Cdd:cd07844   69 --TKKTLTLVFEYLD-TDLKQYMDDcgggLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLIS-ERGELKLADFGL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 179 AEFYH-PNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIfRKEPFFHGH-DNYDQLVRIAKVLGT--EDL 254
Cdd:cd07844  145 ARAKSvPSKTYSNEVVTLWYRPPDVLLGSTEYSTSLDMWGVGCIFYEMA-TGRPLFPGStDVEDQLHKIFRVLGTptEET 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 255 YDYIDKYNIELDPRFNDILGRHSRKRWERFvhsenqhLVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07844  224 WPGVSSNPEFKPYSFPFYPPRPLINHAPRL-------DRIPHGEELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
93-324 1.35e-39

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: 144.04  E-value: 1.35e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIkdpvsrTPALVFEHVNN---------TDFKQL--YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHN 161
Cdd:cd07878   75 NVIGLLDVF------TPATSIENFNEvylvtnlmgADLNNIvkCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSN 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 162 VMIDhEHRKLRLIDWGLAEfyHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIfRKEPFFHGHDNYDQ 241
Cdd:cd07878  149 VAVN-EDCELRILDFGLAR--QADDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELL-KGKALFPGNDYIDQ 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 242 LVRIAKVLGTEDlYDYIDKYNIEldprfndilgrHSRKRWERFVHSENQHLVST------EALDFLDKLLRYDHQARLTA 315
Cdd:cd07878  225 LKRIMEVVGTPS-PEVLKKISSE-----------HARKYIQSLPHMPQQDLKKIfrganpLAIDLLEKMLVLDSDKRISA 292

                 ....*....
gi 528504250 316 REAMDHSYF 324
Cdd:cd07878  293 SEALAHPYF 301
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
92-326 3.35e-39

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: 143.20  E-value: 3.35e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIkdpvsrTPAlvfEHVNntDFKQLY----------------QTLSDYDIRFYMYEILKALDYCHSMGIMHR 155
Cdd:cd07851   74 ENVIGLLDVF------TPA---SSLE--DFQDVYlvthlmgadlnnivkcQKLSDDHIQFLVYQILRGLKYIHSAGIIHR 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 156 DVKPHNVMIDhEHRKLRLIDWGLAEfyHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHG 235
Cdd:cd07851  143 DLKPSNLAVN-EDCELKILDFGLAR--HTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGK-TLFPG 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 236 HDNYDQLVRIAKVLGT-----------EDLYDYIDKYNIELDPRFNDILGRHsrkrwerfvhsenqhlvSTEALDFLDKL 304
Cdd:cd07851  219 SDHIDQLKRIMNLVGTpdeellkkissESARNYIQSLPQMPKKDFKEVFSGA-----------------NPLAIDLLEKM 281
                        250       260
                 ....*....|....*....|..
gi 528504250 305 LRYDHQARLTAREAMDHSYFYP 326
Cdd:cd07851  282 LVLDPDKRITAAEALAHPYLAE 303
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
37-324 4.84e-38

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 138.80  E-value: 4.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKK-----KKIKREIKILENLRGGpNIITLLDIIKDpvSRTPAL 111
Cdd:PLN00009   2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEdegvpSTAIREISLLKEMQHG-NIVRLQDVVHS--EKRLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 VFEHVNnTDFKQLYQTLSDYD-----IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAE-FYHPN 185
Cdd:PLN00009  79 VFEYLD-LDLKKHMDSSPDFAknprlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNALKLADFGLARaFGIPV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 186 QEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIel 265
Cdd:PLN00009 158 RTFTHEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQK-PLFPGDSEIDELFKIFRILGTPNEETWPGVTSL-- 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528504250 266 dPRFNDILGRHSRKRWERFVHSenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:PLN00009 235 -PDYKSAFPKWPPKDLATVVPT-----LEPAGVDLLSKMLRLDPSKRITARAALEHEYF 287
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
39-324 7.26e-38

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: 138.00  E-value: 7.26e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKK----KKIKREIKILENLRGgPNIITLLDIIKdpVSRTPALVFE 114
Cdd:cd07836    2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEegtpSTAIREISLMKELKH-ENIVRLHDVIH--TENKLMLVFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 115 HVNNtDFKQLYQT------LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAE-FYHPNQE 187
Cdd:cd07836   79 YMDK-DLKKYMDThgvrgaLDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGE-LKLADFGLARaFGIPVNT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 188 YNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQLVRIAKVLGTEDLYDYIdkyNIELDP 267
Cdd:cd07836  157 FSNEVVTLWYRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGR-PLFPGTNNEDQLLKIFRIMGTPTESTWP---GISQLP 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 268 RFNDILGRHSRKRWERFVHSenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07836  233 EYKPTFPRYPPQDLQQLFPH-----ADPLGIDLLHRLLQLNPELRISAHDALQHPWF 284
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
92-324 8.80e-38

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: 137.64  E-value: 8.80e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDpvSRTPALVFEHVNNtDFKQLYQT-----LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDH 166
Cdd:cd07860   59 PNIVKLLDVIHT--ENKLYLVFEFLHQ-DLKKFMDAsaltgIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINT 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 167 EHrKLRLIDWGLAE-FYHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQLVRI 245
Cdd:cd07860  136 EG-AIKLADFGLARaFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR-ALFPGDSEIDQLFRI 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 246 AKVLGTED---------LYDYidkynieldprfndilgRHSRKRWERFVHSENQHLVSTEALDFLDKLLRYDHQARLTAR 316
Cdd:cd07860  214 FRTLGTPDevvwpgvtsMPDY-----------------KPSFPKWARQDFSKVVPPLDEDGRDLLSQMLHYDPNKRISAK 276

                 ....*...
gi 528504250 317 EAMDHSYF 324
Cdd:cd07860  277 AALAHPFF 284
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
37-324 9.12e-38

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: 138.04  E-value: 9.12e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKK-----KKIKREIKILENLRGGPNIITLLDIIKDPVSRTPAL 111
Cdd:cd07837    1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEeegvpSTALREVSLLQMLSQSIYIVRLLDVEHVEENGKPLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 --VFEHVNnTDFKQLYQT--------LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAE- 180
Cdd:cd07837   81 ylVFEYLD-TDLKKFIDSygrgphnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLLKIADLGLGRa 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 181 FYHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIfRKEPFFHGHDNYDQLVRIAKVLGTEdlydyidk 260
Cdd:cd07837  160 FTIPIKSYTHEIVTLWYRAPEVLLGSTHYSTPVDMWSVGCIFAEMS-RKQPLFPGDSELQQLLHIFRLLGTP-------- 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504250 261 yNIELDPRFNDILGRHSRKRWERFVHSENQHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07837  231 -NEEVWPGVSKLRDWHEYPQWKPQDLSRAVPDLEPEGVDLLTKMLAYDPAKRISAKAALQHPYF 293
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
92-324 1.17e-37

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: 137.56  E-value: 1.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTpaLVFEHVNNtDFKQLYQTLSDY----DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhE 167
Cdd:cd07839   59 KNIVRLYDVLHSDKKLT--LVFEYCDQ-DLKKYFDSCNGDidpeIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLIN-K 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 168 HRKLRLIDWGLAEFYH-PNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIA 246
Cdd:cd07839  135 NGELKLADFGLARAFGiPVRCYSAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIF 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 247 KVLGT--EDLYDYIDKYnieldPRFNDILGRHSRKRWERFVHSENQhlvstEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07839  215 RLLGTptEESWPGVSKL-----PDYKPYPMYPATTSLVNVVPKLNS-----TGRDLLQNLLVCNPVQRISAEEALQHPYF 284
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
92-324 1.45e-37

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: 137.02  E-value: 1.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDP-VSRTP--ALVFEHVNntdfkqlyQTLSDY------------DIRFYMYEILKALDYCHSMGIMHRD 156
Cdd:cd07838   61 PNVVRLLDVCHGPrTDRELklTLVFEHVD--------QDLATYldkcpkpglppeTIKDLMRQLLRGLDFLHSHRIVHRD 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 157 VKPHNVMIDHEhRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMiFRKEPFFHGH 236
Cdd:cd07838  133 LKPQNILVTSD-GQVKLADFGLARIYSFEMALTSVVVTLWYRAPEVLLQ-SSYATPVDMWSVGCIFAEL-FNRRPLFRGS 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 237 DNYDQLVRIAKVLGTEDLYDYIDkyNIELDPrfnDILGRHSRKRWERFVHSenqhlVSTEALDFLDKLLRYDHQARLTAR 316
Cdd:cd07838  210 SEADQLGKIFDVIGLPSEEEWPR--NSALPR---SSFPSYTPRPFKSFVPE-----IDEEGLDLLKKMLTFNPHKRISAF 279

                 ....*...
gi 528504250 317 EAMDHSYF 324
Cdd:cd07838  280 EALQHPYF 287
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
93-324 2.27e-37

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: 138.16  E-value: 2.27e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIkdpvsrTPALVFEHVNN---------TDFKQL--YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHN 161
Cdd:cd07880   75 NVIGLLDVF------TPDLSLDRFHDfylvmpfmgTDLGKLmkHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGN 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 162 VMIDhEHRKLRLIDWGLAEfyHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQ 241
Cdd:cd07880  149 LAVN-EDCELKILDFGLAR--QTDSEMTGYVVTRWYRAPEVILNWMHYTQTVDIWSVGCIMAEMLTGK-PLFKGHDHLDQ 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 242 LVRIAKVLGTEDlYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSenqhlVSTEALDFLDKLLRYDHQARLTAREAMDH 321
Cdd:cd07880  225 LMEIMKVTGTPS-KEFVQKLQSEDAKNYVKKLPRFRKKDFRSLLPN-----ANPLAVNVLEKMLVLDAESRITAAEALAH 298

                 ...
gi 528504250 322 SYF 324
Cdd:cd07880  299 PYF 301
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
93-324 5.09e-37

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: 137.48  E-value: 5.09e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIkdpvsrTPALVFEHVNN---------TDFKQLY--QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHN 161
Cdd:cd07877   77 NVIGLLDVF------TPARSLEEFNDvylvthlmgADLNNIVkcQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSN 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 162 VMIDhEHRKLRLIDWGLAEfyHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEpFFHGHDNYDQ 241
Cdd:cd07877  151 LAVN-EDCELKILDFGLAR--HTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRT-LFPGTDHIDQ 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 242 LVRIAKVLGTEDlYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENqhlvsTEALDFLDKLLRYDHQARLTAREAMDH 321
Cdd:cd07877  227 LKLILRLVGTPG-AELLKKISSESARNYIQSLTQMPKMNFANVFIGAN-----PLAVDLLEKMLVLDSDKRITAAQALAH 300

                 ...
gi 528504250 322 SYF 324
Cdd:cd07877  301 AYF 303
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
93-323 4.41e-36

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: 134.35  E-value: 4.41e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIKdpvsrtpALVFEHVNNTDFKQ------LY-----QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHN 161
Cdd:cd07849   64 NIIGILDIQR-------PPTFESFKDVYIVQelmetdLYkliktQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSN 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 162 VMIDhEHRKLRLIDWGLAEFYHPNQ-------EYnvrVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFH 234
Cdd:cd07849  137 LLLN-TNCDLKICDFGLARIADPEHdhtgfltEY---VATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNR-PLFP 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 235 GHDNYDQLVRIAKVLGT---EDLY--------DYIDKynieldprfndiLGRHSRKRWER-FVHSENQhlvsteALDFLD 302
Cdd:cd07849  212 GKDYLHQLNLILGILGTpsqEDLNciislkarNYIKS------------LPFKPKVPWNKlFPNADPK------ALDLLD 273
                        250       260
                 ....*....|....*....|.
gi 528504250 303 KLLRYDHQARLTAREAMDHSY 323
Cdd:cd07849  274 KMLTFNPHKRITVEEALAHPY 294
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
85-326 5.93e-36

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: 133.85  E-value: 5.93e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  85 LENLRGgPNIITLLDIIKDPvSRTPALVFEhVNNTDFKQLYQT--LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:cd07856   63 LKHLRH-ENIISLSDIFISP-LEDIYFVTE-LLGTDLHRLLTSrpLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNI 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 163 MIDhEHRKLRLIDWGLAEFYHPnqEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIfRKEPFFHGHDNYDQL 242
Cdd:cd07856  140 LVN-ENCDLKICDFGLARIQDP--QMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEML-EGKPLFPGKDHVNQF 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 243 VRIAKVLGTEDLyDYIDKYNIELDPRFNDILGRHsrkrwERFVHSENQHLVSTEALDFLDKLLRYDHQARLTAREAMDHS 322
Cdd:cd07856  216 SIITELLGTPPD-DVINTICSENTLRFVQSLPKR-----ERVPFSEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHP 289

                 ....
gi 528504250 323 YFYP 326
Cdd:cd07856  290 YLAP 293
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
30-324 7.88e-36

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: 133.21  E-value: 7.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  30 VVDWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKK-----KIKREIKILENLRGgPNIITLLDIIKDP 104
Cdd:cd07866    1 FYGCSKLRDYEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNEKdgfpiTALREIKILKKLKH-PNVVPLIDMAVER 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 105 ---VSRTPALVF------EH-----VNNTDFKqlyqtLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHeHRK 170
Cdd:cd07866   80 pdkSKRKRGSVYmvtpymDHdlsglLENPSVK-----LTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDN-QGI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 171 LRLIDWGLAEFYHPN------------QEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGHDN 238
Cdd:cd07866  154 LKIADFGLARPYDGPppnpkggggggtRKYTNLVVTRWYRPPELLLGERRYTTAVDIWGIGCVFAEMFTRR-PILQGKSD 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 239 YDQLVRIAKVLG--TED---LYDYIdkynieldPRFNDIL--GRHSRKRWERFVHsenqhlVSTEALDFLDKLLRYDHQA 311
Cdd:cd07866  233 IDQLHLIFKLCGtpTEEtwpGWRSL--------PGCEGVHsfTNYPRTLEERFGK------LGPEGLDLLSKLLSLDPYK 298
                        330
                 ....*....|...
gi 528504250 312 RLTAREAMDHSYF 324
Cdd:cd07866  299 RLTASDALEHPYF 311
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
92-324 1.80e-35

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: 131.77  E-value: 1.80e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPvSRTpALVFEHVNnTDFKQLYQTLSDYD------IRFYMYEILKALDYCHSMGIMHRDVKPHNVMID 165
Cdd:cd07861   59 PNIVCLEDVLMQE-NRL-YLVFEFLS-MDLKKYLDSLPKGKymdaelVKSYLYQILQGILFCHSRRVLHRDLKPQNLLID 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 166 HEHrKLRLIDWGLAE-FYHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQLVR 244
Cdd:cd07861  136 NKG-VIKLADFGLARaFGIPVRVYTHEVVTLWYRAPEVLLGSPRYSTPVDIWSIGTIFAEMATKK-PLFHGDSEIDQLFR 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 245 IAKVLGT---------EDLYDYidkynieldprfndilgRHSRKRWERFVHSENQHLVSTEALDFLDKLLRYDHQARLTA 315
Cdd:cd07861  214 IFRILGTptediwpgvTSLPDY-----------------KNTFPKWKKGSLRTAVKNLDEDGLDLLEKMLIYDPAKRISA 276

                 ....*....
gi 528504250 316 REAMDHSYF 324
Cdd:cd07861  277 KKALVHPYF 285
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
33-324 1.10e-34

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: 129.74  E-value: 1.10e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  33 WGNQDDYQLVRKLGRGKYSEVFEAIN-ITNNEKVVVKILKPVKKK---KIKREIKILENLRGGpNIITLLDIIKdpVSRT 108
Cdd:cd07871    1 FGKLETYVKLDKLGEGTYATVFKGRSkLTENLVALKEIRLEHEEGapcTAIREVSLLKNLKHA-NIVTLHDIIH--TERC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 109 PALVFEHVNNtDFKQLYQT----LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYH- 183
Cdd:cd07871   78 LTLVFEYLDS-DLKQYLDNcgnlMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLIN-EKGELKLADFGLARAKSv 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 184 PNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQLVRIAKVLG--TEDLYDYIDKy 261
Cdd:cd07871  156 PTKTYSNEVVTLWYRPPDVLLGSTEYSTPIDMWGVGCILYEMATGR-PMFPGSTVKEELHLIFRLLGtpTEETWPGVTS- 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504250 262 nieldprfndilgrHSRKRWERFVHSENQHLVS------TEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07871  234 --------------NEEFRSYLFPQYRAQPLINhaprldTDGIDLLSSLLLYETKSRISAEAALRHSYF 288
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
93-327 1.17e-34

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: 130.57  E-value: 1.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIKdPVSRTP----ALVFEhVNNTDFKQLY---QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMID 165
Cdd:cd07858   65 NVIAIKDIMP-PPHREAfndvYIVYE-LMDTDLHQIIrssQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLN 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 166 hEHRKLRLIDWGLAEFYHPNQEYNVR-VASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQLVR 244
Cdd:cd07858  143 -ANCDLKICDFGLARTTSEKGDFMTEyVVTRWYRAPELLLNCSEYTTAIDVWSVGCIFAELLGRK-PLFPGKDYVHQLKL 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 245 IAKVLGT---EDLyDYIDKYNIEldpRFNDILGRHSRKRW-ERFVHsenqhlVSTEALDFLDKLLRYDHQARLTAREAMD 320
Cdd:cd07858  221 ITELLGSpseEDL-GFIRNEKAR---RYIRSLPYTPRQSFaRLFPH------ANPLAIDLLEKMLVFDPSKRITVEEALA 290

                 ....*..
gi 528504250 321 HSYFYPI 327
Cdd:cd07858  291 HPYLASL 297
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
33-323 1.60e-34

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: 129.54  E-value: 1.60e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  33 WG--NQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKpvkkkkikreikiLENLRGG-----------------PN 93
Cdd:cd07864    1 WGkrCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVR-------------LDNEKEGfpitaireikilrqlnhRS 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  94 IITLLDIIKDPV--------SRTPALVFEHVNNTDFKQLYQTLSDYD---IRFYMYEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:cd07864   68 VVNLKEIVTDKQdaldfkkdKGAFYLVFEYMDHDLMGLLESGLVHFSedhIKSFMKQLLEGLNYCHKKNFLHRDIKCSNI 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 163 MIDHEHrKLRLIDWGLAEFYHPNQE--YNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYD 240
Cdd:cd07864  148 LLNNKG-QIKLADFGLARLYNSEESrpYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGEL-FTKKPIFQANQELA 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 241 QLVRIAKVLGTEDLYDYIDKynIELdPRFNDIlgrHSRKRWERFVHSENQHLvSTEALDFLDKLLRYDHQARLTAREAMD 320
Cdd:cd07864  226 QLELISRLCGSPCPAVWPDV--IKL-PYFNTM---KPKKQYRRRLREEFSFI-PTPALDLLDHMLTLDPSKRCTAEQALN 298

                 ...
gi 528504250 321 HSY 323
Cdd:cd07864  299 SPW 301
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
92-324 3.37e-34

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: 128.26  E-value: 3.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDpvSRTPALVFEHVNNTDFKQLYQT---LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEH 168
Cdd:cd07847   60 PNLVNLIEVFRR--KRKLHLVFEYCDHTVLNELEKNprgVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILIT-KQ 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 RKLRLIDWGLAEFYH-PNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIfRKEPFFHGHDNYDQLVRIAK 247
Cdd:cd07847  137 GQIKLCDFGFARILTgPGDDYTDYVATRWYRAPELLVGDTQYGPPVDVWAIGCVFAELL-TGQPLWPGKSDVDQLYLIRK 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 248 VLGtedlydyidkyniELDPRFNDILG-------------RHSRKRWERFVHsenqhlVSTEALDFLDKLLRYDHQARLT 314
Cdd:cd07847  216 TLG-------------DLIPRHQQIFStnqffkglsipepETREPLESKFPN------ISSPALSFLKGCLQMDPTERLS 276
                        250
                 ....*....|
gi 528504250 315 AREAMDHSYF 324
Cdd:cd07847  277 CEELLEHPYF 286
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
93-327 7.14e-34

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: 128.87  E-value: 7.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIkdpvsrTPALVFEHVNN---------TDFKQLY-QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:cd07879   75 NVIGLLDVF------TSAVSGDEFQDfylvmpymqTDLQKIMgHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNL 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 163 MIDhEHRKLRLIDWGLAEfyHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEpFFHGHDNYDQL 242
Cdd:cd07879  149 AVN-EDCELKILDFGLAR--HADAEMTGYVVTRWYRAPEVILNWMHYNQTVDIWSVGCIMAEMLTGKT-LFKGKDYLDQL 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 243 VRIAKVLGTEDLyDYIDKYNIELDPRFNDILGRHSRKRWERFVHSenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHS 322
Cdd:cd07879  225 TQILKVTGVPGP-EFVQKLEDKAAKSYIKSLPKYPRKDFSTLFPK-----ASPQAVDLLEKMLELDVDKRLTATEALEHP 298

                 ....*
gi 528504250 323 YFYPI 327
Cdd:cd07879  299 YFDSF 303
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
93-325 3.16e-33

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: 125.89  E-value: 3.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIKdpVSRTPALVFEHVNntdfKQLYQTLSD-------YDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMID 165
Cdd:cd07873   61 NIVTLHDIIH--TEKSLTLVFEYLD----KDLKQYLDDcgnsinmHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLIN 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 166 hEHRKLRLIDWGLAEFYH-PNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQLVR 244
Cdd:cd07873  135 -ERGELKLADFGLARAKSiPTKTYSNEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGR-PLFPGSTVEEQLHF 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 245 IAKVLGT--EDLYDYI------DKYNIeldPRFN-DILGRHSRKrwerfvhsenqhlVSTEALDFLDKLLRYDHQARLTA 315
Cdd:cd07873  213 IFRILGTptEETWPGIlsneefKSYNY---PKYRaDALHNHAPR-------------LDSDGADLLSKLLQFEGRKRISA 276
                        250
                 ....*....|
gi 528504250 316 REAMDHSYFY 325
Cdd:cd07873  277 EEAMKHPYFH 286
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
39-324 2.16e-32

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 126.69  E-value: 2.16e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKiLENLRGgPNIITLLD------IIKDPVSRTPALV 112
Cdd:PTZ00036  68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNRELLI-MKNLNH-INIIFLKDyyytecFKKNEKNIFLNVV 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 113 FEHVNNTDFKQLY------QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPNQ 186
Cdd:PTZ00036 146 MEFIPQTVHKYMKhyarnnHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHTLKLCDFGSAKNLLAGQ 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 187 EYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFrKEPFFHGHDNYDQLVRIAKVLGT---EDLYDYIDKYni 263
Cdd:PTZ00036 226 RSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMIL-GYPIFSGQSSVDQLVRIIQVLGTpteDQLKEMNPNY-- 302
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504250 264 eLDPRFNDILGRHSRKRWERFvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:PTZ00036 303 -ADIKFPDVKPKDLKKVFPKG--------TPDDAINFISQFLKYEPLKRLNPIEALADPFF 354
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
39-324 2.86e-32

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: 123.15  E-value: 2.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGG---PNIITLLDIIKDPVSRTpaLVFEH 115
Cdd:cd07870    2 YLNLEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTAIREASLLKGlkhANIVLLHDIIHTKETLT--FVFEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 116 VNnTDFKQLYQT----LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYH-PNQEYNV 190
Cdd:cd07870   80 MH-TDLAQYMIQhpggLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLG-ELKLADFGLARAKSiPSQTYSS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 191 RVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMiFRKEPFFHGHDN-YDQLVRIAKVLG--TEDLYDYIDK---YNIE 264
Cdd:cd07870  158 EVVTLWYRPPDVLLGATDYSSALDIWGAGCIFIEM-LQGQPAFPGVSDvFEQLEKIWTVLGvpTEDTWPGVSKlpnYKPE 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 265 L-----DPRFNDILGRHSRkrwerfvhsenqhlvSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07870  237 WflpckPQQLRVVWKRLSR---------------PPKAEDLASQMLMMFPKDRISAQDALLHPYF 286
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
92-324 7.74e-32

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: 121.95  E-value: 7.74e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTPALVFEHVNNtDFKQLYQTLSDY----DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE 167
Cdd:cd07843   64 PNIVTVKEVVVGSNLDKIYMVMEYVEH-DLKSLMETMKQPflqsEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNR 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 168 HRkLRLIDWGLA-EFYHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIfRKEPFFHGHDNYDQLVRIA 246
Cdd:cd07843  143 GI-LKICDFGLArEYGSPLKPYTQLVVTLWYRAPELLLGAKEYSTAIDMWSVGCIFAELL-TKKPLFPGKSEIDQLNKIF 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 247 KVLGTEdlydyidkyNIELDPRFNDILGrhsRKRWERFVHSENQ------HLVSTEA-LDFLDKLLRYDHQARLTAREAM 319
Cdd:cd07843  221 KLLGTP---------TEKIWPGFSELPG---AKKKTFTKYPYNQlrkkfpALSLSDNgFDLLNRLLTYDPAKRISAEDAL 288

                 ....*
gi 528504250 320 DHSYF 324
Cdd:cd07843  289 KHPYF 293
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
113-324 8.43e-32

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: 122.27  E-value: 8.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 113 FEHVNNTDFKQLYQTLsdydIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRK-LRLIDWGLAEFYHpNQEYNVr 191
Cdd:cd14210  102 YELLKSNNFQGLSLSL----IRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSsIKVIDFGSSCFEG-EKVYTY- 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 192 VASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLGTEDLYdYIDKynielDPR--- 268
Cdd:cd14210  176 IQSRFYRAPEVILG-LPYDTAIDMWSLGCILAEL-YTGYPLFPGENEEEQLACIMEVLGVPPKS-LIDK-----ASRrkk 247
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504250 269 FNDILGR----HSRKRWERFVHSENQHLVSTEA----LDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14210  248 FFDSNGKprptTNSKGKKRRPGSKSLAQVLKCDdpsfLDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
33-324 9.09e-32

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: 122.41  E-value: 9.09e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  33 WGNQDDYQLVRKLGRGKYSEVFEAIN-ITNNekvvvkilkpvkkkKIKREIKILENLRGGP----------------NII 95
Cdd:cd07872    2 FGKMETYIKLEKLGEGTYATVFKGRSkLTEN--------------LVALKEIRLEHEEGAPctairevsllkdlkhaNIV 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  96 TLLDIIKDPVSRTpaLVFEHVNNtDFKQLY----QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKL 171
Cdd:cd07872   68 TLHDIVHTDKSLT--LVFEYLDK-DLKQYMddcgNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLIN-ERGEL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 172 RLIDWGLAEFYH-PNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQLVRIAKVLG 250
Cdd:cd07872  144 KLADFGLARAKSvPTKTYSNEVVTLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGR-PLFPGSTVEDELHLIFRLLG 222
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 251 T--EDLYDYIDKynieldprfNDILGRHSRKRWERFVHSENQHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07872  223 TptEETWPGISS---------NDEFKNYNFPKYKPQPLINHAPRLDTEGIELLTKFLQYESKKRISAEEAMKHAYF 289
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
111-324 6.05e-31

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: 119.45  E-value: 6.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNT---DFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYH-PNQ 186
Cdd:cd07846   77 LVFEFVDHTvldDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVS-QSGVVKLCDFGFARTLAaPGE 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 187 EYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLGTedlydyidkynieLD 266
Cdd:cd07846  156 VYTDYVATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEM-LTGEPLFPGDSDIDQLYHIIKCLGN-------------LI 221
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 267 PRFNDILGRHsrKRWERFVHSENQHLVSTE---------ALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07846  222 PRHQELFQKN--PLFAGVRLPEVKEVEPLErrypklsgvVIDLAKKCLHIDPDKRPSCSELLHHEFF 286
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
92-324 9.02e-31

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: 119.70  E-value: 9.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTPALVF---EHvnntDFKQLYQ--------TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPH 160
Cdd:cd07842   62 ENVVSLVEVFLEHADKSVYLLFdyaEH----DLWQIIKfhrqakrvSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPA 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 161 NVMI---DHEHRKLRLIDWGLAEFYH----PNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIfRKEPFF 233
Cdd:cd07842  138 NILVmgeGPERGVVKIGDLGLARLFNaplkPLADLDPVVVTIWYRAPELLLGARHYTKAIDIWAIGCIFAELL-TLEPIF 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 234 HGHD---------NYDQLVRIAKVLG--TEDLYDYIDKYnieldPRFNDILGRHSRKRW-----ERFVHSENQhlVSTEA 297
Cdd:cd07842  217 KGREakikksnpfQRDQLERIFEVLGtpTEKDWPDIKKM-----PEYDTLKSDTKASTYpnsllAKWMHKHKK--PDSQG 289
                        250       260
                 ....*....|....*....|....*..
gi 528504250 298 LDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07842  290 FDLLRKLLEYDPTKRITAEEALEHPYF 316
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
133-324 1.14e-30

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: 118.14  E-value: 1.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 133 IRFYMYEILKALDYCHSMGIMHRDVKPHNVMI-DHEHRKLRLIDWGLAEFYHpnQEYNVRVASRYFKGPELLVDYQmYDY 211
Cdd:cd14133  104 IRKIAQQILEALVFLHSLGLIHCDLKPENILLaSYSRCQIKIIDFGSSCFLT--QRLYSYIQSRYYRAPEVILGLP-YDE 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 212 SLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLGtedlydYIDKYNIEldprfndilgrHSRKRWERFVhsenqh 291
Cdd:cd14133  181 KIDMWSLGCILAEL-YTGEPLFPGASEVDQLARIIGTIG------IPPAHMLD-----------QGKADDELFV------ 236
                        170       180       190
                 ....*....|....*....|....*....|...
gi 528504250 292 lvstealDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14133  237 -------DFLKKLLEIDPKERPTASQALSHPWL 262
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
92-324 7.78e-30

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: 115.73  E-value: 7.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTPALVFEHVNN-----TDFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDH 166
Cdd:cd14008   64 PNIVRLYEVIDDPESDKLYLVLEYCEGgpvmeLDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTA 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 167 EhRKLRLIDWGLAEFYH-PNQEYNVRVASRYFKGPELL-VDYQMYD-YSLDMWSLGCMLASMIFRKEPFfhghdNYDQLV 243
Cdd:cd14008  144 D-GTVKISDFGVSEMFEdGNDTLQKTAGTPAFLAPELCdGDSKTYSgKAADIWALGVTLYCLVFGRLPF-----NGDNIL 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 244 riakvlgteDLYDYIDKYNIELDPRFNdilgrhsrkrwerfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14008  218 ---------ELYEAIQNQNDEFPIPPE----------------------LSPELKDLLRRMLEKDPEKRITLKEIKEHPW 266

                 .
gi 528504250 324 F 324
Cdd:cd14008  267 V 267
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
45-225 8.95e-30

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: 114.29  E-value: 8.95e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  45 LGRGKYSEVFEAINITNNEK----VVVKILKPVKKKKIKREIKILENLRGgPNIITLLDIIKDPvsRTPALVFEHVNNTD 120
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKvavkVIPKEKLKKLLEELLREIEILKKLNH-PNIVKLYDVFETE--NFLYLVMEYCEGGS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 121 FKQLYQ----TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHeHRKLRLIDWGLAEFYHPNQEYNVRVASRY 196
Cdd:cd00180   78 LKDLLKenkgPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDS-DGTVKLADFGLAKDLDSDDSLLKTTGGTT 156
                        170       180       190
                 ....*....|....*....|....*....|.
gi 528504250 197 FKG--PELLVDYQMYDYSLDMWSLGCMLASM 225
Cdd:cd00180  157 PPYyaPPELLGGRYYGPKVDIWSLGVILYEL 187
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
38-321 9.86e-30

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: 115.31  E-value: 9.86e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  38 DYQLVRKLGRGKYSEVFEAINITNNEK-----VVVKILKPVKKKKIKREIKILENLRGgPNIITLLDIIKDPvsRTPALV 112
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARHKLTGEKvaikiIDKSKLKEEIEEKIKREIEIMKLLNH-PNIIKLYEVIETE--NKIYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 113 FEHVNNTD-FKQLYQ--TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYN 189
Cdd:cd14003   78 MEYASGGElFDYIVNngRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLD-KNGNLKIIDFGLSNEFRGGSLLK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 190 VRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFfhghDNYDQlvriakvlgtEDLYDYIDKYNIELDPRf 269
Cdd:cd14003  157 TFCGTPAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPF----DDDND----------SKLFRKILKGKYPIPSH- 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528504250 270 ndilgrhsrkrwerfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDH 321
Cdd:cd14003  222 -----------------------LSPDARDLIRRMLVVDPSKRITIEEILNH 250
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
33-324 1.25e-29

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: 116.33  E-value: 1.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  33 WGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGG---PNIITLLDIIKdpVSRTP 109
Cdd:cd07869    1 FGKADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGlkhANIVLLHDIIH--TKETL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 110 ALVFEHVNnTDFKQLYQT----LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYH-P 184
Cdd:cd07869   79 TLVFEYVH-TDLCQYMDKhpggLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLIS-DTGELKLADFGLARAKSvP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 185 NQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGT--EDLYDYIDKYN 262
Cdd:cd07869  157 SHTYSNEVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQLERIFLVLGTpnEDTWPGVHSLP 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528504250 263 IELDPRFNDILGRHSRKRWERFVHSENqhlvsteALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07869  237 HFKPERFTLYSPKNLRQAWNKLSYVNH-------AEDLASKLLQCFPKNRLSAQAALSHEYF 291
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
38-324 1.42e-29

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: 114.99  E-value: 1.42e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  38 DYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLR--GGPNIITLLD--IIKDPVSrtpaLVF 113
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILNEIAILKkcKHPNIVKYYGsyLKKDELW----IVM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 114 EHVNNTDFKQLY----QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYHPNQEYN 189
Cdd:cd05122   77 EFCSGGSLKDLLkntnKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDG-EVKLIDFGLSAQLSDGKTRN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 190 VRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFHGHdnydqlvrIAKVLgtedlyDYIDKYNIeldPRF 269
Cdd:cd05122  156 TFVGTPYWMAPEVIQG-KPYGFKADIWSLGITAIEMAEGKPPYSELP--------PMKAL------FLIATNGP---PGL 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 270 ndilgrhsrkrwerfvhsENQHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd05122  218 ------------------RNPKKWSKEFKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
39-324 2.69e-28

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: 112.43  E-value: 2.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNN---------EKVVVKILKPVKKKKIKREIKILENLRGgPNIITLLDIIKdpVSRTP 109
Cdd:cd07862    3 YECVAEIGEGAYGKVFKARDLKNGgrfvalkrvRVQTGEEGMPLSTIREVAVLRHLETFEH-PNVVRLFDVCT--VSRTD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 110 -----ALVFEHVNNtDFKQLYQTLSD-----YDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLA 179
Cdd:cd07862   80 retklTLVFEHVDQ-DLTTYLDKVPEpgvptETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVT-SSGQIKLADFGLA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 180 EFYHPNQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYID 259
Cdd:cd07862  158 RIYSFQMALTSVVVTLWYRAPEVLLQ-SSYATPVDLWSVGCIFAEM-FRRKPLFRGSSDVDQLGKILDVIGLPGEEDWPR 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 260 KYNIeldPRfnDILGRHSRKRWERFVHSenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07862  236 DVAL---PR--QAFHSKSAQPIEKFVTD-----IDELGKDLLLKCLTFNPAKRISAYSALSHPYF 290
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
92-324 4.11e-28

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: 111.98  E-value: 4.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKdpVSRTP-----ALVFEHVNNtDFKQLYQT-----LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHN 161
Cdd:cd07863   62 PNIVRLMDVCA--TSRTDretkvTLVFEHVDQ-DLRTYLDKvpppgLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPEN 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 162 VMIDhEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQ 241
Cdd:cd07863  139 ILVT-SGGQVKLADFGLARIYSCQMALTPVVVTLWYRAPEVLLQ-STYATPVDMWSVGCIFAEM-FRRKPLFCGNSEADQ 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 242 LVRIAKVLG--TEDLYdyidkynieldPRfnDI-LGRHS-RKRWERFVHSENQHLVSTEAlDFLDKLLRYDHQARLTARE 317
Cdd:cd07863  216 LGKIFDLIGlpPEDDW-----------PR--DVtLPRGAfSPRGPRPVQSVVPEIEESGA-QLLLEMLTFNPHKRISAFR 281

                 ....*..
gi 528504250 318 AMDHSYF 324
Cdd:cd07863  282 ALQHPFF 288
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
93-333 4.35e-28

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: 113.30  E-value: 4.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIKdPVSRTPalvFEHVN------NTDFKQLY---QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVM 163
Cdd:cd07853   60 NVLSALDILQ-PPHIDP---FEEIYvvtelmQSDLHKIIvspQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLL 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 164 IDHEHRkLRLIDWGLAEFYHPNQEYNV--RVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQ 241
Cdd:cd07853  136 VNSNCV-LKICDFGLARVEEPDESKHMtqEVVTQYYRAPEILMGSRHYTSAVDIWSVGCIFAELLGRR-ILFQAQSPIQQ 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 242 LVRIAKVLGTEDLYDYidKYNIElDPRFNDILGRHSRKRWERF--VHSENQHlvstEALDFLDKLLRYDHQARLTAREAM 319
Cdd:cd07853  214 LDLITDLLGTPSLEAM--RSACE-GARAHILRGPHKPPSLPVLytLSSQATH----EAVHLLCRMLVFDPDKRISAADAL 286
                        250
                 ....*....|....
gi 528504250 320 DHSYFypivkDQGR 333
Cdd:cd07853  287 AHPYL-----DEGR 295
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
91-326 3.09e-27

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: 110.64  E-value: 3.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  91 GPNIITLLDIIKDPVSRTPALVFEHVNNTDFKQL--YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEH 168
Cdd:cd07854   72 GPSGSDLTEDVGSLTELNSVYIVQEYMETDLANVleQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTED 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 RKLRLIDWGLAEFYHPNQEY----NVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQLVR 244
Cdd:cd07854  152 LVLKIGDFGLARIVDPHYSHkgylSEGLVTKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGK-PLFAGAHELEQMQL 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 245 IAK---VLGTEDLYD-------YIDKYNIELDPRFNDILGRhsrkrwerfvhsenqhlVSTEALDFLDKLLRYDHQARLT 314
Cdd:cd07854  231 ILEsvpVVREEDRNEllnvipsFVRNDGGEPRRPLRDLLPG-----------------VNPEALDFLEQILTFNPMDRLT 293
                        250
                 ....*....|..
gi 528504250 315 AREAMDHSYFYP 326
Cdd:cd07854  294 AEEALMHPYMSC 305
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
92-324 4.92e-27

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 109.85  E-value: 4.92e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDII--KDPVSrtpaLVFEhVNNTDFKQLYQT---LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDH 166
Cdd:PTZ00024  80 ENIMGLVDVYveGDFIN----LVMD-IMASDLKKVVDRkirLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINS 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 167 EHrKLRLIDWGLA---------------EFYHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKeP 231
Cdd:PTZ00024 155 KG-ICKIADFGLArrygyppysdtlskdETMQRREEMTSKVVTLWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGK-P 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 232 FFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELdprfndilgrhsrkrWERFVHSENQHLVST------EALDFLDKLL 305
Cdd:PTZ00024 233 LFPGENEIDQLGRIFELLGTPNEDNWPQAKKLPL---------------YTEFTPRKPKDLKTIfpnasdDAIDLLQSLL 297
                        250
                 ....*....|....*....
gi 528504250 306 RYDHQARLTAREAMDHSYF 324
Cdd:PTZ00024 298 KLNPLERISAKEALKHEYF 316
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
92-321 1.22e-26

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: 106.93  E-value: 1.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPvsRTPALV---------FEHVNNTDFkqlyqTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:cd14103   50 PRLLQLYDAFETP--REMVLVmeyvaggelFERVVDDDF-----ELTERDCILFMRQICEGVQYMHKQGILHLDLKPENI 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 163 M-IDHEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSLG--C-MLASMIfrkEPFFhGHDN 238
Cdd:cd14103  123 LcVSRTGNQIKIIDFGLARKYDPDKKLKVLFGTPEFVAPE-VVNYEPISYATDMWSVGviCyVLLSGL---SPFM-GDND 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 239 YDQLVRIAKVlgtedlydyidKYNIElDPRFNDIlgrhsrkrwerfvhsenqhlvSTEALDFLDKLLRYDHQARLTAREA 318
Cdd:cd14103  198 AETLANVTRA-----------KWDFD-DEAFDDI---------------------SDEAKDFISKLLVKDPRKRMSAAQC 244

                 ...
gi 528504250 319 MDH 321
Cdd:cd14103  245 LQH 247
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
85-324 1.88e-26

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


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 107.84  E-value: 1.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  85 LENLRGgPNIITLLDIIKDPVSRTPALVFEHVNNtDFKQLY----QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPH 160
Cdd:cd07845   60 LLNLRH-PNIVELKEVVVGKHLDSIFLVMEYCEQ-DLASLLdnmpTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVS 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 161 NV-MIDHEHrkLRLIDWGLAEFY-HPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMiFRKEPFFHGHDN 238
Cdd:cd07845  138 NLlLTDKGC--LKIADFGLARTYgLPAKPMTPKVVTLWYRAPELLLGCTTYTTAIDMWAVGCILAEL-LAHKPLLPGKSE 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 239 YDQLVRIAKVLGT--EDLYDYID------KYNIELDPrFNDIlgRHsrkrweRFvhsenqHLVSTEALDFLDKLLRYDHQ 310
Cdd:cd07845  215 IEQLDLIIQLLGTpnESIWPGFSdlplvgKFTLPKQP-YNNL--KH------KF------PWLSEAGLRLLNFLLMYDPK 279
                        250
                 ....*....|....
gi 528504250 311 ARLTAREAMDHSYF 324
Cdd:cd07845  280 KRATAEEALESSYF 293
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
39-324 2.03e-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: 107.45  E-value: 2.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVKILKpvkkkkikreikiLENLRGG-----------------PNIITLLDII 101
Cdd:cd07865   14 YEKLAKIGQGTFGEVFKARHRKTGQIVALKKVL-------------MENEKEGfpitalreikilqllkhENVVNLIEIC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 102 ---KDPVSRTPA---LVFEHVNNtDFKQLyqtLSDYDIRFYMYEI-------LKALDYCHSMGIMHRDVKPHNVMIDhEH 168
Cdd:cd07865   81 rtkATPYNRYKGsiyLVFEFCEH-DLAGL---LSNKNVKFTLSEIkkvmkmlLNGLYYIHRNKILHRDMKAANILIT-KD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 RKLRLIDWGLAEFYH------PNQeYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRkEPFFHGHDNYDQL 242
Cdd:cd07865  156 GVLKLADFGLARAFSlaknsqPNR-YTNRVVTLWYRPPELLLGERDYGPPIDMWGAGCIMAEMWTR-SPIMQGNTEQHQL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 243 VRIAKVLG--TEDLYDYIDKYnieldPRFNDILGRHSRKRWERfvhSENQHLVST-EALDFLDKLLRYDHQARLTAREAM 319
Cdd:cd07865  234 TLISQLCGsiTPEVWPGVDKL-----ELFKKMELPQGQKRKVK---ERLKPYVKDpYALDLIDKLLVLDPAKRIDADTAL 305

                 ....*
gi 528504250 320 DHSYF 324
Cdd:cd07865  306 NHDFF 310
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
111-324 2.23e-26

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: 106.06  E-value: 2.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTD-FKQLYQ--TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE-HrkLRLIDWGLA-EFYHPN 185
Cdd:cd05123   70 LVLDYVPGGElFSHLSKegRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDgH--IKLTDFGLAkELSSDG 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 186 QEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFhGHDnydqlvriakvlgTEDLYDYIdkynIEL 265
Cdd:cd05123  148 DRTYTFCGTPEYLAPEVLLG-KGYGKAVDWWSLGVLLYEMLTGKPPFY-AEN-------------RKEIYEKI----LKS 208
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528504250 266 DPRFNDIlgrhsrkrwerfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMD---HSYF 324
Cdd:cd05123  209 PLKFPEY--------------------VSPEAKSLISGLLQKDPTKRLGSGGAEEikaHPFF 250
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
37-395 3.07e-26

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 109.72  E-value: 3.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRKLGRGKYSEVFEAINITNNEK------VVVKILKPVKKKKIKREIKILENLRGgPNIITLLDIIKDpvSRTPA 110
Cdd:COG0515    7 GRYRILRLLGRGGMGVVYLARDLRLGRPvalkvlRPELAADPEARERFRREARALARLNH-PNIVRVYDVGEE--DGRPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFKQLYQT---LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHPNQ- 186
Cdd:COG0515   84 LVMEYVEGESLADLLRRrgpLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGR-VKLIDFGIARALGGATl 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 187 -EYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPfFHGHDNYDQLVRIAkvlgtEDLYDYIDKYNIEL 265
Cdd:COG0515  163 tQTGTVVGTPGYMAPEQARG-EPVDPRSDVYSLGVTLYELLTGRPP-FDGDSPAELLRAHL-----REPPPPPSELRPDL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 266 DPRFNDILGR-HSRKRWERFvhsenqhlvsTEALDFLDKLLRYDHQ--ARLTAREAMDHSYFYPIVKDQGRGAPAAGMAA 342
Cdd:COG0515  236 PPALDAIVLRaLAKDPEERY----------QSAAELAAALRAVLRSlaAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 305
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528504250 343 SSTPVSSSSLMAGIASMTPSTQPNIANISAGSPVIPAPNTMATQVPTAAGAQP 395
Cdd:COG0515  306 AAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAAL 358
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
111-324 5.30e-26

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: 105.85  E-value: 5.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNntdfKQLYQTLSDY-------DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYH 183
Cdd:cd07848   77 LVFEYVE----KNMLELLEEMpngvppeKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHND-VLKLCDFGFARNLS 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 184 P--NQEYNVRVASRYFKGPELLVDYQmYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKY 261
Cdd:cd07848  152 EgsNANYTEYVATRWYRSPELLLGAP-YGKAVDMWSVGCILGEL-SDGQPLFPGESEIDQLFTIQKVLGPLPAEQMKLFY 229
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 262 NielDPRFNDIlgrhsrkRWERFVHSEN-----QHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07848  230 S---NPRFHGL-------RFPAVNHPQSlerryLGILSGVLLDLMKNLLKLNPTDRYLTEQCLNHPAF 287
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
38-324 7.05e-26

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: 104.91  E-value: 7.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  38 DYQLVRKLGRGKYSEVFEAINITNNEKV-----VVKILKPVKKKKIKREIKILENLRGgPNIITLLDIIKDPVSRTpaLV 112
Cdd:cd06606    1 RWKKGELLGKGSFGSVYLALNLDTGELMavkevELSGDSEEELEALEREIRILSSLKH-PNIVRYLGTERTENTLN--IF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 113 FEHVNN---TDFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEhRKLRLIDWGLA---EFYHPNQ 186
Cdd:cd06606   78 LEYVPGgslASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSD-GVVKLADFGCAkrlAEIATGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 187 EYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIakvlGTEDLYDYIdkynield 266
Cdd:cd06606  157 GTKSLRGTPYWMAPEVIRG-EGYGRAADIWSLGCTVIEMATGKPPWSELGNPVAALFKI----GSSGEPPPI-------- 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 267 PRFndilgrhsrkrwerfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd06606  224 PEH-----------------------LSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
132-324 1.04e-25

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: 106.11  E-value: 1.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 132 DIRFYMYEILKALDYCHSMGIMHRDVKPHNV--------MIDHEHRK----------LRLIDWGLAEF---YHPNQeynv 190
Cdd:cd14134  116 HVQHIAKQLLEAVAFLHDLKLTHTDLKPENIllvdsdyvKVYNPKKKrqirvpkstdIKLIDFGSATFddeYHSSI---- 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 191 rVASRYFKGPELLVDYQmYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLGTEDLY---------DYIDKY 261
Cdd:cd14134  192 -VSTRHYRAPEVILGLG-WSYPCDVWSIGCILVEL-YTGELLFQTHDNLEHLAMMERILGPLPKRmirrakkgaKYFYFY 268
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504250 262 NIELDPRFNDILGR------HSRKRWERFVHSENQHLvsteaLDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14134  269 HGRLDWPEGSSSGRsikrvcKPLKRLMLLVDPEHRLL-----FDLIRKMLEYDPSKRITAKEALKHPFF 332
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
38-322 4.19e-25

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: 102.55  E-value: 4.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  38 DYQLVRKLGRGKYSEVFEAINIT------------------NNEkvvvkilkpvkkkkikreikilENLR---------G 90
Cdd:cd14007    1 DFEIGKPLGKGKFGNVYLAREKKsgfivalkvisksqlqksGLE----------------------HQLRreieiqshlR 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  91 GPNIITLLDIIKDPVSRTpaLVFEHVNNTD-FKQLYQT--LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHe 167
Cdd:cd14007   59 HPNILRLYGYFEDKKRIY--LILEYAPNGElYKELKKQkrFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGS- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 168 HRKLRLIDWGLAeFYHPNqeyNVRvasRYFKG------PElLVDYQMYDYSLDMWSLGCMLASMIFRKEPfFHGHDNYDQ 241
Cdd:cd14007  136 NGELKLADFGWS-VHAPS---NRR---KTFCGtldylpPE-MVEGKEYDYKVDIWSLGVLCYELLVGKPP-FESKSHQET 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 242 LVRIAKVlgtedLYDYIDKynieldprfndilgrhsrkrwerfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDH 321
Cdd:cd14007  207 YKRIQNV-----DIKFPSS--------------------------------VSPEAKDLISKLLQKDPSKRLSLEQVLNH 249

                 .
gi 528504250 322 S 322
Cdd:cd14007  250 P 250
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
112-324 6.42e-25

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: 102.68  E-value: 6.42e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 VFEHVNNTDFKQL---YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHPNQ-- 186
Cdd:cd05581   79 VLEYAPNGDLLEYirkYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMH-IKITDFGTAKVLGPDSsp 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 187 ------------EYNVRVASryFKG------PELLvDYQMYDYSLDMWSLGCMLASMIFRKEPfFHGHDNYDQLVRIAKV 248
Cdd:cd05581  158 estkgdadsqiaYNQARAAS--FVGtaeyvsPELL-NEKPAGKSSDLWALGCIIYQMLTGKPP-FRGSNEYLTFQKIVKL 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 249 lgtedlydyidkyNIELDPRFNDIlgrhsrkrwerfvhsenqhlvsteALDFLDKLLRYDHQARLTA------REAMDHS 322
Cdd:cd05581  234 -------------EYEFPENFPPD------------------------AKDLIQKLLVLDPSKRLGVnenggyDELKAHP 276

                 ..
gi 528504250 323 YF 324
Cdd:cd05581  277 FF 278
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
92-323 2.71e-24

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: 100.42  E-value: 2.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPvsRTPALVFEHVNNTD-FKQLYQ--TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEH 168
Cdd:cd14006   49 PRIIQLHEAYESP--TELVLILELCSGGElLDRLAErgSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRP 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 R-KLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELlVDYQMYDYSLDMWSLGcMLASMIFRKEPFFHGHDNYDQLVRIak 247
Cdd:cd14006  127 SpQIKIIDFGLARKLNPGEELKEIFGTPEFVAPEI-VNGEPVSLATDMWSIG-VLTYVLLSGLSPFLGEDDQETLANI-- 202
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 248 vlgtedlydyiDKYNIELDPRFNDilgrhsrkrwerfvhsenqhLVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14006  203 -----------SACRVDFSEEYFS--------------------SVSQEAKDFIRKLLVKEPRKRPTAQEALQHPW 247
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
38-323 3.06e-24

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: 100.63  E-value: 3.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  38 DYQLVRKLGRGKYSEVFEAINITNNEKVV----VKILKPVKKKKIKREIKILENLRG--GPNIITLLDIIKDPVSRtpAL 111
Cdd:cd14098    1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAikqiVKRKVAGNDKNLQLFQREINILKSleHPGIVRLIDWYEDDQHI--YL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 VFEHVNN---TDFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEH-RKLRLIDWGLAEFYHPNQE 187
Cdd:cd14098   79 VMEYVEGgdlMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpVIVKISDFGLAKVIHTGTF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 188 YNVRVASRYFKGPELLVDYQM-----YDYSLDMWSLGCMLASMIFRKEPFfhGHDNYDQLV-RIAKvlGTedlydyidkY 261
Cdd:cd14098  159 LVTFCGTMAYLAPEILMSKEQnlqggYSNLVDMWSVGCLVYVMLTGALPF--DGSSQLPVEkRIRK--GR---------Y 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528504250 262 NIELDPRFNdilgrhsrkrwerfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14098  226 TQPPLVDFN----------------------ISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
93-325 4.10e-24

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: 102.03  E-value: 4.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIKDPVS----RTPALVFEHVNNTDFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEH 168
Cdd:cd07876   81 NIISLLNVFTPQKSleefQDVYLVMELMDANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 rKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDYQmYDYSLDMWSLGCMLASMIfRKEPFFHGHDNYDQLVRIAKV 248
Cdd:cd07876  161 -TLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMG-YKENVDIWSVGCIMGELV-KGSVIFQGTDHIDQWNKVIEQ 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 249 LGTED------LYDYIDKYnIELDPRFNDILGRHSRKRWERFVHSENQHLVSTEALDFLDKLLRYDHQARLTAREAMDHS 322
Cdd:cd07876  238 LGTPSaefmnrLQPTVRNY-VENRPQYPGISFEELFPDWIFPSESERDKLKTSQARDLLSKMLVIDPDKRISVDEALRHP 316

                 ...
gi 528504250 323 YFY 325
Cdd:cd07876  317 YIT 319
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
39-232 6.04e-24

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: 99.58  E-value: 6.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNN------EKVVVKILKPVKKKKIKREIKILENLRGgPNIITLLDIIKDPvsRTPALV 112
Cdd:cd14014    2 YRLVRLLGRGGMGEVYRARDTLLGrpvaikVLRPELAEDEEFRERFLREARALARLSH-PNIVRVYDVGEDD--GRPYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 113 FEHVNNTDFKQLYQTLSDYDIRF---YMYEILKALDYCHSMGIMHRDVKPHNVMIDHEhRKLRLIDWGLAEFYHPNQEY- 188
Cdd:cd14014   79 MEYVEGGSLADLLRERGPLPPREalrILAQIADALAAAHRAGIVHRDIKPANILLTED-GRVKLTDFGIARALGDSGLTq 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 528504250 189 -NVRVASRYFKGPELLVDYQmYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14014  158 tGSVLGTPAYMAPEQARGGP-VDPRSDIYSLGVVLYELLTGRPPF 201
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
92-238 1.31e-23

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: 98.92  E-value: 1.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPvSRTPALVFEHVNNTDFKQL---YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEH 168
Cdd:cd13994   57 PNIVKVLDLCQDL-HGKWCLVMEYCPGGDLFTLiekADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDG 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 rKLRLIDWGLAEFYHPNQEYNvrvaSRYFKG---------PELLVDYQmYD-YSLDMWSLGCMLASMIFRKEPFFHGHDN 238
Cdd:cd13994  136 -VLKLTDFGTAEVFGMPAEKE----SPMSAGlcgsepymaPEVFTSGS-YDgRAVDVWSCGIVLFALFTGRFPWRSAKKS 209
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
92-324 1.47e-23

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: 100.24  E-value: 1.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRT---PALVFEhVNNTDFKQLYQT---LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMID 165
Cdd:cd07859   59 PDIVEIKHIMLPPSRREfkdIYVVFE-LMESDLHQVIKAnddLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILAN 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 166 HEHrKLRLIDWGLAEFYHPNQEYNV----RVASRYFKGPELLVD-YQMYDYSLDMWSLGCMLASMIFRKePFFHGHDNYD 240
Cdd:cd07859  138 ADC-KLKICDFGLARVAFNDTPTAIfwtdYVATRWYRAPELCGSfFSKYTPAIDIWSIGCIFAEVLTGK-PLFPGKNVVH 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 241 QLVRIAKVLGTEDLyDYIDKYNIELDPRF-NDILGRHSRKRWERFVHSENQhlvsteALDFLDKLLRYDHQARLTAREAM 319
Cdd:cd07859  216 QLDLITDLLGTPSP-ETISRVRNEKARRYlSSMRKKQPVPFSQKFPNADPL------ALRLLERLLAFDPKDRPTAEEAL 288

                 ....*
gi 528504250 320 DHSYF 324
Cdd:cd07859  289 ADPYF 293
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
111-324 3.69e-23

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: 97.67  E-value: 3.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFKQL---YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE-HrkLRLIDWGLAEF----- 181
Cdd:cd05579   70 LVMEYLPGGDLYSLlenVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANgH--LKLTDFGLSKVglvrr 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 182 ----YHPNQEYNVR-VASRYFKG------PELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFfhgHDNYdqlvriakvlg 250
Cdd:cd05579  148 qiklSIQKKSNGAPeKEDRRIVGtpdylaPEILLG-QGHGKTVDWWSLGVILYEFLVGIPPF---HAET----------- 212
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 251 TEDLYDYIDKYNIEldprfndilgrhsrkrWERFVHsenqhlVSTEALDFLDKLLRYDHQARLTAR---EAMDHSYF 324
Cdd:cd05579  213 PEEIFQNILNGKIE----------------WPEDPE------VSDEAKDLISKLLTPDPEKRLGAKgieEIKNHPFF 267
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
111-324 1.18e-22

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: 97.32  E-value: 1.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFKQL----YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV-MIDHEHRKLRLIDWGLAEFyhPN 185
Cdd:cd14212   79 IVFELLGVNLYELLkqnqFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENIlLVNLDSPEIKLIDFGSACF--EN 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 186 QEYNVRVASRYFKGPELLVDYQmYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLGT-------------- 251
Cdd:cd14212  157 YTLYTYIQSRFYRSPEVLLGLP-YSTAIDMWSLGCIAAEL-FLGLPLFPGNSEYNQLSRIIEMLGMppdwmlekgkntnk 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 252 ----------------EDLYDYIDKYNIELDPR---FN-----DILGRHSRKRwERFVHSENQHLVSTEALDFLDKLLRY 307
Cdd:cd14212  235 ffkkvaksggrstyrlKTPEEFEAENNCKLEPGkryFKyktleDIIMNYPMKK-SKKEQIDKEMETRLAFIDFLKGLLEY 313
                        250
                 ....*....|....*..
gi 528504250 308 DHQARLTAREAMDHSYF 324
Cdd:cd14212  314 DPKKRWTPDQALNHPFI 330
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
39-232 1.22e-22

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


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 96.27  E-value: 1.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINI-TNNEKVVVKILKPVKKKKIKREIKILENLR---------GGPNIITLLDIIKDPVSRt 108
Cdd:cd13993    2 YQLISPIGEGAYGVVYLAVDLrTGRKYAIKCLYKSGPNSKDGNDFQKLPQLReidlhrrvsRHPNIITLHDVFETEVAI- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 109 pALVFEHVNNTDF------KQLYQTlSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLA--E 180
Cdd:cd13993   81 -YIVLEYCPNGDLfeaiteNRIYVG-KTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGTVKLCDFGLAttE 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 181 FYhpnqEYNVRVASRYFKGPELLVDY----QMYD-YSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd13993  159 KI----SMDFGVGSEFYMAPECFDEVgrslKGYPcAAGDIWSLGIILLNLTFGRNPW 211
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
92-323 1.48e-22

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: 97.48  E-value: 1.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIkdpvsrTPALVFEhvnntDFKQLY--------------QTLSDYD-IRFYMYEILKALDYCHSMGIMHRD 156
Cdd:cd07850   59 KNIIGLLNVF------TPQKSLE-----EFQDVYlvmelmdanlcqviQMDLDHErMSYLLYQMLCGIKHLHSAGIIHRD 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 157 VKPHNVMIDHEHrKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDYQmYDYSLDMWSLGCMLASMIfRKEPFFHGH 236
Cdd:cd07850  128 LKPSNIVVKSDC-TLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMG-YKENVDIWSVGCIMGEMI-RGTVLFPGT 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 237 DNYDQLVRIAKVLGTEDlYDYIDKynieLDPRFNDIL---GRHSRKRWERFV--------HSENQHLVSTEALDFLDKLL 305
Cdd:cd07850  205 DHIDQWNKIIEQLGTPS-DEFMSR----LQPTVRNYVenrPKYAGYSFEELFpdvlfppdSEEHNKLKASQARDLLSKML 279
                        250
                 ....*....|....*...
gi 528504250 306 RYDHQARLTAREAMDHSY 323
Cdd:cd07850  280 VIDPEKRISVDDALQHPY 297
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
111-324 4.51e-22

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: 95.85  E-value: 4.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVN--------NTDFKQLYQTLsdydIRFYMYEILKALDYCHS--MGIMHRDVKPHNVMIDHEHRK-LRLIDWGLA 179
Cdd:cd14226   92 LVFELLSynlydllrNTNFRGVSLNL----TRKFAQQLCTALLFLSTpeLSIIHCDLKPENILLCNPKRSaIKIIDFGSS 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 180 efYHPNQEYNVRVASRYFKGPELLVdYQMYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLG--------- 250
Cdd:cd14226  168 --CQLGQRIYQYIQSRFYRSPEVLL-GLPYDLAIDMWSLGCILVEM-HTGEPLFSGANEVDQMNKIVEVLGmppvhmldq 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 251 ----------TEDLYDYIDKYNIELDPRFN------DILGRHS-----RKRWERfVHSENQHLvstEALDFLDKLLRYDH 309
Cdd:cd14226  244 apkarkffekLPDGTYYLKKTKDGKKYKPPgsrklhEILGVETggpggRRAGEP-GHTVEDYL---KFKDLILRMLDYDP 319
                        250
                 ....*....|....*
gi 528504250 310 QARLTAREAMDHSYF 324
Cdd:cd14226  320 KTRITPAEALQHSFF 334
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
133-324 3.85e-20

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: 88.85  E-value: 3.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 133 IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLvDYQMYDYS 212
Cdd:cd05578  102 VKFYICEIVLALDYLHSKNIIHRDIKPDNILLD-EQGHVHITDFNIATKLTDGTLATSTSGTKPYMAPEVF-MRAGYSFA 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 213 LDMWSLGCMLASMIFRKEPfFHGHDNydqlvriakvlGTEDLYDYIDKYNIELDPrfndilgrhsrKRWerfvhsenqhl 292
Cdd:cd05578  180 VDWWSLGVTAYEMLRGKRP-YEIHSR-----------TSIEEIRAKFETASVLYP-----------AGW----------- 225
                        170       180       190
                 ....*....|....*....|....*....|...
gi 528504250 293 vSTEALDFLDKLLRYDHQARLTAREAM-DHSYF 324
Cdd:cd05578  226 -SEEAIDLINKLLERDPQKRLGDLSDLkNHPYF 257
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
85-324 5.96e-20

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: 88.56  E-value: 5.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  85 LENLRGGPNIITLLDIIKdpvsrTPA---LVFEHVNNTD-FKQLYQ--TLSDYDIRFYMYEILKALDYCHSMGIMHRDVK 158
Cdd:cd14093   62 LRQVSGHPNIIELHDVFE-----SPTfifLVFELCRKGElFDYLTEvvTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLK 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 159 PHNVMIDHEHrKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLvDYQMYD----YSL--DMWSLGCMLASMIFRKEPF 232
Cdd:cd14093  137 PENILLDDNL-NVKISDFGFATRLDEGEKLRELCGTPGYLAPEVL-KCSMYDnapgYGKevDMWACGVIMYTLLAGCPPF 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 233 FHghdnYDQLVRIAKVLGtedlydyiDKYNIElDPRFNDIlgrhsrkrwerfvhsenqhlvSTEALDFLDKLLRYDHQAR 312
Cdd:cd14093  215 WH----RKQMVMLRNIME--------GKYEFG-SPEWDDI---------------------SDTAKDLISKLLVVDPKKR 260
                        250
                 ....*....|..
gi 528504250 313 LTAREAMDHSYF 324
Cdd:cd14093  261 LTAEEALEHPFF 272
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
111-327 8.44e-20

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: 88.35  E-value: 8.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFK-QLYQT----LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPN 185
Cdd:cd05577   70 LVLTLMNGGDLKyHIYNVgtrgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLD-DHGHVRISDLGLAVEFKGG 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 186 QEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFfhghdnydqlvriakvlgtedlYDYIDKyniel 265
Cdd:cd05577  149 KKIKGRVGTHGYMAPEVLQKEVAYDFSVDWFALGCMLYEMIAGRSPF----------------------RQRKEK----- 201
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 266 dprfndiLGRHSRKRWERFVHSENQHLVSTEALDFLDKLLRYDHQARL-----TAREAMDHSYFYPI 327
Cdd:cd05577  202 -------VDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKDPERRLgcrggSADEVKEHPFFRSL 261
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
93-323 1.28e-19

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: 89.38  E-value: 1.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIkdpvsrTPALVFEHVNNT---------DFKQLYQTLSDYD-IRFYMYEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:cd07874   77 NIISLLNVF------TPQKSLEEFQDVylvmelmdaNLCQVIQMELDHErMSYLLYQMLCGIKHLHSAGIIHRDLKPSNI 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 163 MIDHEHrKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDYQmYDYSLDMWSLGCMLASMIfRKEPFFHGHDNYDQL 242
Cdd:cd07874  151 VVKSDC-TLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMG-YKENVDIWSVGCIMGEMV-RHKILFPGRDYIDQW 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 243 VRIAKVLGT------EDLYDYIDKYnIELDPRFNDILGRHSRKRWERFVHSENQHLVSTEALDFLDKLLRYDHQARLTAR 316
Cdd:cd07874  228 NKVIEQLGTpcpefmKKLQPTVRNY-VENRPKYAGLTFPKLFPDSLFPADSEHNKLKASQARDLLSKMLVIDPAKRISVD 306

                 ....*..
gi 528504250 317 EAMDHSY 323
Cdd:cd07874  307 EALQHPY 313
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
92-323 1.35e-19

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: 87.54  E-value: 1.35e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKdpvSRTPA-LVFEHVNNT---DFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMI--- 164
Cdd:cd14105   68 PNIITLHDVFE---NKTDVvLILELVAGGelfDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLldk 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 165 DHEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELlVDYQMYDYSLDMWSLGCMLASMIFRKEPFFhGHDNYDQLVR 244
Cdd:cd14105  145 NVPIPRIKLIDFGLAHKIEDGNEFKNIFGTPEFVAPEI-VNYEPLGLEADMWSIGVITYILLSGASPFL-GDTKQETLAN 222
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504250 245 IAKVLgtedlYDYIDKYnieldprfndilgrhsrkrwerFVHSenqhlvSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14105  223 ITAVN-----YDFDDEY----------------------FSNT------SELAKDFIRQLLVKDPRKRMTIQESLRHPW 268
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
128-323 2.61e-19

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: 86.89  E-value: 2.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVM-IDHEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELlVDY 206
Cdd:cd14193   99 LTELDTILFIKQICEGIQYMHQMYILHLDLKPENILcVSREANQVKIIDFGLARRYKPREKLRVNFGTPEFLAPEV-VNY 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 207 QMYDYSLDMWSLGcMLASMIFRKEPFFHGHDNYDQLVRIAKVlgtedlydyidKYNIElDPRFNDIlgrhsrkrwerfvh 286
Cdd:cd14193  178 EFVSFPTDMWSLG-VIAYMLLSGLSPFLGEDDNETLNNILAC-----------QWDFE-DEEFADI-------------- 230
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 528504250 287 senqhlvSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14193  231 -------SEEAKDFISKLLIKEKSWRMSASEALKHPW 260
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
93-323 5.15e-19

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: 87.41  E-value: 5.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIKDPVS----RTPALVFEhVNNTDFKQLYQTLSDYD-IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE 167
Cdd:cd07875   84 NIIGLLNVFTPQKSleefQDVYIVME-LMDANLCQVIQMELDHErMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 168 HrKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDYQmYDYSLDMWSLGCMLASMIFRKePFFHGHDNYDQLVRIAK 247
Cdd:cd07875  163 C-TLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMG-YKENVDIWSVGCIMGEMIKGG-VLFPGTDHIDQWNKVIE 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 248 VLGT------EDLYDYIDKYnIELDPRFndiLGRHSRKRWERFV---HSENQHLVSTEALDFLDKLLRYDHQARLTAREA 318
Cdd:cd07875  240 QLGTpcpefmKKLQPTVRTY-VENRPKY---AGYSFEKLFPDVLfpaDSEHNKLKASQARDLLSKMLVIDASKRISVDEA 315

                 ....*
gi 528504250 319 MDHSY 323
Cdd:cd07875  316 LQHPY 320
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
92-321 5.68e-19

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: 85.35  E-value: 5.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPvsRTPALVFEHVNNTDFKQL---YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMI--DH 166
Cdd:cd14009   52 PNIVRLYDVQKTE--DFIYLVLEYCAGGDLSQYirkRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstSG 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 167 EHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPFfhGHDNYDQLVRia 246
Cdd:cd14009  130 DDPVLKIADFGFARSLQPASMAETLCGSPLYMAPEIL-QFQKYDAKADLWSVGAILFEMLVGKPPF--RGSNHVQLLR-- 204
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 247 kvlgtedlydyidkyNIEldpRFNDILGRHSRkrwerfvhsenqHLVSTEALDFLDKLLRYDHQARLTAREAMDH 321
Cdd:cd14009  205 ---------------NIE---RSDAVIPFPIA------------AQLSPDCKDLLRRLLRRDPAERISFEEFFAH 249
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
85-324 7.08e-19

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: 85.44  E-value: 7.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  85 LENLRGGPNIITLLDIIkdpvsrTPALVFEHVNNTDFKqlyqtLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVM- 163
Cdd:cd14191   65 VDAFEEKANIVMVLEMV------SGGELFERIIDEDFE-----LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMc 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 164 IDHEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNyDQLV 243
Cdd:cd14191  134 VNKTGTKIKLIDFGLARRLENAGSLKVLFGTPEFVAPE-VINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDN-ETLA 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 244 RIakvlgTEDLYDYIDKynieldpRFNDIlgrhsrkrwerfvhsenqhlvSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14191  212 NV-----TSATWDFDDE-------AFDEI---------------------SDDAKDFISNLLKKDMKARLTCTQCLQHPW 258

                 .
gi 528504250 324 F 324
Cdd:cd14191  259 L 259
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
88-324 8.63e-19

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: 85.76  E-value: 8.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  88 LRGG--PNIITLLDIIKDpvSRTPALVFEHVNNTDF--KQLYQT-LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:cd14091   48 LRYGqhPNIITLRDVYDD--GNSVYLVTELLRGGELldRILRQKfFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNI 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 163 M-IDHEHR--KLRLIDWGLAE------------FYHPNqeynvrvasryFKGPELLvDYQMYDYSLDMWSLGCMLASMIF 227
Cdd:cd14091  126 LyADESGDpeSLRICDFGFAKqlraengllmtpCYTAN-----------FVAPEVL-KKQGYDAACDIWSLGVLLYTMLA 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 228 RKEPFFHGHDNydqlvriakvlgTEDlydyidkynieldprfnDILGRHSRKRWErfVHSENQHLVSTEALDFLDKLLRY 307
Cdd:cd14091  194 GYTPFASGPND------------TPE-----------------VILARIGSGKID--LSGGNWDHVSDSAKDLVRKMLHV 242
                        250
                 ....*....|....*..
gi 528504250 308 DHQARLTAREAMDHSYF 324
Cdd:cd14091  243 DPSQRPTAAQVLQHPWI 259
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
92-232 1.01e-18

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: 85.19  E-value: 1.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIkdpvsRTPA---LVFEHVNNtdfKQLYQ------TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:cd14077   73 PHICRLRDFL-----RTPNhyyMLFEYVDG---GQLLDyiishgKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENI 144
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504250 163 MIDhEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLvDYQMY-DYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14077  145 LIS-KSGNIKIIDFGLSNLYDPRRLLRTFCGSLYFAAPELL-QAQPYtGPEVDVWSFGVVLYVLVCGKVPF 213
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
92-324 1.49e-18

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: 84.54  E-value: 1.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKdpvsrTPALVF------EHVNNTDFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMID 165
Cdd:cd14080   62 PNIIQVYSIFE-----RGSKVFifmeyaEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLD 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 166 hEHRKLRLIDWGLAEFYHPNQEynvRVASRYFKG------PELLVDyQMYDYSL-DMWSLGCMLASMIFRKEPFfhghdn 238
Cdd:cd14080  137 -SNNNVKLSDFGFARLCPDDDG---DVLSKTFCGsaayaaPEILQG-IPYDPKKyDIWSLGVILYIMLCGSMPF------ 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 239 ydqlvriakvlgtedlydyiDKYNIELdprfndILGRHSRKRWErfvHSENQHLVSTEALDFLDKLLRYDHQARLTAREA 318
Cdd:cd14080  206 --------------------DDSNIKK------MLKDQQNRKVR---FPSSVKKLSPECKDLIDQLLEPDPTKRATIEEI 256

                 ....*.
gi 528504250 319 MDHSYF 324
Cdd:cd14080  257 LNHPWL 262
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
133-324 2.00e-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: 85.45  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 133 IRFYMYEILKALDYCHSMGIMHRDVKPHNVM--------IDHEHRK----------LRLIDWGLAEFYHpnQEYNVRVAS 194
Cdd:cd14214  119 IRHMAYQLCHALKFLHENQLTHTDLKPENILfvnsefdtLYNESKSceeksvkntsIRVADFGSATFDH--EHHTTIVAT 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 195 RYFKGPELLVDYQmYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLG---TEDLY-----DYIDKYNIELD 266
Cdd:cd14214  197 RHYRPPEVILELG-WAQPCDVWSLGCILFEY-YRGFTLFQTHENREHLVMMEKILGpipSHMIHrtrkqKYFYKGSLVWD 274
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528504250 267 PRFNDilGRHSRKRWERF----VHSENQHlvsTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14214  275 ENSSD--GRYVSENCKPLmsymLGDSLEH---TQLFDLLRRMLEFDPALRITLKEALLHPFF 331
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
38-233 2.22e-18

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: 83.86  E-value: 2.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  38 DYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREI------KILENLRGgPNIITLLD--------IIkd 103
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMDAKARQdclkeiDLLQQLNH-PNIIKYLAsfiennelNI-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 104 pvsrtpalVFEHVNNTDFKQLY-------QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDW 176
Cdd:cd08224   78 --------VLELADAGDLSRLIkhfkkqkRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGV-VKLGDL 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 177 GLAEFYHPNQ-EYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFF 233
Cdd:cd08224  149 GLGRFFSSKTtAAHSLVGTPYYMSPERIRE-QGYDFKSDIWSLGCLLYEMAALQSPFY 205
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
85-324 2.73e-18

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: 84.25  E-value: 2.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  85 LENLRGGPNIITLLDIIKDpvSRTPALVFEHVNNTD-FKQLYQ--TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHN 161
Cdd:cd14181   69 LRQVSGHPSIITLIDSYES--STFIFLVFDLMRRGElFDYLTEkvTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPEN 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 162 VMIDHEhRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELL---VD--YQMYDYSLDMWSLGCMLASMIFRKEPFFHGH 236
Cdd:cd14181  147 ILLDDQ-LHIKLSDFGFSCHLEPGEKLRELCGTPGYLAPEILkcsMDetHPGYGKEVDLWACGVILFTLLAGSPPFWHRR 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 237 dnydQLVRIAKVLgtEDLYDYIDKyniELDPRfndilgrhsrkrwerfvhsenqhlvSTEALDFLDKLLRYDHQARLTAR 316
Cdd:cd14181  226 ----QMLMLRMIM--EGRYQFSSP---EWDDR-------------------------SSTVKDLISRLLVVDPEIRLTAE 271

                 ....*...
gi 528504250 317 EAMDHSYF 324
Cdd:cd14181  272 QALQHPFF 279
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
88-323 2.92e-18

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: 84.31  E-value: 2.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  88 LRGG--PNIITLLDIIKDpvSRTPALVFEHVNNTDF--KQLYQTL-SDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:cd14175   49 LRYGqhPNIITLKDVYDD--GKHVYLVTELMRGGELldKILRQKFfSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNI 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 163 MIDHEH---RKLRLIDWGLA-EFYHPNQEYNVRVASRYFKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDN 238
Cdd:cd14175  127 LYVDESgnpESLRICDFGFAkQLRAENGLLMTPCYTANFVAPEVL-KRQGYDEGCDIWSLGILLYTMLAGYTPFANGPSD 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 239 YDQlvriakvlgtedlydyidkynieldprfnDILGRHSRKRWErfVHSENQHLVSTEALDFLDKLLRYDHQARLTAREA 318
Cdd:cd14175  206 TPE-----------------------------EILTRIGSGKFT--LSGGNWNTVSDAAKDLVSKMLHVDPHQRLTAKQV 254

                 ....*
gi 528504250 319 MDHSY 323
Cdd:cd14175  255 LQHPW 259
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
93-232 3.50e-18

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: 83.90  E-value: 3.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIKDPVSrtPALVFEHVNNTDFKQLYQ---TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHR 169
Cdd:cd14201   66 NIVALYDVQEMPNS--VFLVMEYCNGGDLADYLQakgTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASR 143
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504250 170 K--------LRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14201  144 KkssvsgirIKIADFGFARYLQSNMMAATLCGSPMYMAPEVIMS-QHYDAKADLWSIGTVIYQCLVGKPPF 213
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
44-324 4.16e-18

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act 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 (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. 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 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 84.34  E-value: 4.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  44 KLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLR--GGPNIITLLDIIKDPVSRTPALVFEHVNN--- 118
Cdd:cd07868   24 KVGRGTYGHVYKAKRKDGKDDKDYALKQIEGTGISMSACREIALLRelKHPNVISLQKVFLSHADRKVWLLFDYAEHdlw 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 119 --TDFKQLYQT------LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMI---DHEHRKLRLIDWGLAEFYH---- 183
Cdd:cd07868  104 hiIKFHRASKAnkkpvqLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgeGPERGRVKIADMGFARLFNsplk 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 184 PNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIfRKEPFFHGHD---------NYDQLVRIAKVLGTEDL 254
Cdd:cd07868  184 PLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELL-TSEPIFHCRQediktsnpyHHDQLDRIFNVMGFPAD 262
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504250 255 YDYIDkynIELDPRFNDILGRHSRKRWER--FVHSENQHLVS--TEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07868  263 KDWED---IKKMPEHSTLMKDFRRNTYTNcsLIKYMEKHKVKpdSKAFHLLQKLLTMDPIKRITSEQAMQDPYF 333
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
92-323 5.29e-18

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: 83.08  E-value: 5.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTpaLVFEHVNNT---DFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEH 168
Cdd:cd14196   68 PNIITLHDVYENRTDVV--LILELVSGGelfDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKN 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 ---RKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFhGHDNYDQLVRI 245
Cdd:cd14196  146 ipiPHIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFL-GDTKQETLANI 223
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 246 AKVlgtedlydyidkyNIELDPRFndilgrhsrkrwerFVHSenqhlvSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14196  224 TAV-------------SYDFDEEF--------------FSHT------SELAKDFIRKLLVKETRKRLTIQEALRHPW 268
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
92-273 7.34e-18

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: 82.30  E-value: 7.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPvsrtpalvFEHVNNTDFKQ--LYQTLSD------YDIRFYMYEILKALDYCHSMGIMHRDVKPHNVM 163
Cdd:cd14002   60 PNIIEMLDSFETK--------KEFVVVTEYAQgeLFQILEDdgtlpeEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNIL 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 164 IDhEHRKLRLIDWGLAEfyhpNQEYNVRVAsRYFKG------PElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFhgHD 237
Cdd:cd14002  132 IG-KGGVVKLCDFGFAR----AMSCNTLVL-TSIKGtplymaPE-LVQEQPYDHTADLWSLGCILYELFVGQPPFY--TN 202
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 528504250 238 NYDQLVRIAkvlgtedLYDYIdKYNIELDPRFNDIL 273
Cdd:cd14002  203 SIYQLVQMI-------VKDPV-KWPSNMSPEFKSFL 230
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
37-323 7.62e-18

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: 82.83  E-value: 7.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRKLGRGKYSEV---FE-------AINITN-NEKVVVKILKPVKKKKIKREIKILENLRGgPNIITLLDIIKDPV 105
Cdd:cd14084    6 KKYIMSRTLGSGACGEVklaYDkstckkvAIKIINkRKFTIGSRREINKPRNIETEIEILKKLSH-PCIIKIEDFFDAED 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 106 SRTpaLVFEHVNN-------TDFKQLYQTLSdydiRFYMYEILKALDYCHSMGIMHRDVKPHNVMI--DHEHRKLRLIDW 176
Cdd:cd14084   85 DYY--IVLELMEGgelfdrvVSNKRLKEAIC----KLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssQEEECLIKITDF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 177 GLAEFYHPNQEYNVRVASRYFKGPELLVDYQMYDYS--LDMWSLGCMLASMIFRKEPFFHghdnydqlvriakvlgtedl 254
Cdd:cd14084  159 GLSKILGETSLMKTLCGTPTYLAPEVLRSFGTEGYTraVDCWSLGVILFICLSGYPPFSE-------------------- 218
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 255 ydyiDKYNIELDprfNDIL-GRHsrkrweRFVHSENQHlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14084  219 ----EYTQMSLK---EQILsGKY------TFIPKAWKN-VSEEAKDLVKKMLVVDPSRRPSIEEALEHPW 274
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
111-327 9.76e-18

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: 82.14  E-value: 9.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFKQLYQT---LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQE 187
Cdd:cd05611   74 LVMEYLNGGDCASLIKTlggLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLID-QTGHLKLTDFGLSRNGLEKRH 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 188 YNVRVASRYFKGPELLV---DYQMYDYsldmWSLGCMLASMIFRKEPFfhgHDNYDQLVriakvlgtedlydyidkynie 264
Cdd:cd05611  153 NKKFVGTPDYLAPETILgvgDDKMSDW----WSLGCVIFEFLFGYPPF---HAETPDAV--------------------- 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 265 ldprFNDILGRhsRKRWerfvHSENQHLVSTEALDFLDKLLRYDHQARLTA---REAMDHSYFYPI 327
Cdd:cd05611  205 ----FDNILSR--RINW----PEEVKEFCSPEAVDLINRLLCMDPAKRLGAngyQEIKSHPFFKSI 260
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
92-324 1.09e-17

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: 82.27  E-value: 1.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPvsRTPALVFEHVNNTD-FKQLYQT---LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVM-IDH 166
Cdd:cd14190   61 RNLIQLYEAIETP--NEIVLFMEYVEGGElFERIVDEdyhLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILcVNR 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 167 EHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDnydqlvria 246
Cdd:cd14190  139 TGHQVKIIDFGLARRYNPREKLKVNFGTPEFLSPE-VVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDD--------- 208
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 247 kvlgTEDLydyidkynieldprfNDILGRHSRKRWERFVHsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14190  209 ----TETL---------------NNVLMGNWYFDEETFEH------VSDEAKDFVSNLIIKERSARMSATQCLKHPWL 261
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
44-324 1.12e-17

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. 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 CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 83.19  E-value: 1.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  44 KLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLR--GGPNIITLLDIIKDPVSRTPALVFEHVN---- 117
Cdd:cd07867    9 KVGRGTYGHVYKAKRKDGKDEKEYALKQIEGTGISMSACREIALLRelKHPNVIALQKVFLSHSDRKVWLLFDYAEhdlw 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 118 -----------NTDFKQLYQTLsdydIRFYMYEILKALDYCHSMGIMHRDVKPHNVMI---DHEHRKLRLIDWGLAEFYH 183
Cdd:cd07867   89 hiikfhraskaNKKPMQLPRSM----VKSLLYQILDGIHYLHANWVLHRDLKPANILVmgeGPERGRVKIADMGFARLFN 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 184 ----PNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIfRKEPFFHGHD---------NYDQLVRIAKVLG 250
Cdd:cd07867  165 splkPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELL-TSEPIFHCRQediktsnpfHHDQLDRIFSVMG 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 251 TEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSEnQHLVSTEALDF--LDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd07867  244 FPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYME-KHKVKPDSKVFllLQKLLTMDPTKRITSEQALQDPYF 318
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
111-341 1.35e-17

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: 82.59  E-value: 1.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFKQLYqtlSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRK--LRLIDWGLA-EFYHPNQE 187
Cdd:cd14094   92 LCFEIVKRADAGFVY---SEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapVKLGGFGVAiQLGESGLV 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 188 YNVRVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFfhghdnydqlvriakvLGT-EDLYDYIDKYNIELD 266
Cdd:cd14094  169 AGGRVGTPHFMAPE-VVKREPYGKPVDVWGCGVILFILLSGCLPF----------------YGTkERLFEGIIKGKYKMN 231
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 267 PRfndilgrhsrkRWERfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHsyfyPIVKDQGRGAPAAGMA 341
Cdd:cd14094  232 PR-----------QWSH---------ISESAKDLVRRMLMLDPAERITVYEALNH----PWIKERDRYAYRIHLP 282
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
92-324 1.51e-17

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: 81.53  E-value: 1.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDpvSRTPALVFEHVNNTD-FKQLYQ--TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEH 168
Cdd:cd14081   61 PNVLKLYDVYEN--KKYLYLVLEYVSGGElFDYLVKkgRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLD-EK 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 RKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPElLVDYQMYD-YSLDMWSLGCMLASMIFRKEPFfhGHDNYDQLVRIAK 247
Cdd:cd14081  138 NNIKIADFGMASLQPEGSLLETSCGSPHYACPE-VIKGEKYDgRKADIWSCGVILYALLVGALPF--DDDNLRQLLEKVK 214
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 248 VlgtedlydyiDKYNIeldPRFndilgrhsrkrwerfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14081  215 R----------GVFHI---PHF-----------------------ISPDAQDLLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
112-323 1.67e-17

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: 81.83  E-value: 1.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 VFEHVNNTDFKqlyqtLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVM-IDHEHRKLRLIDWGLAEFYHPNQEYNV 190
Cdd:cd14104   83 IFERITTARFE-----LNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIyCTRRGSYIKIIEFGQSRQLKPGDKFRL 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 191 RVASRYFKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPFFhGHDNYDQLVRIakvlgtedlydyidkynIELDPRFN 270
Cdd:cd14104  158 QYTSAEFYAPEVH-QHESVSTATDMWSLGCLVYVLLSGINPFE-AETNQQTIENI-----------------RNAEYAFD 218
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528504250 271 DilgrhsrkrwERFVHsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14104  219 D----------EAFKN------ISIEALDFVDRLLVKERKSRMTAQEALNHPW 255
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
93-324 1.71e-17

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: 81.55  E-value: 1.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIKDPVSRTpaLVFEHVNNTD-FKQL----YQtLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVM-IDH 166
Cdd:cd14192   62 NLIQLYDAFESKTNLT--LIMEYVDGGElFDRItdesYQ-LTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNS 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 167 EHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDnydqlvria 246
Cdd:cd14192  139 TGNQIKIIDFGLARRYKPREKLKVNFGTPEFLAPE-VVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETD--------- 208
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 247 kvlgtEDLYDYIDKYNIELDprfndilgrhsrkrwerfvhSENQHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14192  209 -----AETMNNIVNCKWDFD--------------------AEAFENLSEEAKDFISRLLVKEKSCRMSATQCLKHEWL 261
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
85-323 1.90e-17

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: 81.49  E-value: 1.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  85 LENLRGGPNIITLLDIikdPVSRTPALVF---EHvNNTDF-----KQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRD 156
Cdd:cd14131   53 LKKLKGSDRIIQLYDY---EVTDEDDYLYmvmEC-GEIDLatilkKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSD 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 157 VKPHN-VMIDhehRKLRLIDWGLAEFYHPNQEYNVR---VASRYFKGPELLVDYQMYD---------YSLDMWSLGCMLA 223
Cdd:cd14131  129 LKPANfLLVK---GRLKLIDFGIAKAIQNDTTSIVRdsqVGTLNYMSPEAIKDTSASGegkpkskigRPSDVWSLGCILY 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 224 SMIFRKEPFFHGHDNYDQLVRIakvlgtedlydyID-KYNIEldprFNDIlgrhsrkrwerfvhsenqhlVSTEALDFLD 302
Cdd:cd14131  206 QMVYGKTPFQHITNPIAKLQAI------------IDpNHEIE----FPDI--------------------PNPDLIDVMK 249
                        250       260
                 ....*....|....*....|.
gi 528504250 303 KLLRYDHQARLTAREAMDHSY 323
Cdd:cd14131  250 RCLQRDPKKRPSIPELLNHPF 270
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
126-324 3.15e-17

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: 80.68  E-value: 3.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 126 QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLA---EFYH---------PNqeynvrva 193
Cdd:cd14099   96 KALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLD-ENMNVKIGDFGLAarlEYDGerkktlcgtPN-------- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 194 sryFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFfhghDNYDqlvriakvlgTEDLYDYIdkynieldprfndil 273
Cdd:cd14099  167 ---YIAPEVLEKKKGHSFEVDIWSLGVILYTLLVGKPPF----ETSD----------VKETYKRI--------------- 214
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528504250 274 gRHSRKRWERFVHsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14099  215 -KKNEYSFPSHLS------ISDEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
92-323 9.39e-17

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: 79.68  E-value: 9.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTpaLVFEHVNNT---DFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMI---D 165
Cdd:cd14194   68 PNVITLHEVYENKTDVI--LILELVAGGelfDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLldrN 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 166 HEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFhGHDNYDQLVRI 245
Cdd:cd14194  146 VPKPRIKIIDFGLAHKIDFGNEFKNIFGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFL-GDTKQETLANV 223
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 246 AKVlgtedlydyidkyNIELDPRFndilgrhsrkrwerFVHSenqhlvSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14194  224 SAV-------------NYEFEDEY--------------FSNT------SALAKDFIRRLLVKDPKKRMTIQDSLQHPW 268
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
90-232 9.76e-17

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: 80.08  E-value: 9.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  90 GGPNIITLLDIIKDPVSRTpaLVFEHVNNTDF---KQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMI-- 164
Cdd:cd14179   60 GHPNIVKLHEVYHDQLHTF--LVMELLKGGELlerIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtd 137
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504250 165 DHEHRKLRLIDWGLAEFYHP-NQEYNVRVASRYFKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14179  138 ESDNSEIKIIDFGFARLKPPdNQPLKTPCFTLHYAAPELL-NYNGYDESCDLWSLGVILYTMLSGQVPF 205
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
111-324 1.41e-16

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: 80.02  E-value: 1.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFKQLyqtLSDYDI------RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE-HrkLRLIDWGLA---- 179
Cdd:cd05573   78 LVMEYMPGGDLMNL---LIKYDVfpeetaRFYIAELVLALDSLHKLGFIHRDIKPDNILLDADgH--IKLADFGLCtkmn 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 180 ----EFYHPNQEYNV----RVASRYFKGPELLV---------DY--------QMYDYSLDMWSLGCMLASMIFRKEPFfh 234
Cdd:cd05573  153 ksgdRESYLNDSVNTlfqdNVLARRRPHKQRRVraysavgtpDYiapevlrgTGYGPECDWWSLGVILYEMLYGFPPF-- 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 235 ghdnYDQLVRIAkvlgtedlydyidkynieldprFNDILgrhsrkRWERFVHSENQHLVSTEALDFLDKLLRyDHQARLT 314
Cdd:cd05573  231 ----YSDSLVET----------------------YSKIM------NWKESLVFPDDPDVSPEAIDLIRRLLC-DPEDRLG 277
                        250
                 ....*....|.
gi 528504250 315 -AREAMDHSYF 324
Cdd:cd05573  278 sAEEIKAHPFF 288
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
125-323 1.46e-16

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: 79.12  E-value: 1.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 125 YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYHPNQEYNVRVASR-------YF 197
Cdd:cd06628  100 YGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKG-GIKISDFGISKKLEANSLSTKNNGARpslqgsvFW 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 198 KGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFfhghDNYDQLVRIAKVLGTedlydyidkynieLDPRFNDIlgrhs 277
Cdd:cd06628  179 MAPE-VVKQTSYTRKADIWSLGCLVVEMLTGTHPF----PDCTQMQAIFKIGEN-------------ASPTIPSN----- 235
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 528504250 278 rkrwerfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd06628  236 ---------------ISSEARDFLEKTFEIDHNKRPTADELLKHPF 266
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
134-331 1.53e-16

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: 79.67  E-value: 1.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE-HrkLRLIDWGLA-EFYHPNQEYNVRVASRYFKGPELLVDyQMYDY 211
Cdd:cd05575   99 RFYAAEIASALGYLHSLNIIYRDLKPENILLDSQgH--VVLTDFGLCkEGIEPSDTTSTFCGTPEYLAPEVLRK-QPYDR 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 212 SLDMWSLGCMLASMIFRKEPFfhghdnydqlvriakvlgtedlydyidkYNIELDPRFNDILGRHSRKRwerfvhsenqH 291
Cdd:cd05575  176 TVDWWCLGAVLYEMLYGLPPF----------------------------YSRDTAEMYDNILHKPLRLR----------T 217
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 528504250 292 LVSTEALDFLDKLLRYDHQARLTAR----EAMDHSYFYPIVKDQ 331
Cdd:cd05575  218 NVSPSARDLLEGLLQKDRTKRLGSGndflEIKNHSFFRPINWDD 261
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
38-233 1.67e-16

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: 78.92  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  38 DYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLR-----GGPNIITLLD-IIKDpvsRTPAL 111
Cdd:cd08228    3 NFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKARQDCVKEIDllkqlNHPNVIKYLDsFIED---NELNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 VFEHVNNTD-------FKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYHP 184
Cdd:cd08228   80 VLELADAGDlsqmikyFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATG-VVKLGDLGLGRFFSS 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 528504250 185 -NQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFF 233
Cdd:cd08228  159 kTTAAHSLVGTPYYMSPERIHE-NGYNFKSDIWSLGCLLYEMAALQSPFY 207
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
85-324 2.44e-16

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: 78.42  E-value: 2.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  85 LENLRGGPNIITLLDIIKDpvSRTPALVFEHVNNTD-FKQLYQ--TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHN 161
Cdd:cd14182   63 LRKVSGHPNIIQLKDTYET--NTFFFLVFDLMKKGElFDYLTEkvTLSEKETRKIMRALLEVICALHKLNIVHRDLKPEN 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 162 VMIDhEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLV-----DYQMYDYSLDMWSLGCMLASMIFRKEPFFHgh 236
Cdd:cd14182  141 ILLD-DDMNIKLTDFGFSCQLDPGEKLREVCGTPGYLAPEIIEcsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWH-- 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 237 dnYDQLVRIAKVLGTEdlYDYIdkynielDPRFNDilgrhsrkrwerfvhsenqhlVSTEALDFLDKLLRYDHQARLTAR 316
Cdd:cd14182  218 --RKQMLMLRMIMSGN--YQFG-------SPEWDD---------------------RSDTVKDLISRFLVVQPQKRYTAE 265

                 ....*...
gi 528504250 317 EAMDHSYF 324
Cdd:cd14182  266 EALAHPFF 273
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
88-323 2.76e-16

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: 78.52  E-value: 2.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  88 LRGG--PNIITLLDIIKDpvSRTPALVFEHVNNTDF--KQLYQT-LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:cd14178   51 LRYGqhPNIITLKDVYDD--GKFVYLVMELMRGGELldRILRQKcFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNI 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 163 MIDHEH---RKLRLIDWGLA-EFYHPNQEYNVRVASRYFKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDN 238
Cdd:cd14178  129 LYMDESgnpESIRICDFGFAkQLRAENGLLMTPCYTANFVAPEVL-KRQGYDAACDIWSLGILLYTMLAGFTPFANGPDD 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 239 YDQ--LVRIAKvlgtedlydyiDKYNIeldprfndilgrhSRKRWERfvhsenqhlVSTEALDFLDKLLRYDHQARLTAR 316
Cdd:cd14178  208 TPEeiLARIGS-----------GKYAL-------------SGGNWDS---------ISDAAKDIVSKMLHVDPHQRLTAP 254

                 ....*..
gi 528504250 317 EAMDHSY 323
Cdd:cd14178  255 QVLRHPW 261
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
92-324 3.57e-16

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: 77.68  E-value: 3.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTPALVFEHVNNTdfkqlYQTLSDY--DIRF-------YMYEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:cd14119   54 RNVIKLVDVLYNEEKQKLYMVMEYCVGG-----LQEMLDSapDKRLpiwqahgYFVQLIDGLEYLHSQGIIHKDIKPGNL 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 163 MIDHEHRkLRLIDWGLAEFYHP-NQEYNVRVA--SRYFKGPELLVDYQMYD-YSLDMWSLGCMLASMIFRKEPfFHGHDN 238
Cdd:cd14119  129 LLTTDGT-LKISDFGVAEALDLfAEDDTCTTSqgSPAFQPPEIANGQDSFSgFKVDIWSAGVTLYNMTTGKYP-FEGDNI 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 239 YdqlvriakvlgteDLYDYIDKYNIELDPrfndilgrhsrkrwerfvhsenqhLVSTEALDFLDKLLRYDHQARLTAREA 318
Cdd:cd14119  207 Y-------------KLFENIGKGEYTIPD------------------------DVDPDLQDLLRGMLEKDPEKRFTIEQI 249

                 ....*.
gi 528504250 319 MDHSYF 324
Cdd:cd14119  250 RQHPWF 255
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
122-323 3.98e-16

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 79.02  E-value: 3.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 122 KQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRK-LRLIDWGLAEFYHpnQEYNVRVASRYFKGP 200
Cdd:cd14224  159 KNKFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSgIKVIDFGSSCYEH--QRIYTYIQSRFYRAP 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 201 ELLVDYQmYDYSLDMWSLGCMLASMIfRKEPFFHGHDNYDQLVRIAKVLG--TEDLYDYIDK----YNIELDPRFNDIL- 273
Cdd:cd14224  237 EVILGAR-YGMPIDMWSFGCILAELL-TGYPLFPGEDEGDQLACMIELLGmpPQKLLETSKRaknfISSKGYPRYCTVTt 314
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 274 ----------GRHSRKRWERfvHSENQHLVS-------TEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14224  315 lpdgsvvlngGRSRRGKMRG--PPGSKDWVTalkgcddPLFLDFLKRCLEWDPAARMTPSQALRHPW 379
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
133-324 4.17e-16

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: 78.42  E-value: 4.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 133 IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPNQ--EYNVrvaSRYFKGPELLVDYqMYD 210
Cdd:cd14135  107 VRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNTLKLCDFGSASDIGENEitPYLV---SRFYRAPEIILGL-PYD 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 211 YSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLG-----------------TEDL---YDYIDKYN-------I 263
Cdd:cd14135  183 YPIDMWSVGCTLYEL-YTGKILFPGKTNNHMLKLMMDLKGkfpkkmlrkgqfkdqhfDENLnfiYREVDKVTkkevrrvM 261
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528504250 264 ELDPRFNDILGR-HSRKRWERFVHSENQHLVstealDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14135  262 SDIKPTKDLKTLlIGKQRLPDEDRKKLLQLK-----DLLDKCLMLDPEKRITPNEALQHPFI 318
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
85-244 4.36e-16

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: 77.58  E-value: 4.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  85 LENLRGgPNIITLLDIIKDPVSRTPALVFEHVNNTDFKQL---YQTLSDY----DIRFYMYEILKALDYCH-----SMGI 152
Cdd:cd08217   53 LRELKH-PNIVRYYDRIVDRANTTLYIVMEYCEGGDLAQLikkCKKENQYipeeFIWKIFTQLLLALYECHnrsvgGGKI 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 153 MHRDVKPHNVMIDHEHrKLRLIDWGLA-EFYHPNQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEP 231
Cdd:cd08217  132 LHRDLKPANIFLDSDN-NVKLGDFGLArVLSHDSSFAKTYVGTPYYMSPELLNE-QSYDEKSDIWSLGCLIYELCALHPP 209
                        170
                 ....*....|...
gi 528504250 232 fFHGHdNYDQLVR 244
Cdd:cd08217  210 -FQAA-NQLELAK 220
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
93-232 5.00e-16

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: 77.36  E-value: 5.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIikDPVSRTPALVFEHVNN---TDFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEH- 168
Cdd:cd14202   62 NIVALYDF--QEIANSVYLVMEYCNGgdlADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGg 139
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504250 169 RK-------LRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14202  140 RKsnpnnirIKIADFGFARYLQNNMMAATLCGSPMYMAPEVIMS-QHYDAKADLWSIGTIIYQCLTGKAPF 209
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
111-327 5.04e-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: 78.92  E-value: 5.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFKQLYQ---TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE-HRKlrLIDWGLA------- 179
Cdd:cd05600   88 LAMEYVPGGDFRTLLNnsgILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSgHIK--LTDFGLAsgtlspk 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 180 --------------------------EFYH------PNQEYNVrVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIF 227
Cdd:cd05600  166 kiesmkirleevkntafleltakerrNIYRamrkedQNYANSV-VGSPDYMAPEVLRG-EGYDLTVDYWSLGCILFECLV 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 228 RKEPFfhghdnydqlvriakvlgtedlydyidkYNIELDPRFNDIlgRHSRK--RWERFVHSENQHLVSTEALDFLDKLL 305
Cdd:cd05600  244 GFPPF----------------------------SGSTPNETWANL--YHWKKtlQRPVYTDPDLEFNLSDEAWDLITKLI 293
                        250       260
                 ....*....|....*....|...
gi 528504250 306 RyDHQARLTA-REAMDHSYFYPI 327
Cdd:cd05600  294 T-DPQDRLQSpEQIKNHPFFKNI 315
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
123-321 5.13e-16

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: 77.06  E-value: 5.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 123 QLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHPNQEYNVRVASRYFKGPEL 202
Cdd:cd06632   94 QRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGV-VKLADFGMAKHVEAFSFAKSFKGSPYWMAPEV 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 203 LVDYQ-MYDYSLDMWSLGCMLASMIFRKEPFfhghDNYDQLVRIAKVLGTEDLydyidkynieldPRFNDilgrhsrkrw 281
Cdd:cd06632  173 IMQKNsGYGLAVDIWSLGCTVLEMATGKPPW----SQYEGVAAIFKIGNSGEL------------PPIPD---------- 226
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 528504250 282 erfvhsenqHLvSTEALDFLDKLLRYDHQARLTAREAMDH 321
Cdd:cd06632  227 ---------HL-SPDAKDFIRLCLQRDPEDRPTASQLLEH 256
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
134-327 6.70e-16

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: 77.40  E-value: 6.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSL 213
Cdd:cd05605  105 VFYAAEITCGLEHLHSERIVYRDLKPENILLD-DHGHVRISDLGLAVEIPEGETIRGRVGTVGYMAPE-VVKNERYTFSP 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 214 DMWSLGCMLASMIFRKEPFfhghdnydqLVRIAKVLGTEdlydyIDKynieldprfndilgrhsRKRWERFVHSENqhlV 293
Cdd:cd05605  183 DWWGLGCLIYEMIEGQAPF---------RARKEKVKREE-----VDR-----------------RVKEDQEEYSEK---F 228
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528504250 294 STEALDFLDKLLRYDHQARL-----TAREAMDHSYFYPI 327
Cdd:cd05605  229 SEEAKSICSQLLQKDPKTRLgcrgeGAEDVKSHPFFKSI 267
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
92-323 6.82e-16

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: 76.97  E-value: 6.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTpaLVFEHVNNT---DFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMI---D 165
Cdd:cd14195   68 PNIITLHDIFENKTDVV--LILELVSGGelfDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLldkN 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 166 HEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFhGHDNYDQLVRI 245
Cdd:cd14195  146 VPNPRIKLIDFGIAHKIEAGNEFKNIFGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFL-GETKQETLTNI 223
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 246 AKVlgtedLYDYIDKYnieldprFNDilgrhsrkrwerfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14195  224 SAV-----NYDFDEEY-------FSN---------------------TSELAKDFIRRLLVKDPKKRMTIAQSLEHSW 268
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
88-331 7.01e-16

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: 78.14  E-value: 7.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  88 LRGG--PNIITLLDIIKDpvSRTPALVFEHVNNTDF--KQLYQTL-SDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:cd14176   67 LRYGqhPNIITLKDVYDD--GKYVYVVTELMKGGELldKILRQKFfSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNI 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 163 MIDHEH---RKLRLIDWGLA-EFYHPNQEYNVRVASRYFKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDN 238
Cdd:cd14176  145 LYVDESgnpESIRICDFGFAkQLRAENGLLMTPCYTANFVAPEVL-ERQGYDAACDIWSLGVLLYTMLTGYTPFANGPDD 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 239 YDQ--LVRIAKvlgtedlydyiDKYNIeldprfndilgrhSRKRWERfvhsenqhlVSTEALDFLDKLLRYDHQARLTAR 316
Cdd:cd14176  224 TPEeiLARIGS-----------GKFSL-------------SGGYWNS---------VSDTAKDLVSKMLHVDPHQRLTAA 270
                        250
                 ....*....|....*
gi 528504250 317 EAMDHSYFypIVKDQ 331
Cdd:cd14176  271 LVLRHPWI--VHWDQ 283
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
39-321 7.03e-16

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: 77.48  E-value: 7.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNN----------EKVVVKILKPVKKKKIKREIKILENLRGGPNIITLLDIIKDPVSRT 108
Cdd:cd14096    3 YRLINKIGEGAFSNVYKAVPLRNTgkpvaikvvrKADLSSDNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 109 paLVFEHVNNTD-FKQL--YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMID--------HEHRKL------ 171
Cdd:cd14096   83 --IVLELADGGEiFHQIvrLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEpipfipsiVKLRKAdddetk 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 172 ------------------RLIDWGLAEFYHPNQEyNVRVASRYFKGPELLVDYQmYDYSLDMWSLGCMLASMIFRKEPFF 233
Cdd:cd14096  161 vdegefipgvggggigivKLADFGLSKQVWDSNT-KTPCGTVGYTAPEVVKDER-YSKKVDMWALGCVLYTLLCGFPPFY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 234 hgHDNYDQLVRiaKVLGTEdlYDYidkynieLDPRFNDIlgrhsrkrwerfvhsenqhlvSTEALDFLDKLLRYDHQARL 313
Cdd:cd14096  239 --DESIETLTE--KISRGD--YTF-------LSPWWDEI---------------------SKSAKDLISHLLTVDPAKRY 284

                 ....*...
gi 528504250 314 TAREAMDH 321
Cdd:cd14096  285 DIDEFLAH 292
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
92-244 7.32e-16

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: 76.92  E-value: 7.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDpvSRTPALVFEHVNNTDfkqLY------QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMID 165
Cdd:cd14161   62 PHIISVYEVFEN--SSKIVIVMEYASRGD---LYdyiserQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLD 136
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504250 166 hEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPfFHGHDnYDQLVR 244
Cdd:cd14161  137 -ANGNIKIADFGLSNLYNQDKFLQTYCGSPLYASPEIVNGRPYIGPEVDSWSLGVLLYILVHGTMP-FDGHD-YKILVK 212
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
92-232 9.99e-16

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: 76.63  E-value: 9.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTPALVFEHVNNTDFKQL--YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHR 169
Cdd:cd14118   74 PNVVKLVEVLDDPNEDNLYMVFELVDKGAVMEVptDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGH 153
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 170 kLRLIDWGLAEFYHPNQEYNVRVA-SRYFKGPELLVDYQmYDYS---LDMWSLGCMLASMIFRKEPF 232
Cdd:cd14118  154 -VKIADFGVSNEFEGDDALLSSTAgTPAFMAPEALSESR-KKFSgkaLDIWAMGVTLYCFVFGRCPF 218
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
112-324 1.01e-15

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: 76.47  E-value: 1.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 VFEHVNNTDFKqlyqtLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMID-HEHRKLRLIDWGLAEFYHPNQEYNV 190
Cdd:cd14114   86 LFERIAAEHYK-----MSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtKRSNEVKLIDFGLATHLDPKESVKV 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 191 RVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFfhGHDNYDQLVRIAKvlgtedlydyidkyniELDPRFN 270
Cdd:cd14114  161 TTGTAEFAAPE-IVEREPVGFYTDMWAVGVLSYVLLSGLSPF--AGENDDETLRNVK----------------SCDWNFD 221
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528504250 271 DilgrhsrkrwERFVHsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14114  222 D----------SAFSG------ISEEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
126-324 1.49e-15

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: 75.85  E-value: 1.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 126 QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE--HRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELL 203
Cdd:cd14106  103 ECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEfpLGDIKLCDFGISRVIGEGEEIREILGTPDYVAPEIL 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 204 vDYQMYDYSLDMWSLGCMLASMIFRKEPFFhGHDNYDQLVRIAKVLGT--EDLYdyidkynieldprfndilgrhsrkrw 281
Cdd:cd14106  183 -SYEPISLATDMWSIGVLTYVLLTGHSPFG-GDDKQETFLNISQCNLDfpEELF-------------------------- 234
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 528504250 282 erfvhsenqHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14106  235 ---------KDVSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
38-324 1.89e-15

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: 75.44  E-value: 1.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  38 DYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKreikiLENLR---------GGPNIITLLDIIKDPvsRT 108
Cdd:cd14069    2 DWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDC-----PENIKkevciqkmlSHKNVVRFYGHRREG--EF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 109 PALVFEHVNNTDfkqLYQTLS-DY-----DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAE-F 181
Cdd:cd14069   75 QYLFLEYASGGE---LFDKIEpDVgmpedVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLD-ENDNLKISDFGLATvF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 182 YHPNQE--YNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNydqlvriakvlgTEDLYDYID 259
Cdd:cd14069  151 RYKGKErlLNKMCGTLPYVAPELLAKKKYRAEPVDVWSCGIVLFAMLAGELPWDQPSDS------------CQEYSDWKE 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 260 KYNIELDPrfndilgrhsrkrWERfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14069  219 NKKTYLTP-------------WKK---------IDTAALSLLRKILTENPNKRITIEDIKKHPWY 261
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
113-250 2.36e-15

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: 76.22  E-value: 2.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 113 FEHVNNT--DFKQLYQTLSDY------------DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHR---KLRLID 175
Cdd:cd14229   70 FQHRNHTclVFEMLEQNLYDFlkqnkfsplplkVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDPVRqpyRVKVID 149
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 176 WGLAEfYHPNQEYNVRVASRYFKGPELLVDYQMYDySLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLG 250
Cdd:cd14229  150 FGSAS-HVSKTVCSTYLQSRYYRAPEIILGLPFCE-AIDMWSLGCVIAEL-FLGWPLYPGALEYDQIRYISQTQG 221
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
92-234 3.05e-15

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: 74.50  E-value: 3.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPvsRTPALVFEHVNNTDfkqLYQTLSDYDIRF-------YMYEILKALDYCHSMGIMHRDVKPHNVMI 164
Cdd:cd13999   50 PNIVQFIGACLSP--PPLCIVTEYMPGGS---LYDLLHKKKIPLswslrlkIALDIARGMNYLHSPPIIHRDLKSLNILL 124
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504250 165 DhEHRKLRLIDWGLAEFYHPNQEYNVRVASRY-FKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPFFH 234
Cdd:cd13999  125 D-ENFTVKIADFGLSRIKNSTTEKMTGVVGTPrWMAPEVL-RGEPYTEKADVYSFGIVLWELLTGEVPFKE 193
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
93-232 3.13e-15

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: 74.71  E-value: 3.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDiikdpVSRTPA---LVFEHVNNTDFKQLYQ---TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDH 166
Cdd:cd14120   53 NVVALLD-----CQETSSsvyLVMEYCNGGDLADYLQakgTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSH 127
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504250 167 EHR--------KLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDYQmYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14120  128 NSGrkpspndiRLKIADFGFARFLQDGMMAATLCGSPMYMAPEVIMSLQ-YDAKADLWSIGTIVYQCLTGKAPF 200
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
134-327 3.19e-15

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: 76.21  E-value: 3.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLA-EFYHPNQEYNVRVASRYFKGPELLvDYQMYDYS 212
Cdd:cd05602  111 RFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGH-IVLTDFGLCkENIEPNGTTSTFCGTPEYLAPEVL-HKQPYDRT 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 213 LDMWSLGCMLASMIFRKEPFFHGHdnydqlvriakvlgTEDLYDYIDKYNIELDPRfndilgrhsrkrwerfvhsenqhl 292
Cdd:cd05602  189 VDWWCLGAVLYEMLYGLPPFYSRN--------------TAEMYDNILNKPLQLKPN------------------------ 230
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528504250 293 VSTEALDFLDKLLRYDHQARLTAR----EAMDHSYFYPI 327
Cdd:cd05602  231 ITNSARHLLEGLLQKDRTKRLGAKddftEIKNHIFFSPI 269
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
37-323 4.17e-15

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: 75.15  E-value: 4.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILE----NLRGGPNIITLLDIIKDPVSRTpaLV 112
Cdd:cd14086    1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREaricRLLKHPNIVRLHDSISEEGFHY--LV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 113 FEHVNNTDF------KQLYqtlSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHR--KLRLIDWGLAEFYHP 184
Cdd:cd14086   79 FDLVTGGELfedivaREFY---SEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKgaAVKLADFGLAIEVQG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 185 NQEYNVRVASRY-FKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPFFhghdNYDQLVRIAKVLGTEdlYDYidkyni 263
Cdd:cd14086  156 DQQAWFGFAGTPgYLSPEVL-RKDPYGKPVDIWACGVILYILLVGYPPFW----DEDQHRLYAQIKAGA--YDY------ 222
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 264 eldprfndilgrhSRKRWErfvhsenqhLVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14086  223 -------------PSPEWD---------TVTPEAKDLINQMLTVNPAKRITAAEALKHPW 260
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
92-323 4.53e-15

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: 75.05  E-value: 4.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDpvSRTPALVFEHVNNTDF--KQLYQT-LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEH 168
Cdd:cd14177   58 PNIITLKDVYDD--GRYVYLVTELMKGGELldRILRQKfFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDS 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 R---KLRLIDWGLA-EFYHPNQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQ--L 242
Cdd:cd14177  136 AnadSIRICDFGFAkQLRGENGLLLTPCYTANFVAPEVLMR-QGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEeiL 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 243 VRIAKvlgtedlydyiDKYNIeldprfndilgrhSRKRWERfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHS 322
Cdd:cd14177  215 LRIGS-----------GKFSL-------------SGGNWDT---------VSDAAKDLLSHMLHVDPHQRYTAEQVLKHS 261

                 .
gi 528504250 323 Y 323
Cdd:cd14177  262 W 262
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
92-321 4.63e-15

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: 74.28  E-value: 4.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTpaLVFEHVNNTD-FKQLYQT--LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIdHEH 168
Cdd:cd14095   58 PNIVQLIEEYDTDTELY--LVMELVKGGDlFDAITSStkFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLV-VEH 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 ----RKLRLIDWGLAEfYHPNQEYNVRVASRYFkGPELLVDyQMYDYSLDMWSLGCMLASMI--FrkePFFHGHDNyDQl 242
Cdd:cd14095  135 edgsKSLKLADFGLAT-EVKEPLFTVCGTPTYV-APEILAE-TGYGLKVDIWAAGVITYILLcgF---PPFRSPDR-DQ- 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 243 vriakvlgtEDLYDYIDKYNIE-LDPRFNDIlgrhsrkrwerfvhsenqhlvSTEALDFLDKLLRYDHQARLTAREAMDH 321
Cdd:cd14095  207 ---------EELFDLILAGEFEfLSPYWDNI---------------------SDSAKDLISRMLVVDPEKRYSAGQVLDH 256
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
92-323 4.64e-15

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: 74.60  E-value: 4.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKdpVSRTPALVFEHVNNTD-FKQLYQTL--SDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEH 168
Cdd:cd14185   58 PNIVKLFEVYE--TEKEIYLILEYVRGGDlFDAIIESVkfTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNP 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 RK---LRLIDWGLAEfyHPNQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRI 245
Cdd:cd14185  136 DKsttLKLADFGLAK--YVTGPIFTVCGTPTYVAPEILSE-KGYGLEVDMWAAGVILYILLCGFPPFRSPERDQEELFQI 212
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 246 AKvLGTedlYDYIDKYnieldprfndilgrhsrkrWERfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14185  213 IQ-LGH---YEFLPPY-------------------WDN---------ISEAAKDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
137-321 4.96e-15

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: 74.25  E-value: 4.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 137 MYEILKALDYCHSMGIMHRDVKPHNVMI--DHEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLvDYQMYDYSLD 214
Cdd:cd14089  106 MRQIGSAVAHLHSMNIAHRDLKPENLLYssKGPNAILKLTDFGFAKETTTKKSLQTPCYTPYYVAPEVL-GPEKYDKSCD 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 215 MWSLGCMLASMIFRKEPFFHGHDnydqlVRIAKvlgtedlydyidkynieldprfndilGRHSRKR--WERFVHSENQHl 292
Cdd:cd14089  185 MWSLGVIMYILLCGYPPFYSNHG-----LAISP--------------------------GMKKRIRngQYEFPNPEWSN- 232
                        170       180
                 ....*....|....*....|....*....
gi 528504250 293 VSTEALDFLDKLLRYDHQARLTAREAMDH 321
Cdd:cd14089  233 VSEEAKDLIRGLLKTDPSERLTIEEVMNH 261
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
39-244 5.32e-15

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: 74.35  E-value: 5.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLR-----GGPNIITLLDII--KDPVsrtpAL 111
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIEimsslNHPHIIRIYEVFenKDKI----VI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 VFEHVNNT---DFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHPNQEY 188
Cdd:cd14073   79 VMEYASGGelyDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGN-AKIADFGLSNLYSKDKLL 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 189 NVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFfhGHDNYDQLVR 244
Cdd:cd14073  158 QTFCGSPLYASPEIVNGTPYQGPEVDCWSLGVLLYTLVYGTMPF--DGSDFKRLVK 211
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
122-243 7.83e-15

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: 73.65  E-value: 7.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 122 KQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHPNQEY-NVRVASRYFKGP 200
Cdd:cd08215   94 KKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGV-VKLGDFGISKVLESTTDLaKTVVGTPYYLSP 172
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 528504250 201 ELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFfhGHDNYDQLV 243
Cdd:cd08215  173 ELCEN-KPYNYKSDIWALGCVLYELCTLKHPF--EANNLPALV 212
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
38-324 7.86e-15

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: 74.96  E-value: 7.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  38 DYQLVRKLGRGKYSEVFEAINITNNEKVVVKI----------LKPVKKKKIKREIKILENLRGGPNIITL---------L 98
Cdd:cd05614    1 NFELLKVLGTGAYGKVFLVRKVSGHDANKLYAmkvlrkaalvQKAKTVEHTRTERNVLEHVRQSPFLVTLhyafqtdakL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  99 DIIKDPVSrtpalvfehvNNTDFKQLYQT--LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDW 176
Cdd:cd05614   81 HLILDYVS----------GGELFTHLYQRdhFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGH-VVLTDF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 177 GLA-EFYHPNQEYNVR-VASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPF-FHGHDNYDQLV--RIAKvlgt 251
Cdd:cd05614  150 GLSkEFLTEEKERTYSfCGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFtLEGEKNTQSEVsrRILK---- 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 252 edlydyidkynieLDPRFNDILGrhsrkrwerfvhsenqhlvsTEALDFLDKLLRYDHQARL-----TAREAMDHSYF 324
Cdd:cd05614  226 -------------CDPPFPSFIG--------------------PVARDLLQKLLCKDPKKRLgagpqGAQEIKEHPFF 270
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
92-323 8.09e-15

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: 73.91  E-value: 8.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKdpvSRTPA-LVFEHVNNTD-FKQLYQT--LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVM---I 164
Cdd:cd14167   61 PNIVALDDIYE---SGGHLyLIMQLVSGGElFDRIVEKgfYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysL 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 165 DhEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDnydqlvr 244
Cdd:cd14167  138 D-EDSKIMISDFGLSKIEGSGSVMSTACGTPGYVAPEVLAQ-KPYSKAVDCWSIGVIAYILLCGYPPFYDEND------- 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 245 iAKvlgtedLYDYIDKYNIELD-PRFNDIlgrhsrkrwerfvhsenqhlvSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14167  209 -AK------LFEQILKAEYEFDsPYWDDI---------------------SDSAKDFIQHLMEKDPEKRFTCEQALQHPW 260
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
92-232 8.99e-15

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: 74.23  E-value: 8.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTPALVFEHVNNTDFKQL--YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHR 169
Cdd:cd14199   85 PNVVKLVEVLDDPSEDHLYMVFELVKQGPVMEVptLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVG-EDG 163
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 170 KLRLIDWGLA-EFYHPNQEYNVRVASRYFKGPELLVDYQ--MYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14199  164 HIKIADFGVSnEFEGSDALLTNTVGTPAFMAPETLSETRkiFSGKALDVWAMGVTLYCFVFGQCPF 229
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
92-232 9.35e-15

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: 73.58  E-value: 9.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKdpVSRTPALVFEHVNNT---DFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHeH 168
Cdd:cd14071   59 PHIIKLYQVME--TKDMLYLVTEYASNGeifDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDA-N 135
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504250 169 RKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14071  136 MNIKIADFGFSNFFKPGELLKTWCGSPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGALPF 199
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
87-258 1.08e-14

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: 73.19  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  87 NLRGGPNIITLLDIIKDPVSRTpaLVFE-HVNNTD---FKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:cd14004   63 NKRSHPNIVKLLDFFEDDEFYY--LVMEkHGSGMDlfdFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENV 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 163 MIDhEHRKLRLIDWGLAEFYHPNQeYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQL 242
Cdd:cd14004  141 ILD-GNGTIKLIDFGSAAYIKSGP-FDTFVGTIDYAAPEVLRGNPYGGKEQDIWALGVLLYTLVFKENPFYNIEEILEAD 218
                        170
                 ....*....|....*.
gi 528504250 243 VRIAKVLgTEDLYDYI 258
Cdd:cd14004  219 LRIPYAV-SEDLIDLI 233
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
134-327 1.21e-14

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: 74.24  E-value: 1.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLrLIDWGLA-EFYHPNQEYNVRVASRYFKGPELLVDyQMYDYS 212
Cdd:cd05603   99 RFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVV-LTDFGLCkEGMEPEETTSTFCGTPEYLAPEVLRK-EPYDRT 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 213 LDMWSLGCMLASMIFRKEPFfhghdnYDQLVriakvlgtEDLYDYIDKYNIELDPrfndilGRhsrkrwerfvhsenqhl 292
Cdd:cd05603  177 VDWWCLGAVLYEMLYGLPPF------YSRDV--------SQMYDNILHKPLHLPG------GK----------------- 219
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528504250 293 vSTEALDFLDKLLRYDHQARLTAR----EAMDHSYFYPI 327
Cdd:cd05603  220 -TVAACDLLQGLLHKDQRRRLGAKadflEIKNHVFFSPI 257
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
39-324 1.36e-14

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: 74.35  E-value: 1.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVK--ILKPVKKKKIKREIKILENLR-----GGPNIITLLD--IIKDPVSRTP 109
Cdd:cd14225   45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKiiRNKKRFHHQALVEVKILDALRrkdrdNSHNVIHMKEyfYFRNHLCITF 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 110 AL----VFEHVNNTDFkqlyQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHR-KLRLIDWGLAEFYHp 184
Cdd:cd14225  125 ELlgmnLYELIKKNNF----QGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQsSIKVIDFGSSCYEH- 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 185 nQEYNVRVASRYFKGPELLVDYQmYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLGT--EDLYDYIDKYN 262
Cdd:cd14225  200 -QRVYTYIQSRFYRSPEVILGLP-YSMAIDMWSLGCILAEL-YTGYPLFPGENEVEQLACIMEVLGLppPELIENAQRRR 276
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 263 IELDPRFN--DILGRHSRKRWerfVHSEN-QHLVSTEA---LDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14225  277 LFFDSKGNprCITNSKGKKRR---PNSKDlASALKTSDplfLDFIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
85-324 1.62e-14

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: 73.49  E-value: 1.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  85 LENLRGGPNIITLLDIIKDPVSRTpaLVFEHVNNTD-FKQLYQ--TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHN 161
Cdd:cd14092   52 LRLCQGHPNIVKLHEVFQDELHTY--LVMELLRGGElLERIRKkkRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPEN 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 162 VMIDHEHRK--LRLIDWGLAEFYHPNQEYNVRVASRYFKGPELL---VDYQMYDYSLDMWSLGCMLASMIFRKEPfFHGH 236
Cdd:cd14092  130 LLFTDEDDDaeIKIVDFGFARLKPENQPLKTPCFTLPYAAPEVLkqaLSTQGYDESCDLWSLGVILYTMLSGQVP-FQSP 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 237 DNYDQlvriakvlgTEDLYDYIDKYNIELDprfndilgrhsrkrwerfvhSENQHLVSTEALDFLDKLLRYDHQARLTAR 316
Cdd:cd14092  209 SRNES---------AAEIMKRIKSGDFSFD--------------------GEEWKNVSSEAKSLIQGLLTVDPSKRLTMS 259

                 ....*...
gi 528504250 317 EAMDHSYF 324
Cdd:cd14092  260 ELRNHPWL 267
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
112-327 1.78e-14

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: 73.57  E-value: 1.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 VFEHVNNTDFKQLYQTLSDYDI---RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEfyhpNQEY 188
Cdd:cd05592   74 VMEYLNGGDLMFHIQQSGRFDEdraRFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGH-IKIADFGMCK----ENIY 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 189 NVRVASRY-----FKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPfFHGHDNydqlvriakvlgtEDLYDYIdkyni 263
Cdd:cd05592  149 GENKASTFcgtpdYIAPEILKG-QKYNQSVDWWSFGVLLYEMLIGQSP-FHGEDE-------------DELFWSI----- 208
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504250 264 eldprFNDILgrhSRKRWerfvhsenqhlVSTEALDFLDKLLRYDHQARL-----TAREAMDHSYFYPI 327
Cdd:cd05592  209 -----CNDTP---HYPRW-----------LTKEAASCLSLLLERNPEKRLgvpecPAGDIRDHPFFKTI 258
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
37-323 1.82e-14

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: 73.14  E-value: 1.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRKL-GRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENL---RGGPNIITLLDIIKDPVSRTpaLV 112
Cdd:cd14174    1 DLYRLTDELlGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSRVFREVETLyqcQGNKNILELIEFFEDDTRFY--LV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 113 FEHVNNTDFKQLYQTLSDYDIR---FYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHR--KLRLIDWGLAEFYHPNQ- 186
Cdd:cd14174   79 FEKLRGGSILAHIQKRKHFNEReasRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKvsPVKICDFDLGSGVKLNSa 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 187 -------EYNVRVASRYFKGPELLVDY----QMYDYSLDMWSLGCMLASMIFRKEPFFhGHDNYD------QLVRIAKvl 249
Cdd:cd14174  159 ctpittpELTTPCGSAEYMAPEVVEVFtdeaTFYDKRCDLWSLGVILYIMLSGYPPFV-GHCGTDcgwdrgEVCRVCQ-- 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504250 250 gtEDLYDYIDKYNIEldprFNDilgrhsrKRWERfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14174  236 --NKLFESIQEGKYE----FPD-------KDWSH---------ISSEAKDLISKLLVRDAKERLSAAQVLQHPW 287
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
92-324 2.03e-14

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: 72.54  E-value: 2.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDpvSRTPALVFEHVNNT--DFKQLYQTLSDY----DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMID 165
Cdd:cd14109   56 PNIVQMHDAYDD--EKLAVTVIDNLASTieLVRDNLLPGKDYyterQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQ 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 166 HEHrkLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDYQMyDYSLDMWSLGCMLASMIFRKEPfFHGHDNYDQLVRI 245
Cdd:cd14109  134 DDK--LKLADFGQSRRLLRGKLTTLIYGSPEFVSPEIVNSYPV-TLATDMWSVGVLTYVLLGGISP-FLGDNDRETLTNV 209
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504250 246 akvlgtedlydyidkynieldprfndilgRHSrkRWErFVHSENQHlVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14109  210 -----------------------------RSG--KWS-FDSSPLGN-ISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
129-324 2.19e-14

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: 72.86  E-value: 2.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 129 SDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYnVRVASRYFKGPELLVDYQM 208
Cdd:cd05606   96 SEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLD-EHGHVRISDLGLACDFSKKKPH-ASVGTHGYMAPEVLQKGVA 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 209 YDYSLDMWSLGCMLASMIFRKEPFFHgHDNYDQlvriakvlgtedlyDYIDKYNIELDPRFNDILgrhsrkrwerfvhse 288
Cdd:cd05606  174 YDSSADWFSLGCMLYKLLKGHSPFRQ-HKTKDK--------------HEIDRMTLTMNVELPDSF--------------- 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 528504250 289 nqhlvSTEALDFLDKLLRYDHQARL-----TAREAMDHSYF 324
Cdd:cd05606  224 -----SPELKSLLEGLLQRDVSKRLgclgrGATEVKEHPFF 259
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
135-232 2.48e-14

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: 72.75  E-value: 2.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 135 FYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSLD 214
Cdd:cd05630  106 FYAAEICCGLEDLHRERIVYRDLKPENILLD-DHGHIRISDLGLAVHVPEGQTIKGRVGTVGYMAPE-VVKNERYTFSPD 183
                         90
                 ....*....|....*...
gi 528504250 215 MWSLGCMLASMIFRKEPF 232
Cdd:cd05630  184 WWALGCLLYEMIAGQSPF 201
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
132-324 2.76e-14

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: 73.35  E-value: 2.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 132 DIRFYMYEILKALDYCHSMGIMHRDVKPHNVM-------------IDHEHRKL-----RLIDWGLAEFYHpnQEYNVRVA 193
Cdd:cd14213  117 HIRNMAYQICKSVNFLHHNKLTHTDLKPENILfvqsdyvvkynpkMKRDERTLknpdiKVVDFGSATYDD--EHHSTLVS 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 194 SRYFKGPELLVDYQmYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLGTEDLY--------DYIDKYNIEL 265
Cdd:cd14213  195 TRHYRAPEVILALG-WSQPCDVWSIGCILIEY-YLGFTVFQTHDSKEHLAMMERILGPLPKHmiqktrkrKYFHHDQLDW 272
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528504250 266 DPRFNDilGRHSRKR---WERFVHSENQHlvSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14213  273 DEHSSA--GRYVRRRckpLKEFMLSQDVD--HEQLFDLIQKMLEYDPAKRITLDEALKHPFF 330
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
37-236 3.64e-14

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: 71.95  E-value: 3.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRKLGRGKYSEVFEAINITNNEKVVV--KILKPVKKKKIKREIKILENLRGGPNIITLLDIIKDPVSRTPA---- 110
Cdd:cd06608    6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIkiMDIIEDEEEEIKLEINILRKFSNHPNIATFYGAFIKKDPPGGDdqlw 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNN---TD----FKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGL-AEFY 182
Cdd:cd06608   86 LVMEYCGGgsvTDlvkgLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAE-VKLVDFGVsAQLD 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 183 HPNQEYNVRVASRYFKGPELLV-DYQM---YDYSLDMWSLGCMLASMIFRKEPFFHGH 236
Cdd:cd06608  165 STLGRRNTFIGTPYWMAPEVIAcDQQPdasYDARCDVWSLGITAIELADGKPPLCDMH 222
PTZ00284 PTZ00284
protein kinase; Provisional
143-336 3.65e-14

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 73.85  E-value: 3.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 143 ALDYCHS-MGIMHRDVKPHNVMIDHE--------HRKL-------RLIDWGLAefyhpNQEYNVR---VASRYFKGPELL 203
Cdd:PTZ00284 243 ALDYFHTeLHLMHTDLKPENILMETSdtvvdpvtNRALppdpcrvRICDLGGC-----CDERHSRtaiVSTRHYRSPEVV 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 204 VDYQmYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVL-----------GTE---DLYDYIDKYNIELDPRF 269
Cdd:PTZ00284 318 LGLG-WMYSTDMWSMGCIIYEL-YTGKLLYDTHDNLEHLHLMEKTLgrlpsewagrcGTEearLLYNSAGQLRPCTDPKH 395
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 270 ndiLGRHSRKRWERFVHSENQhlvsteALDFLDKLLRYDHQARLTAREAMDHSY---FYPivkdQGRGAP 336
Cdd:PTZ00284 396 ---LARIARARPVREVIRDDL------LCDLIYGLLHYDRQKRLNARQMTTHPYvlkYYP----ECRQHP 452
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
134-327 3.88e-14

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: 72.63  E-value: 3.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE-HRKlrLIDWGLAEfyhPNQEYNVRvaSRYFKG------PELLVdY 206
Cdd:cd05570   99 RFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEgHIK--IADFGMCK---EGIWGGNT--TSTFCGtpdyiaPEILR-E 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 207 QMYDYSLDMWSLGCMLASMIFRKEPfFHGHDNydqlvriakvlgtEDLYDYIdkynieldpRFNDILgrhsRKRWerfvh 286
Cdd:cd05570  171 QDYGFSVDWWALGVLLYEMLAGQSP-FEGDDE-------------DELFEAI---------LNDEVL----YPRW----- 218
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 528504250 287 senqhlVSTEALDFLDKLLRYDHQARL-----TAREAMDHSYFYPI 327
Cdd:cd05570  219 ------LSREAVSILKGLLTKDPARRLgcgpkGEADIKAHPFFRNI 258
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
92-244 4.00e-14

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: 71.56  E-value: 4.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIkDPVSRTpALVFEHVNNTDFKQLYQT---LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEH 168
Cdd:cd14162   60 PNLICFYEAI-ETTSRV-YIIMELAENGDLLDYIRKngaLPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLD-KN 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 RKLRLIDWGLAEFYHPNQEyNVRVASRYFKG------PELLvDYQMYDYSL-DMWSLGCMLASMIFRKEPFfhGHDNYDQ 241
Cdd:cd14162  137 NNLKITDFGFARGVMKTKD-GKPKLSETYCGsyayasPEIL-RGIPYDPFLsDIWSMGVVLYTMVYGRLPF--DDSNLKV 212

                 ...
gi 528504250 242 LVR 244
Cdd:cd14162  213 LLK 215
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
132-247 5.14e-14

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: 72.05  E-value: 5.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 132 DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAE--FYHPNQEYNVRVASRYFkGPElLVDYQMY 209
Cdd:cd05582   98 DVKFYLAELALALDHLHSLGIIYRDLKPENILLD-EDGHIKLTDFGLSKesIDHEKKAYSFCGTVEYM-APE-VVNRRGH 174
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 528504250 210 DYSLDMWSLGCMLASMIFRKEPfFHGHDNYDQLVRIAK 247
Cdd:cd05582  175 TQSADWWSFGVLMFEMLTGSLP-FQGKDRKETMTMILK 211
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
39-232 5.61e-14

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: 71.60  E-value: 5.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILE---NLRGGPNIITLLD--IIKDPVSRTPALVF 113
Cdd:cd13985    2 YQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVAIKEIEimkRLCGHPNIVQYYDsaILSSEGRKEVLLLM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 114 EHVNNTDFKQLYQT----LSDYDIRFYMYEILKALDYCHSMG--IMHRDVKPHNVMIDHEhRKLRLIDWGLA--EFYHPN 185
Cdd:cd13985   82 EYCPGSLVDILEKSppspLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNT-GRFKLCDFGSAttEHYPLE 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 186 QEYNVRVA----SRY----FKGPEL--LVDYQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd13985  161 RAEEVNIIeeeiQKNttpmYRAPEMidLYSKKPIGEKADIWALGCLLYKLCFFKLPF 217
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
134-237 7.00e-14

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: 70.90  E-value: 7.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDyQMYDY-S 212
Cdd:cd14074  106 RKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGEKLETSCGSLAYSAPEILLG-DEYDApA 184
                         90       100
                 ....*....|....*....|....*
gi 528504250 213 LDMWSLGCMLASMIFRKEPFFHGHD 237
Cdd:cd14074  185 VDIWSLGVILYMLVCGQPPFQEAND 209
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
128-280 7.98e-14

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: 71.62  E-value: 7.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYnVRVASRYFKGPELLVDYQ 207
Cdd:cd14223  100 FSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLD-EFGHVRISDLGLACDFSKKKPH-ASVGTHGYMAPEVLQKGV 177
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504250 208 MYDYSLDMWSLGCMLASMIFRKEPFF-HGHDNYDQLVRIAKVLGTEdlydYIDKYNIELDPRFNDILGRHSRKR 280
Cdd:cd14223  178 AYDSSADWFSLGCMLFKLLRGHSPFRqHKTKDKHEIDRMTLTMAVE----LPDSFSPELRSLLEGLLQRDVNRR 247
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
36-236 8.29e-14

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: 70.76  E-value: 8.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  36 QDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKIlkpvkkkkikreikiLENLRGGPNIITLLDIIKDpvSRTPA----- 110
Cdd:cd06612    2 EEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKV---------------VPVEEDLQEIIKEISILKQ--CDSPYivkyy 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 ----------LVFEH-----VNntDFKQLYQ-TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEhRKLRLI 174
Cdd:cd06612   65 gsyfkntdlwIVMEYcgagsVS--DIMKITNkTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEE-GQAKLA 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528504250 175 DWGLA-EFYHPNQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFHGH 236
Cdd:cd06612  142 DFGVSgQLTDTMAKRNTVIGTPFWMAPEVIQE-IGYNNKADIWSLGITAIEMAEGKPPYSDIH 203
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
137-247 8.33e-14

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: 70.97  E-value: 8.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 137 MYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGL-AEFYHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDM 215
Cdd:cd06917  107 MREVLVALKFIHKDGIIHRDIKAANILVTNTGN-VKLCDFGVaASLNQNSSKRSTFVGTPYWMAPEVITEGKYYDTKADI 185
                         90       100       110
                 ....*....|....*....|....*....|..
gi 528504250 216 WSLGCMLASMIFrKEPFFHGHDNYDQLVRIAK 247
Cdd:cd06917  186 WSLGITTYEMAT-GNPPYSDVDALRAVMLIPK 216
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
38-279 8.48e-14

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: 71.98  E-value: 8.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  38 DYQLVRKLGRGKYSEVFeAINITNNEKVVVKILKPVKKKK-------IKREIKILENLRGGPNIITLLDIIKDPvSRTpA 110
Cdd:cd05617   16 DFDLIRVIGRGSYAKVL-LVRLKKNDQIYAMKVVKKELVHddedidwVQTEKHVFEQASSNPFLVGLHSCFQTT-SRL-F 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFK---QLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLA-EFYHPNQ 186
Cdd:cd05617   93 LVIEYVNGGDLMfhmQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGH-IKLTDYGMCkEGLGPGD 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 187 EYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDqlvriakvLGTED-LYDYIDKYNIEL 265
Cdd:cd05617  172 TTSTFCGTPNYIAPEILRG-EEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPD--------MNTEDyLFQVILEKPIRI 242
                        250
                 ....*....|....
gi 528504250 266 dPRFNDILGRHSRK 279
Cdd:cd05617  243 -PRFLSVKASHVLK 255
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
111-237 8.52e-14

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: 71.88  E-value: 8.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFKQLYQTLSDYDI---RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLA-EFYHPNQ 186
Cdd:cd05619   83 FVMEYLNGGDLMFHIQSCHKFDLpraTFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGH-IKIADFGMCkENMLGDA 161
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528504250 187 EYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPfFHGHD 237
Cdd:cd05619  162 KTSTFCGTPDYIAPEILLG-QKYNTSVDWWSFGVLLYEMLIGQSP-FHGQD 210
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
134-327 8.99e-14

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: 71.53  E-value: 8.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHPNQEYNVR-VASRYFKGPELLVDyQMYDYS 212
Cdd:cd05604  100 RFYAAEIASALGYLHSINIVYRDLKPENILLDSQGH-IVLTDFGLCKEGISNSDTTTTfCGTPEYLAPEVIRK-QPYDNT 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 213 LDMWSLGCMLASMIFRKEPFFhghdNYDqlvriakvlgTEDLYDYIDKYNIELDPRfndilgrhsrkrwerfvhsenqhl 292
Cdd:cd05604  178 VDWWCLGSVLYEMLYGLPPFY----CRD----------TAEMYENILHKPLVLRPG------------------------ 219
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528504250 293 VSTEALDFLDKLLRYDHQARLTAR----EAMDHSYFYPI 327
Cdd:cd05604  220 ISLTAWSILEELLEKDRQLRLGAKedflEIKNHPFFESI 258
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
125-324 1.01e-13

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: 71.59  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 125 YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMI---DHEHR---------------KLRLIDWGLAEFYHpnQ 186
Cdd:cd14215  110 YLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFvnsDYELTynlekkrdersvkstAIRVVDFGSATFDH--E 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 187 EYNVRVASRYFKGPELLVDYQmYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLG--TEDLYDYIDK---- 260
Cdd:cd14215  188 HHSTIVSTRHYRAPEVILELG-WSQPCDVWSIGCIIFEY-YVGFTLFQTHDNREHLAMMERILGpiPSRMIRKTRKqkyf 265
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 261 YNIELDPRFNDILGRHSR---KRWERFVHSENQHlvSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14215  266 YHGRLDWDENTSAGRYVRencKPLRRYLTSEAEE--HHQLFDLIESMLEYEPSKRLTLAAALKHPFF 330
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
113-323 1.07e-13

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 71.33  E-value: 1.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 113 FEHVNNT--DFKQLYQTLSDY------------DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHR---KLRLID 175
Cdd:cd14211   69 FQHKNHTclVFEMLEQNLYDFlkqnkfsplplkYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRqpyRVKVID 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 176 WGLAEfyHPNQEY-NVRVASRYFKGPELLVDYQmYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLG--TE 252
Cdd:cd14211  149 FGSAS--HVSKAVcSTYLQSRYYRAPEIILGLP-FCEAIDMWSLGCVIAEL-FLGWPLYPGSSEYDQIRYISQTQGlpAE 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 253 DLYDYIDK----YNIELDPRFNDI-----------LGRHSRKRWERFVHSENQ--------HLVSTEAL----------D 299
Cdd:cd14211  225 HLLNAATKtsrfFNRDPDSPYPLWrlktpeeheaeTGIKSKEARKYIFNCLDDmaqvngpsDLEGSELLaekadrrefiD 304
                        250       260
                 ....*....|....*....|....
gi 528504250 300 FLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14211  305 LLKRMLTIDQERRITPGEALNHPF 328
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
127-324 1.23e-13

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: 70.32  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 127 TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGL-AEFYHPNQEYNVRVASRYFKGPELLVD 205
Cdd:cd06614   93 RMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGS-VKLADFGFaAQLTKEKSKRNSVVGTPYWMAPEVIKR 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 206 yQMYDYSLDMWSLGCMLASMIFRKEPFFhghdNYDQLvRIAKVLGTEDLydyidkynieldPRFndilgrhsrkrwerfv 285
Cdd:cd06614  172 -KDYGPKVDIWSLGIMCIEMAEGEPPYL----EEPPL-RALFLITTKGI------------PPL---------------- 217
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528504250 286 hsENQHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd06614  218 --KNPEKWSPEFKDFLNKCLVKDPEKRPSAEELLQHPFL 254
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
136-226 1.42e-13

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: 70.40  E-value: 1.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 136 YMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYH---------------PNQEYNVRVASRYFKGP 200
Cdd:cd13996  112 LFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQVKIGDFGLATSIGnqkrelnnlnnnnngNTSNNSVGIGTPLYASP 191
                         90       100
                 ....*....|....*....|....*.
gi 528504250 201 ELLvDYQMYDYSLDMWSLGCMLASMI 226
Cdd:cd13996  192 EQL-DGENYNEKADIYSLGIILFEML 216
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
126-324 1.62e-13

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: 69.96  E-value: 1.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 126 QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHP-NQEYNVRVASRYFKGPELLV 204
Cdd:cd14189   96 HTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFIN-ENMELKVGDFGLAARLEPpEQRKKTICGTPNYLAPEVLL 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 205 DyQMYDYSLDMWSLGCMLASMIFRKEPFfhghdnydqlvriaKVLGTEDLYDYIDKYNIELdprfndilgrhsrkrwERF 284
Cdd:cd14189  175 R-QGHGPESDVWSLGCVMYTLLCGNPPF--------------ETLDLKETYRCIKQVKYTL----------------PAS 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 528504250 285 VHSENQHLVSTealdfldkLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14189  224 LSLPARHLLAG--------ILKRNPGDRLTLDQILEHEFF 255
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
128-321 1.62e-13

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: 69.72  E-value: 1.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHPNQEYNVRV--ASRYFKGPELLVD 205
Cdd:cd14078   98 LSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQN-LKLIDFGLCAKPKGGMDHHLETccGSPAYAAPELIQG 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 206 YQMYDYSLDMWSLGCMLASMIFRKEPFfhGHDNydqlvriakvlgTEDLYDYIDKynieldprfndilGRHSRKRWerfv 285
Cdd:cd14078  177 KPYIGSEADVWSMGVLLYALLCGFLPF--DDDN------------VMALYRKIQS-------------GKYEEPEW---- 225
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 528504250 286 hsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDH 321
Cdd:cd14078  226 -------LSPSSKLLLDQMLQVDPKKRITVKELLNH 254
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
128-280 1.82e-13

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: 70.86  E-value: 1.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYnVRVASRYFKGPELLVDYQ 207
Cdd:cd05633  105 FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLD-EHGHVRISDLGLACDFSKKKPH-ASVGTHGYMAPEVLQKGT 182
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504250 208 MYDYSLDMWSLGCMLASMIFRKEPFF-HGHDNYDQLVRIAKVLGTEdlydYIDKYNIELDPRFNDILGRHSRKR 280
Cdd:cd05633  183 AYDSSADWFSLGCMLFKLLRGHSPFRqHKTKDKHEIDRMTLTVNVE----LPDSFSPELKSLLEGLLQRDVSKR 252
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
92-323 1.85e-13

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: 69.92  E-value: 1.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTpaLVFEHVNNTD-FKQLYQ--TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMID--H 166
Cdd:cd14169   61 ENIVSLEDIYESPTHLY--LAMELVTGGElFDRIIErgSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpF 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 167 EHRKLRLIDWGLAEFYHPNQeYNVRVASRYFKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNydqlvria 246
Cdd:cd14169  139 EDSKIMISDFGLSKIEAQGM-LSTACGTPGYVAPELL-EQKPYGKAVDVWAIGVISYILLCGYPPFYDENDS-------- 208
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 247 kvlgteDLYDYIDKYNIELD-PRFNDIlgrhsrkrwerfvhsenqhlvSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14169  209 ------ELFNQILKAEYEFDsPYWDDI---------------------SESAKDFIRHLLERDPEKRFTCEQALQHPW 259
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
92-323 2.18e-13

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: 70.24  E-value: 2.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTpaLVFEHVNNTD-FKQLYQT--LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMI--DH 166
Cdd:cd14085   58 PNIIKLKEIFETPTEIS--LVLELVTGGElFDRIVEKgyYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYatPA 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 167 EHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFhgHDNYDQLVrIA 246
Cdd:cd14085  136 PDAPLKIADFGLSKIVDQQVTMKTVCGTPGYCAPEILRG-CAYGPEVDMWSVGVITYILLCGFEPFY--DERGDQYM-FK 211
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 247 KVLGTEdlYDYIdkynielDPRFNDilgrhsrkrwerfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14085  212 RILNCD--YDFV-------SPWWDD---------------------VSLNAKDLVKKLIVLDPKKRLTTQQALQHPW 258
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
128-232 2.50e-13

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: 70.42  E-value: 2.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYD-------IRFYMYEILKALDYCHSMGIMHRDVKPHNVMID---HehrkLRLIDWGLAEFYHPNQEYNVR--VASR 195
Cdd:cd05601   92 LSRYDdifeesmARFYLAELVLAIHSLHSMGYVHRDIKPENILIDrtgH----IKLADFGSAAKLSSDKTVTSKmpVGTP 167
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 528504250 196 YFKGPELL-----VDYQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd05601  168 DYIAPEVLtsmngGSKGTYGVECDWWSLGIVAYEMLYGKTPF 209
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
113-250 3.22e-13

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: 70.12  E-value: 3.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 113 FEHVNNT--DFKQLYQTLSDY------------DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHR---KLRLID 175
Cdd:cd14227   85 FQHKNHTclVFEMLEQNLYDFlkqnkfsplplkYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRqpyRVKVID 164
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 176 WGLAEfyHPNQEY-NVRVASRYFKGPELLVDYQMYDySLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLG 250
Cdd:cd14227  165 FGSAS--HVSKAVcSTYLQSRYYRAPEIILGLPFCE-AIDMWSLGCVIAEL-FLGWPLYPGASEYDQIRYISQTQG 236
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
85-233 3.29e-13

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: 69.23  E-value: 3.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  85 LENLRGgPNIITLLDIIKDPVSRtpALVFEHVNN---TDFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHN 161
Cdd:cd14113   57 LQSLQH-PQLVGLLDTFETPTSY--ILVLEMADQgrlLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPEN 133
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 162 VMIDHEHRK--LRLIDWGLAefYHPNQEYNVR--VASRYFKGPELLVDYQMyDYSLDMWSLGCMLASMIFRKEPFF 233
Cdd:cd14113  134 ILVDQSLSKptIKLADFGDA--VQLNTTYYIHqlLGSPEFAAPEIILGNPV-SLTSDLWSIGVLTYVLLSGVSPFL 206
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
140-324 3.35e-13

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: 69.01  E-value: 3.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 140 ILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEfyHPNQEYNVR---VASRYFKGPElLVDYQMYDYSLDMW 216
Cdd:cd06648  112 VLKALSFLHSQGVIHRDIKSDSILLTSDGR-VKLSDFGFCA--QVSKEVPRRkslVGTPYWMAPE-VISRLPYGTEVDIW 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 217 SLGCMLASMIFRKEPFFHghdnyDQLVRIAKvlgtedlydyidkynieldpRFNDILGRHSRkrwerfvhseNQHLVSTE 296
Cdd:cd06648  188 SLGIMVIEMVDGEPPYFN-----EPPLQAMK--------------------RIRDNEPPKLK----------NLHKVSPR 232
                        170       180
                 ....*....|....*....|....*...
gi 528504250 297 ALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd06648  233 LRSFLDRMLVRDPAQRATAAELLNHPFL 260
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
135-324 3.74e-13

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: 69.74  E-value: 3.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 135 FYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE-HRKlrLIDWGLA-EFYHPNQEYNVRVASRYFKGPELLVDyQMYDYS 212
Cdd:cd05584  104 FYLAEITLALGHLHSLGIIYRDLKPENILLDAQgHVK--LTDFGLCkESIHDGTVTHTFCGTIEYMAPEILTR-SGHGKA 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 213 LDMWSLGCMLASMIFRKEPFfhGHDNYDQlvRIAKVLgtedlydyidKYNIELDPrfndilgrhsrkrwerfvhsenqHL 292
Cdd:cd05584  181 VDWWSLGALMYDMLTGAPPF--TAENRKK--TIDKIL----------KGKLNLPP-----------------------YL 223
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 528504250 293 vSTEALDFLDKLLRYDHQARL-----TAREAMDHSYF 324
Cdd:cd05584  224 -TNEARDLLKKLLKRNVSSRLgsgpgDAEEIKAHPFF 259
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
38-232 3.90e-13

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: 68.59  E-value: 3.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  38 DYQLVRKLGRGKYSEVFEAINITNNEKVV------VKILKPVKKKKIKREIKILENLRGgPNIITLLDIIKdpvSRTPA- 110
Cdd:cd14663    1 RYELGRTLGEGTFAKVKFARNTKTGESVAikiidkEQVAREGMVEQIKREIAIMKLLRH-PNIVELHEVMA---TKTKIf 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTD-FKQLYQT--LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQE 187
Cdd:cd14663   77 FVMELVTGGElFSKIAKNgrLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLD-EDGNLKISDFGLSALSEQFRQ 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 528504250 188 YNV---RVASRYFKGPELLVDyQMYD-YSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14663  156 DGLlhtTCGTPNYVAPEVLAR-RGYDgAKADIWSCGVILFVLLAGYLPF 203
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
92-323 4.40e-13

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: 68.83  E-value: 4.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDpVSRTpALVFEHVNNTDFKQLYQTLSDYDIR---FYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEH 168
Cdd:cd14116   65 PNILRLYGYFHD-ATRV-YLILEYAPLGTVYRELQKLSKFDEQrtaTYITELANALSYCHSKRVIHRDIKPENLLLG-SA 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 RKLRLIDWGLAeFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFfhGHDNYDQLVR-IAK 247
Cdd:cd14116  142 GELKIADFGWS-VHAPSSRRTTLCGTLDYLPPE-MIEGRMHDEKVDLWSLGVLCYEFLVGKPPF--EANTYQETYKrISR 217
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 248 VLGTEDLYdyidkynieldprfndilgrhsrkrwerfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14116  218 VEFTFPDF-------------------------------------VTEGARDLISRLLKHNPSQRPMLREVLEHPW 256
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
128-262 4.81e-13

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: 68.41  E-value: 4.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHPNQ---------EYnvrVAsryfk 198
Cdd:cd05572   90 FDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGY-VKLVDFGFAKKLGSGRktwtfcgtpEY---VA----- 160
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504250 199 gPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFfhGHDNYDQLVRIAKVLGTEDLYDYIDKYN 262
Cdd:cd05572  161 -PEIILN-KGYDFSVDYWSLGILLYELLTGRPPF--GGDDEDPMKIYNIILKGIDKIEFPKYID 220
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
135-280 5.07e-13

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: 69.23  E-value: 5.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 135 FYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDyQMYDYSLD 214
Cdd:cd05632  108 FYAAEILCGLEDLHRENTVYRDLKPENILLD-DYGHIRISDLGLAVKIPEGESIRGRVGTVGYMAPEVLNN-QRYTLSPD 185
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 215 MWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDyiDKYNIELDPRFNDILGRHSRKR 280
Cdd:cd05632  186 YWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYS--AKFSEEAKSICKMLLTKDPKQR 249
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
37-323 5.46e-13

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: 68.90  E-value: 5.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRK-LGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENL---RGGPNIITLLDIIKDpvSRTPALV 112
Cdd:cd14173    1 DVYQLQEEvLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRVFREVEMLyqcQGHRNVLELIEFFEE--EDKFYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 113 FEHV-NNTDFKQLY--QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHR--KLRLIDWGLAEFYHPNQ- 186
Cdd:cd14173   79 FEKMrGGSILSHIHrrRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQvsPVKICDFDLGSGIKLNSd 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 187 -------EYNVRVASRYFKGPELLVDYQ----MYDYSLDMWSLGCMLASMIFRKEPFFhGHdnydqlvriakvLGTEDLY 255
Cdd:cd14173  159 cspistpELLTPCGSAEYMAPEVVEAFNeeasIYDKRCDLWSLGVILYIMLSGYPPFV-GR------------CGSDCGW 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 256 DYidkynIELDPRFNDILGRHSRKRWERFVHSENQHlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14173  226 DR-----GEACPACQNMLFESIQEGKYEFPEKDWAH-ISCAAKDLISKLLVRDAKQRLSAAQVLQHPW 287
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
133-324 5.90e-13

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 70.21  E-value: 5.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 133 IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEfyhpnqeyNVRVASRY----------FKGPEl 202
Cdd:PLN03225 257 IQTIMRQILFALDGLHSTGIVHRDVKPQNIIFSEGSGSFKIIDLGAAA--------DLRVGINYipkeflldprYAAPE- 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 203 lvDYQMYDYS------------------------LDMWSLGCMLASMIFrkePFFHGHDNYDQLVRIAKVLGtEDLydyi 258
Cdd:PLN03225 328 --QYIMSTQTpsapsapvatalspvlwqlnlpdrFDIYSAGLIFLQMAF---PNLRSDSNLIQFNRQLKRND-YDL---- 397
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528504250 259 DKYNIELDPRFN-------DILGRHSRKRWErfvhsenqhlvstealdFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:PLN03225 398 VAWRKLVEPRASpdlrrgfEVLDLDGGAGWE-----------------LLKSMMRFKGRQRISAKAALAHPYF 453
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
123-331 5.99e-13

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: 68.90  E-value: 5.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 123 QLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGL-AEFYHPNQEYNVRVASRYFKGPE 201
Cdd:cd06644  102 ELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDG-DIKLADFGVsAKNVKTLQRRDSFIGTPYWMAPE 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 202 LLVDYQM----YDYSLDMWSLGCMLASMIfRKEPFFHGHDNYDQLVRIAKvlgtedlydyidkynieldprfNDILGRHS 277
Cdd:cd06644  181 VVMCETMkdtpYDYKADIWSLGITLIEMA-QIEPPHHELNPMRVLLKIAK----------------------SEPPTLSQ 237
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528504250 278 RKRWerfvhsenqhlvSTEALDFLDKLLRYDHQARLTAREAMDHSYFYPIVKDQ 331
Cdd:cd06644  238 PSKW------------SMEFRDFLKTALDKHPETRPSAAQLLEHPFVSSVTSNR 279
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
113-250 6.94e-13

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: 69.35  E-value: 6.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 113 FEHVNNT--DFKQLYQTLSDY------------DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHR---KLRLID 175
Cdd:cd14228   85 FQHKNHTclVFEMLEQNLYDFlkqnkfsplplkYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVRqpyRVKVID 164
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 176 WGLAEfyHPNQEY-NVRVASRYFKGPELLVDYQMYDySLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVRIAKVLG 250
Cdd:cd14228  165 FGSAS--HVSKAVcSTYLQSRYYRAPEIILGLPFCE-AIDMWSLGCVIAEL-FLGWPLYPGASEYDQIRYISQTQG 236
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
133-324 7.09e-13

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: 69.00  E-value: 7.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 133 IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLA------------EF-----YHPNQEYnvrVASR 195
Cdd:cd14013  122 IKSIMRQILVALRKLHSTGIVHRDVKPQNIIVSEGDGQFKIIDLGAAadlriginyipkEFlldprYAPPEQY---IMST 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 196 YF-KGPELLVD-------YQMYDYSL-DMWSLGCMLASMIFrkePFFHGHDNydqlvriakvlgtedlydyIDKYNIELD 266
Cdd:cd14013  199 QTpSAPPAPVAaalspvlWQMNLPDRfDMYSAGVILLQMAF---PNLRSDSN-------------------LIAFNRQLK 256
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504250 267 PRFNDIlgrhsrKRWERFVHSENQHLVsTEALDFLD-----------KLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14013  257 QCDYDL------NAWRMLVEPRASADL-REGFEILDlddgagwdlvtKLIRYKPRGRLSASAALAHPYF 318
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
90-234 7.23e-13

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: 68.07  E-value: 7.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  90 GGPNIITLLDIIKDPVSRTpaLVFEHVNNT----DFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMID 165
Cdd:cd14100   63 GFRGVIRLLDWFERPDSFV--LVLERPEPVqdlfDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILID 140
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504250 166 HEHRKLRLIDWGLAEFYHpNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFH 234
Cdd:cd14100  141 LNTGELKLIDFGSGALLK-DTVYTDFDGTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDIPFEH 208
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
92-324 8.97e-13

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: 67.61  E-value: 8.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKdpVSRTPALVFEHVNNTDF-KQLYQ--TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEH 168
Cdd:cd14107   58 RRLTCLLDQFE--TRKTLILILELCSSEELlDRLFLkgVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPT 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 RK-LRLIDWGLAEFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFhGHDNYDQLVRIAK 247
Cdd:cd14107  136 REdIKICDFGFAQEITPSEHQFSKYGSPEFVAPE-IVHQEPVSAATDIWALGVIAYLSLTCHSPFA-GENDRATLLNVAE 213
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504250 248 vlgtedlydyidkynieldprfndilGRHSrkrWE--RFVHsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14107  214 --------------------------GVVS---WDtpEITH------LSEDAKDFIKRVLQPDPEKRPSASECLSHEWF 257
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
128-289 9.54e-13

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: 67.70  E-value: 9.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLA---------EFYHPNQEYNVRVASR--- 195
Cdd:cd14010   91 LPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLD-GNGTLKLSDFGLArregeilkeLFGQFSDEGNVNKVSKkqa 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 196 -----YFKGPELLVDYQmYDYSLDMWSLGCMLASMIFRKEPFFhgHDNYDQLVRiaKVLgTEDLYDYIDKYNIELDPRFN 270
Cdd:cd14010  170 krgtpYYMAPELFQGGV-HSFASDLWALGCVLYEMFTGKPPFV--AESFTELVE--KIL-NEDPPPPPPKVSSKPSPDFK 243
                        170       180
                 ....*....|....*....|....*
gi 528504250 271 DILGR------HSRKRWERFVHSEN 289
Cdd:cd14010  244 SLLKGllekdpAKRLSWDELVKHPF 268
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
85-324 1.00e-12

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: 67.80  E-value: 1.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  85 LENLRGGPNIITLLDIIKdpvsrTPA---LVFEHVNNTD-FKQLYQT--LSDYDIRFYMYEILKALDYCHSMGIMHRDVK 158
Cdd:cd05583   52 LEAVRQSPFLVTLHYAFQ-----TDAklhLILDYVNGGElFTHLYQRehFTESEVRIYIGEIVLALEHLHKLGIIYRDIK 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 159 PHNVMIDHE-HrkLRLIDWGLAEFYHPNQEYnvRVASryFKG------PELL-VDYQMYDYSLDMWSLGCMLASMIFRKE 230
Cdd:cd05583  127 LENILLDSEgH--VVLTDFGLSKEFLPGEND--RAYS--FCGtieymaPEVVrGGSDGHDKAVDWWSLGVLTYELLTGAS 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 231 PFfhghdnydqlvriakvlGTEDlydyidkynieldprfndilGRHSRKRWERFVHSEN---QHLVSTEALDFLDKLLRY 307
Cdd:cd05583  201 PF-----------------TVDG--------------------ERNSQSEISKRILKSHppiPKTFSAEAKDFILKLLEK 243
                        250       260
                 ....*....|....*....|..
gi 528504250 308 DHQARL-----TAREAMDHSYF 324
Cdd:cd05583  244 DPKKRLgagprGAHEIKEHPFF 265
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
85-232 1.19e-12

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: 67.97  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  85 LENLRGGPNIITLLDIIKDPVSRTpaLVFEHVNNTDF-----KQlyQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKP 159
Cdd:cd14180   54 LRLCQSHPNIVALHEVLHDQYHTY--LVMELLRGGELldrikKK--ARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKP 129
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 160 HNVMI--DHEHRKLRLIDWGLAEFYHPNQE-YNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14180  130 ENILYadESDGAVLKVIDFGFARLRPQGSRpLQTPCFTLQYAAPELFSN-QGYDESCDLWSLGVILYTMLSGQVPF 204
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
90-232 1.48e-12

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: 67.18  E-value: 1.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  90 GGPNIITLLDIIKDPvsRTPALVFE---HVNNT-DFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMID 165
Cdd:cd14101   65 GHRGVIRLLDWFEIP--EGFLLVLErpqHCQDLfDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVD 142
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 166 HEHRKLRLIDWGLAEFYHpNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14101  143 LRTGDIKLIDFGSGATLK-DSMYTDFDGTRVYSPPEWILYHQYHALPATVWSLGILLYDMVCGDIPF 208
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
92-232 1.51e-12

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: 67.16  E-value: 1.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKdpVSRTPALVFEHVNNT---DFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEh 168
Cdd:cd14072   59 PNIVKLFEVIE--TEKTLYLVMEYASGGevfDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDAD- 135
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 169 RKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELlvdYQMYDY---SLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14072  136 MNIKIADFGFSNEFTPGNKLDTFCGSPPYAAPEL---FQGKKYdgpEVDVWSLGVILYTLVSGSLPF 199
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
20-243 1.52e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 69.38  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250   20 PREYWDYESHVvdwgnqDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILE-----NLRGgPNI 94
Cdd:PTZ00266    2 PGKYDDGESRL------NEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEvnvmrELKH-KNI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250   95 ITLLDIIKDPVSRTPALVFEHVNNTDFK-------QLYQTLSDYDIRFYMYEILKALDYCHSMG-------IMHRDVKPH 160
Cdd:PTZ00266   75 VRYIDRFLNKANQKLYILMEFCDAGDLSrniqkcyKMFGKIEEHAIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  161 NVMIDHEHRKL----------------RLIDWGLAEFYHPNQEYNVRVASRYFKGPELLV-DYQMYDYSLDMWSLGCMLA 223
Cdd:PTZ00266  155 NIFLSTGIRHIgkitaqannlngrpiaKIGDFGLSKNIGIESMAHSCVGTPYYWSPELLLhETKSYDDKSDMWALGCIIY 234
                         250       260
                  ....*....|....*....|
gi 528504250  224 SMIFRKEPfFHGHDNYDQLV 243
Cdd:PTZ00266  235 ELCSGKTP-FHKANNFSQLI 253
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
92-232 1.62e-12

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: 66.91  E-value: 1.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKdpvsrTPA---LVFEHVNNT---DFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMID 165
Cdd:cd14079   62 PHIIRLYEVIE-----TPTdifMVMEYVSGGelfDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLD 136
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 166 HeHRKLRLIDWGLAEFYH-----------PNQEYNVRVASRYFKGPEllvdyqmydysLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14079  137 S-NMNVKIADFGLSNIMRdgeflktscgsPNYAAPEVISGKLYAGPE-----------VDVWSCGVILYALLCGSLPF 202
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
111-242 1.66e-12

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: 67.66  E-value: 1.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFKQLYQTLSDYDI---RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLA-EFYHPNQ 186
Cdd:cd05620   73 FVMEFLNGGDLMFHIQDKGRFDLyraTFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGH-IKIADFGMCkENVFGDN 151
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 187 EYNVRVASRYFKGPELLVDYQmYDYSLDMWSLGCMLASMIFRKEPfFHGhDNYDQL 242
Cdd:cd05620  152 RASTFCGTPDYIAPEILQGLK-YTFSVDWWSFGVLLYEMLIGQSP-FHG-DDEDEL 204
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
45-323 1.67e-12

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: 67.02  E-value: 1.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  45 LGRGKYSEVFEAINITNNE----------KVVVKILKPVKKKKIKREIKILENLRG--GPNIITLLDIikdpvSRTP--- 109
Cdd:cd06629    9 IGKGTYGRVYLAMNATTGEmlavkqvelpKTSSDRADSRQKTVVDALKSEIDTLKDldHPNIVQYLGF-----EETEdyf 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 110 ALVFEHVNNTDFKQLYQTLSDYD---IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGL----AEFY 182
Cdd:cd06629   84 SIFLEYVPGGSIGSCLRKYGKFEedlVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEG-ICKISDFGIskksDDIY 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 183 HPNQEYNVRvASRYFKGPELLVDY-QMYDYSLDMWSLGCMLASMIFRKEPFfhghdNYDQLVRIAKVLGTEDlydyidky 261
Cdd:cd06629  163 GNNGATSMQ-GSVFWMAPEVIHSQgQGYSAKVDIWSLGCVVLEMLAGRRPW-----SDDEAIAAMFKLGNKR-------- 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528504250 262 niELDPRFNDIlgrhsrkrwerfvhsenqhLVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd06629  229 --SAPPVPEDV-------------------NLSPEALDFLNACFAIDPRDRPTAAELLSHPF 269
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
85-324 1.72e-12

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: 67.27  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  85 LENLRGGPNIITLLDIIKDPVSRTpaLVFEHVNNTD-FKQLY----QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKP 159
Cdd:cd14197   62 LELAQANPWVINLHEVYETASEMI--LVLEYAAGGEiFNQCVadreEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKP 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 160 HNVMIDHEHR--KLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPFFhGHD 237
Cdd:cd14197  140 QNILLTSESPlgDIKIVDFGLSRILKNSEELREIMGTPEYVAPEIL-SYEPISTATDMWSIGVLAYVMLTGISPFL-GDD 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 238 NYDQLVRIAKVlgtedlydyidkyNIELDprfndilgrhsrkrwerfvhSENQHLVSTEALDFLDKLLRYDHQARLTARE 317
Cdd:cd14197  218 KQETFLNISQM-------------NVSYS--------------------EEEFEHLSESAIDFIKTLLIKKPENRATAED 264

                 ....*..
gi 528504250 318 AMDHSYF 324
Cdd:cd14197  265 CLKHPWL 271
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
134-327 1.83e-12

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: 67.72  E-value: 1.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLA-EFYHPNQEYNVRVASRYFKGPELLVDYQmYDYS 212
Cdd:cd05595   98 RFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGH-IKITDFGLCkEGITDGATMKTFCGTPEYLAPEVLEDND-YGRA 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 213 LDMWSLGCMLASMIFRKEPFFhghdNYDQlvriakvlgtEDLYDYIDKYNIeldprfndilgrhsrkrweRFVHSenqhl 292
Cdd:cd05595  176 VDWWGLGVVMYEMMCGRLPFY----NQDH----------ERLFELILMEEI-------------------RFPRT----- 217
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 528504250 293 VSTEALDFLDKLLRYDHQARL-----TAREAMDHSYFYPI 327
Cdd:cd05595  218 LSPEAKSLLAGLLKKDPKQRLgggpsDAKEVMEHRFFLSI 257
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
134-330 1.84e-12

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: 67.77  E-value: 1.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE-HRKlrLIDWGLAEfyhpnQEYNVRVASRYFKG------PELLVDY 206
Cdd:cd05571   98 RFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDgHIK--ITDFGLCK-----EEISYGATTKTFCGtpeylaPEVLEDN 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 207 QmYDYSLDMWSLGCMLASMIFRKEPFFhghdNYDQLVRIAKVLgTEDLydyidkynieldpRFNDILgrhsrkrwerfvh 286
Cdd:cd05571  171 D-YGRAVDWWGLGVVMYEMMCGRLPFY----NRDHEVLFELIL-MEEV-------------RFPSTL------------- 218
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 528504250 287 senqhlvSTEALDFLDKLLRYDHQARL-----TAREAMDHSYFYPIVKD 330
Cdd:cd05571  219 -------SPEAKSLLAGLLKKDPKKRLgggprDAKEIMEHPFFASINWD 260
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
135-232 2.01e-12

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: 67.24  E-value: 2.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 135 FYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDyQMYDYSLD 214
Cdd:cd05607  108 FYSAQITCGILHLHSLKIVYRDMKPENVLLD-DNGNCRLSDLGLAVEVKEGKPITQRAGTNGYMAPEILKE-ESYSYPVD 185
                         90
                 ....*....|....*...
gi 528504250 215 MWSLGCMLASMIFRKEPF 232
Cdd:cd05607  186 WFAMGCSIYEMVAGRTPF 203
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
90-323 2.02e-12

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: 66.94  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  90 GGPNIITLLDIIKD--PVSRTPALVFEHVNNTD-FKQLY----QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:cd14172   55 GGPHIVHILDVYENmhHGKRCLLIIMECMEGGElFSRIQergdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENL 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 163 MIDHEHRK--LRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPFFhghDNYD 240
Cdd:cd14172  135 LYTSKEKDavLKLTDFGFAKETTVQNALQTPCYTPYYVAPEVL-GPEKYDKSCDMWSLGVIMYILLCGFPPFY---SNTG 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 241 QLV------RIAkvlgtedlydyIDKYNIElDPRFNDilgrhsrkrwerfvhsenqhlVSTEALDFLDKLLRYDHQARLT 314
Cdd:cd14172  211 QAIspgmkrRIR-----------MGQYGFP-NPEWAE---------------------VSEEAKQLIRHLLKTDPTERMT 257

                 ....*....
gi 528504250 315 AREAMDHSY 323
Cdd:cd14172  258 ITQFMNHPW 266
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
37-233 2.34e-12

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: 67.72  E-value: 2.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILEN-----LRGGPNIITLLDIIKDpvSRTPAL 111
Cdd:cd05622   73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEErdimaFANSPWVVQLFYAFQD--DRYLYM 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 VFEHVNNTDFKQLyqtLSDYDI-----RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAefYHPNQ 186
Cdd:cd05622  151 VMEYMPGGDLVNL---MSNYDVpekwaRFYTAEVVLALDAIHSMGFIHRDVKPDNMLLD-KSGHLKLADFGTC--MKMNK 224
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528504250 187 EYNVR----VASRYFKGPELLVDY---QMYDYSLDMWSLGCMLASMIFRKEPFF 233
Cdd:cd05622  225 EGMVRcdtaVGTPDYISPEVLKSQggdGYYGRECDWWSVGVFLYEMLVGDTPFY 278
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
137-324 2.40e-12

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: 67.22  E-value: 2.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 137 MYEILKALDYCHSM-GIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHpnQEYNVRVASRYFKGPELLVDYQmYDYSLDM 215
Cdd:cd14136  125 ARQVLQGLDYLHTKcGIIHTDIKPENVLLCISKIEVKIADLGNACWTD--KHFTEDIQTRQYRSPEVILGAG-YGTPADI 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 216 WSLGCM---LASMIFRKEPffHGHDNY----DQLVRIAKVLGtedlydYIDKYNIELDPRFNDILGRHSR-------KRW 281
Cdd:cd14136  202 WSTACMafeLATGDYLFDP--HSGEDYsrdeDHLALIIELLG------RIPRSIILSGKYSREFFNRKGElrhisklKPW 273
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 528504250 282 -------ERFVHSENQhlvSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14136  274 pledvlvEKYKWSKEE---AKEFASFLLPMLEYDPEKRATAAQCLQHPWL 320
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
135-232 2.88e-12

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: 66.83  E-value: 2.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 135 FYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYHPNQEYNVRVA-SRYFKGPELLVDyQMYDYSL 213
Cdd:cd05608  109 FYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDG-NVRISDLGLAVELKDGQTKTKGYAgTPGFMAPELLLG-EEYDYSV 186
                         90
                 ....*....|....*....
gi 528504250 214 DMWSLGCMLASMIFRKEPF 232
Cdd:cd05608  187 DYFTLGVTLYEMIAARGPF 205
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
128-332 3.16e-12

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: 66.30  E-value: 3.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGL-AEFYHPNQEYNVRVASRYFKGPELLVDY 206
Cdd:cd06611  100 LTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLT-LDGDVKLADFGVsAKNKSTLQKRDTFIGTPYWMAPEVVACE 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 207 QM----YDYSLDMWSLGCMLASMIFRKEPffhgHDNYDQLVRIAKVLGTEdlydyidkynielDPRFndilgrhsrkrwe 282
Cdd:cd06611  179 TFkdnpYDYKADIWSLGITLIELAQMEPP----HHELNPMRVLLKILKSE-------------PPTL------------- 228
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 528504250 283 rfvhsENQHLVSTEALDFLDKLLRYDHQARLTAREAMDHsyfyPIVKDQG 332
Cdd:cd06611  229 -----DQPSKWSSSFNDFLKSCLVKDPDDRPTAAELLKH----PFVSDQS 269
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
39-232 3.33e-12

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: 65.99  E-value: 3.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREikiLENLR---------GGPNIITLLDIIKDPVSRTp 109
Cdd:cd14070    4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYV---TKNLRregriqqmiRHPNITQLLDILETENSYY- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 110 aLVFEHVNNTDF-KQLY--QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGL---AEFYH 183
Cdd:cd14070   80 -LVMELCPGGNLmHRIYdkKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLD-ENDNIKLIDFGLsncAGILG 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528504250 184 PNQEYNVRVASRYFKGPELLVdYQMYDYSLDMWSLGCMLASMI-----FRKEPF 232
Cdd:cd14070  158 YSDPFSTQCGSPAYAAPELLA-RKKYGPKVDVWSIGVNMYAMLtgtlpFTVEPF 210
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
92-234 3.37e-12

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: 66.11  E-value: 3.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRtpALVFEHVNNT----DFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE 167
Cdd:cd14005   66 PGVIRLLDWYERPDGF--LLIMERPEPCqdlfDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLR 143
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 168 HRKLRLIDWGLAEFYHpNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFH 234
Cdd:cd14005  144 TGEVKLIDFGCGALLK-DSVYTDFDGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGDIPFEN 209
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
92-258 3.57e-12

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: 66.16  E-value: 3.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRtpALVFEHVNNtdfKQLYQTL------SDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMID 165
Cdd:cd14665   56 PNIVRFKEVILTPTHL--AIVMEYAAG---GELFERIcnagrfSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLD 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 166 -HEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDyQMYDYSL-DMWSLGCMLASMIFRKEPFFHGHDNYDQLV 243
Cdd:cd14665  131 gSPAPRLKICDFGYSKSSVLHSQPKSTVGTPAYIAPEVLLK-KEYDGKIaDVWSCGVTLYVMLVGAYPFEDPEEPRNFRK 209
                        170
                 ....*....|....*.
gi 528504250 244 RIAKVLGTE-DLYDYI 258
Cdd:cd14665  210 TIQRILSVQySIPDYV 225
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
111-281 3.94e-12

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: 65.84  E-value: 3.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNT---DFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHR--KLRLIDWGLAefyHPN 185
Cdd:cd14012   81 LLTEYAPGGslsELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAGtgIVKLTDYSLG---KTL 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 186 QEYNVRVASRYFKG-----PELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDnyDQLVRIAKVLgTEDLYDYIDK 260
Cdd:cd14012  158 LDMCSRGSLDEFKQtywlpPELAQGSKSPTRKTDVWDLGLLFLQMLFGLDVLEKYTS--PNPVLVSLDL-SASLQDFLSK 234
                        170       180
                 ....*....|....*....|.
gi 528504250 261 YNiELDPrfndilgrhsRKRW 281
Cdd:cd14012  235 CL-SLDP----------KKRP 244
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
125-275 3.95e-12

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: 65.91  E-value: 3.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 125 YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAefyhpnqeynVRVASRY-----FKG 199
Cdd:cd06630   97 YGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQRLRIADFGAA----------ARLASKGtgageFQG 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 200 ----------PELLVDYQmYDYSLDMWSLGCMLASMIFRKEPF-FHGHDNYDQLV-RIAKVLGTEDLYDYidkynieLDP 267
Cdd:cd06630  167 qllgtiafmaPEVLRGEQ-YGRSCDVWSVGCVIIEMATAKPPWnAEKISNHLALIfKIASATTPPPIPEH-------LSP 238

                 ....*...
gi 528504250 268 RFNDILGR 275
Cdd:cd06630  239 GLRDVTLR 246
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
92-280 4.07e-12

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: 65.97  E-value: 4.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDpvSRTPALVFEHVNNT---DFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEH 168
Cdd:cd14076   66 PNIVRLLDVLKT--KKYIGIVLEFVSGGelfDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLD-KN 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 RKLRLIDWGLA-EFYHPNQE-YNVRVASRYFKGPELLVDYQMYDYS-LDMWSLGCMLASMIFRKEPFFHGHDN--YDQLV 243
Cdd:cd14076  143 RNLVITDFGFAnTFDHFNGDlMSTSCGSPCYAAPELVVSDSMYAGRkADIWSCGVILYAMLAGYLPFDDDPHNpnGDNVP 222
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 528504250 244 RiakvlgtedLYDYID----KYNIELDPRFNDILGR----HSRKR 280
Cdd:cd14076  223 R---------LYRYICntplIFPEYVTPKARDLLRRilvpNPRKR 258
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
111-232 4.09e-12

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: 66.68  E-value: 4.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFK---QLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLA-EFYHPNQ 186
Cdd:cd05588   73 FVIEFVNGGDLMfhmQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGH-IKLTDYGMCkEGLRPGD 151
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 528504250 187 EYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd05588  152 TTSTFCGTPNYIAPEILRG-EDYGFSVDWWALGVLMFEMLAGRSPF 196
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
92-323 6.78e-12

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: 65.00  E-value: 6.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDpvSRTPALVFEHVNNTD---FKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEH 168
Cdd:cd14121   55 PHIVELKDFQWD--EEHIYLIMEYCSGGDlsrFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRY 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 RK-LRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFfhGHDNYDQLVriAK 247
Cdd:cd14121  133 NPvLKLADFGFAQHLKPNDEAHSLRGSPLYMAPEMILK-KKYDARVDLWSVGVILYECLFGRAPF--ASRSFEELE--EK 207
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 248 VLGTEDlydyidkynIELDPRFNdilgrhsrkrwerfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14121  208 IRSSKP---------IEIPTRPE----------------------LSADCRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
111-241 7.25e-12

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: 66.21  E-value: 7.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFK---QLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLA-EFYHPNQ 186
Cdd:cd05618   98 FVIEYVNGGDLMfhmQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGH-IKLTDYGMCkEGLRPGD 176
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 187 EYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPF--FHGHDNYDQ 241
Cdd:cd05618  177 TTSTFCGTPNYIAPEILRG-EDYGFSVDWWALGVLMFEMMAGRSPFdiVGSSDNPDQ 232
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
92-321 8.30e-12

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: 65.09  E-value: 8.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPvsRTPALVFEHVNNTD-FKQLYQ--TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMI--DH 166
Cdd:cd14083   61 PNIVQLLDIYESK--SHLYLVMELVTGGElFDRIVEkgSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYysPD 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 167 EHRKLRLIDWGLAEFYHPNQEYNVRVASRYFkGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNydqlvria 246
Cdd:cd14083  139 EDSKIMISDFGLSKMEDSGVMSTACGTPGYV-APEVLAQ-KPYGKAVDCWSIGVISYILLCGYPPFYDENDS-------- 208
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 247 kvlgteDLYDYIDKYNIELD-PRFNDIlgrhsrkrwerfvhsenqhlvSTEALDFLDKLLRYDHQARLTAREAMDH 321
Cdd:cd14083  209 ------KLFAQILKAEYEFDsPYWDDI---------------------SDSAKDFIRHLMEKDPNKRYTCEQALEH 257
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
122-232 9.59e-12

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: 64.74  E-value: 9.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 122 KQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEY-NVRVASRYFKGP 200
Cdd:cd08529   92 SQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLD-KGDNVKIGDLGVAKILSDTTNFaQTIVGTPYYLSP 170
                         90       100       110
                 ....*....|....*....|....*....|..
gi 528504250 201 ELLVDyQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd08529  171 ELCED-KPYNEKSDVWALGCVLYELCTGKHPF 201
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
37-321 1.02e-11

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: 65.13  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRK-LGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENL---RGGPNIITLLDIIKDPVSRTpaLV 112
Cdd:cd14090    1 DLYKLTGElLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRVFREVETLhqcQGHPNILQLIEYFEDDERFY--LV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 113 FEHVNNTDFKQLYQ---TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHR--KLRLIDWGLAEFYHPNQE 187
Cdd:cd14090   79 FEKMRGGPLLSHIEkrvHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvsPVKICDFDLGSGIKLSST 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 188 YN---------VRVASRYFKGPElLVD---YQ--MYDYSLDMWSLGCMLASMIFRKEPFFhGH--------------DNY 239
Cdd:cd14090  159 SMtpvttpellTPVGSAEYMAPE-VVDafvGEalSYDKRCDLWSLGVILYIMLCGYPPFY-GRcgedcgwdrgeacqDCQ 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 240 DQLV-RIakvlgTEDLYDYIDkynieldprfndilgrhsrKRWerfvhsenqHLVSTEALDFLDKLLRYDHQARLTAREA 318
Cdd:cd14090  237 ELLFhSI-----QEGEYEFPE-------------------KEW---------SHISAEAKDLISHLLVRDASQRYTAEQV 283

                 ...
gi 528504250 319 MDH 321
Cdd:cd14090  284 LQH 286
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
133-323 1.09e-11

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: 64.63  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 133 IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYHPNQ------EYNVRVASRYFKGPELLVDY 206
Cdd:cd06626  101 IRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNG-LIKLGDFGSAVKLKNNTttmapgEVNSLVGTPAYMAPEVITGN 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 207 QMYDY--SLDMWSLGCMLASMIFRKEPfFHGHDNYDQLVriakvlgtedlydyidkYNIEL--DPRFNDILGrhsrkrwe 282
Cdd:cd06626  180 KGEGHgrAADIWSLGCVVLEMATGKRP-WSELDNEWAIM-----------------YHVGMghKPPIPDSLQ-------- 233
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 528504250 283 rfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd06626  234 ----------LSPEGKDFLSRCLESDPKKRPTASELLDHPF 264
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
37-219 1.12e-11

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: 64.69  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIkreikiLENLR---------GGPNIIT----------- 96
Cdd:cd06610    1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTS------MDELRkeiqamsqcNHPNVVSyytsfvvgdel 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  97 -----------LLDIIKdpvSRTPALVFEHVNntdfkqlyqtlsdydIRFYMYEILKALDYCHSMGIMHRDVKPHNVMID 165
Cdd:cd06610   75 wlvmpllsggsLLDIMK---SSYPRGGLDEAI---------------IATVLKEVLKGLEYLHSNGQIHRDVKAGNILLG 136
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528504250 166 hEHRKLRLIDWGL-AEFYHPNQ-EYNVR---VASRYFKGPELLVDYQMYDYSLDMWSLG 219
Cdd:cd06610  137 -EDGSVKIADFGVsASLATGGDrTRKVRktfVGTPCWMAPEVMEQVRGYDFKADIWSFG 194
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
139-321 1.12e-11

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: 64.70  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLA-----EFYHPNQEYN--------------VRVASRYFKG 199
Cdd:cd14046  112 QILEGLAYIHSQGIIHRDLKPVNIFLD-SNGNVKIGDFGLAtsnklNVELATQDINkstsaalgssgdltGNVGTALYVA 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 200 PELLVDYQ-MYDYSLDMWSLGCMLASMIFrkePFFHGHDnydqlvRIaKVLGTedlydyIDKYNIELDPRFNDILGRHSR 278
Cdd:cd14046  191 PEVQSGTKsTYNEKVDMYSLGIIFFEMCY---PFSTGME------RV-QILTA------LRSVSIEFPPDFDDNKHSKQA 254
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 528504250 279 K--RWerfvhsenqhlvstealdfldkLLRYDHQARLTAREAMDH 321
Cdd:cd14046  255 KliRW----------------------LLNHDPAKRPSAQELLKS 277
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
39-233 1.36e-11

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: 64.17  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEK-----VVVKILKPVKKKKIKREIKILENLRGgPNIITLLDIIKDPVSRTpaLVF 113
Cdd:cd06627    2 YQLGDLIGRGAFGSVYKGLNLNTGEFvaikqISLEKIPKSDLKSVMGEIDLLKKLNH-PNIVKYIGSVKTKDSLY--IIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 114 EHVNNtdfKQLYQTLSDYD------IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYHPN-Q 186
Cdd:cd06627   79 EYVEN---GSLASIIKKFGkfpeslVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDG-LVKLADFGVATKLNEVeK 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 528504250 187 EYNVRVASRYFKGPELLvdyQMYDYSL--DMWSLGCMLASMIFRKEPFF 233
Cdd:cd06627  155 DENSVVGTPYWMAPEVI---EMSGVTTasDIWSVGCTVIELLTGNPPYY 200
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
94-232 1.39e-11

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: 64.21  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  94 IITLLDIIKDP-----VSRTPALVFEHVnntDFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEH 168
Cdd:cd14102   66 VIKLLDWYERPdgfliVMERPEPVKDLF---DFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRT 142
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504250 169 RKLRLIDWGLAEFYHpNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14102  143 GELKLIDFGSGALLK-DTVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPF 205
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
134-337 1.41e-11

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: 65.03  E-value: 1.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMID-HEHRKlrLIDWGLA---EFYHPNQEYNVR--VASRYFKGPELLVDyQ 207
Cdd:cd05598  104 RFYIAELVCAIESVHKMGFIHRDIKPDNILIDrDGHIK--LTDFGLCtgfRWTHDSKYYLAHslVGTPNYIAPEVLLR-T 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 208 MYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLvriaKVLgtedlydyidkynieldprfndilgrhsrkRWERFVHS 287
Cdd:cd05598  181 GYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQL----KVI------------------------------NWRTTLKI 226
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528504250 288 ENQHLVSTEALDFLDKLLRyDHQARL---TAREAMDHSYFYPIVKDQGRGAPA 337
Cdd:cd05598  227 PHEANLSPEAKDLILRLCC-DAEDRLgrnGADEIKAHPFFAGIDWEKLRKQKA 278
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
121-324 1.50e-11

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: 64.03  E-value: 1.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 121 FKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEfyHPNQEYNVRVA-SRYFKG 199
Cdd:cd14165   92 FIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDF-NIKLTDFGFSK--RCLRDENGRIVlSKTFCG 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 200 ------PELL--VDYQMYDYslDMWSLGCMLASMIFRKEPFfhGHDNYDQLVRIAKvlgtedlydyidkynieldprfnd 271
Cdd:cd14165  169 saayaaPEVLqgIPYDPRIY--DIWSLGVILYIMVCGSMPY--DDSNVKKMLKIQK------------------------ 220
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528504250 272 ilgrhsrKRWERFVHSENQhlvSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14165  221 -------EHRVRFPRSKNL---TSECKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
126-242 1.72e-11

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: 63.94  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 126 QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLA---EFYHPNQEYNvrvaSRYFkGPEL 202
Cdd:cd13997   98 SKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGT-CKIGDFGLAtrlETSGDVEEGD----SRYL-APEL 171
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 528504250 203 LVDYQMYDYSLDMWSLGCMLASMIfRKEPFFHGHDNYDQL 242
Cdd:cd13997  172 LNENYTHLPKADIFSLGVTVYEAA-TGEPLPRNGQQWQQL 210
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
132-232 1.72e-11

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: 63.95  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 132 DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIdHEHRKLRLIDWGLAEFYHPNQEYNVrVASRYFKGPELLVDyQMYDY 211
Cdd:cd08530  104 DIWRIFIQMLRGLKALHDQKILHRDLKSANILL-SAGDLVKIGDLGISKVLKKNLAKTQ-IGTPLYAAPEVWKG-RPYDY 180
                         90       100
                 ....*....|....*....|.
gi 528504250 212 SLDMWSLGCMLASMIFRKEPF 232
Cdd:cd08530  181 KSDIWSLGCLLYEMATFRPPF 201
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
92-232 1.81e-11

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: 63.73  E-value: 1.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKdpVSRTPALVFEHVNNTDFKQLYQTLSDY---DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEH 168
Cdd:cd14164   60 PNIVQMFECIE--VANGRLYIVMEAAATDLLQKIQEVHHIpkdLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADD 137
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 169 RKLRLIDWGLAEFYH-PNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14164  138 RKIKIADFGFARFVEdYPELSTTFCGSRAYTPPEVILGTPYDPKKYDVWSLGVVLYVMVTGTMPF 202
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
92-234 1.83e-11

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: 64.39  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIiKDPV-----SRTPALVFEHVNNTDFKQL------YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPH 160
Cdd:cd13989   53 PNVVSARDV-PPELeklspNDLPLLAMEYCSGGDLRKVlnqpenCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPE 131
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 161 NVMIDHEHRKL--RLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFH 234
Cdd:cd13989  132 NIVLQQGGGRViyKLIDLGYAKELDQGSLCTSFVGTLQYLAPELFES-KKYTCTVDYWSFGTLAFECITGYRPFLP 206
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
111-234 1.91e-11

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: 64.71  E-value: 1.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFKQLyqtLSDYDI-----RFYMYEILKALDYCHSMGIMHRDVKPHNVMID-HEHrkLRLIDWGLAefYHP 184
Cdd:cd05596  103 MVMDYMPGGDLVNL---MSNYDVpekwaRFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDaSGH--LKLADFGTC--MKM 175
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 185 NQEYNVR----VASRYFKGPELLVD---YQMYDYSLDMWSLGCMLASMIFRKEPFFH 234
Cdd:cd05596  176 DKDGLVRsdtaVGTPDYISPEVLKSqggDGVYGRECDWWSVGVFLYEMLVGDTPFYA 232
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
129-323 2.10e-11

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: 63.71  E-value: 2.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 129 SDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE--HRKLRLIDWGLAEFY--HPNQEYNVRVASRYFKGPELLV 204
Cdd:cd14087   95 TERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPgpDSKIMITDFGLASTRkkGPNCLMKTTCGTPEYIAPEILL 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 205 DyQMYDYSLDMWSLGCMLASMIFRKEPFfhGHDNYDQLVRiaKVLGTedlydyidKYNIELDPrfndilgrhsrkrWERf 284
Cdd:cd14087  175 R-KPYTQSVDMWAVGVIAYILLSGTMPF--DDDNRTRLYR--QILRA--------KYSYSGEP-------------WPS- 227
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528504250 285 vhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14087  228 --------VSNLAKDFIDRLLTVNPGERLSATQALKHPW 258
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
126-232 2.29e-11

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: 63.49  E-value: 2.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 126 QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHP-NQEYNVRVASRYFKGPELLv 204
Cdd:cd14188   96 KVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFIN-ENMELKVGDFGLAARLEPlEHRRRTICGTPNYLSPEVL- 173
                         90       100
                 ....*....|....*....|....*...
gi 528504250 205 DYQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14188  174 NKQGHGCESDIWALGCVMYTMLLGRPPF 201
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
122-233 2.34e-11

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: 63.69  E-value: 2.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 122 KQLYQTLSDY------DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYHPN--QEYNVRVA 193
Cdd:cd14111   84 KELLHSLIDRfrysedDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLN-AIKIVDFGSAQSFNPLslRQLGRRTG 162
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 528504250 194 SRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFF 233
Cdd:cd14111  163 TLEYMAPE-MVKGEPVGPPADIWSIGVLTYIMLSGRSPFE 201
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
135-280 2.40e-11

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: 63.86  E-value: 2.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 135 FYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELlVDYQMYDYSLD 214
Cdd:cd05631  106 FYAAELCCGLEDLQRERIVYRDLKPENILLD-DRGHIRISDLGLAVQIPEGETVRGRVGTVGYMAPEV-INNEKYTFSPD 183
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504250 215 MWSLGCMLASMIFRKEPFFH-----GHDNYDQLVRiakvlgtEDLYDYIDKYNIELDPRFNDILGRHSRKR 280
Cdd:cd05631  184 WWGLGCLIYEMIQGQSPFRKrkervKREEVDRRVK-------EDQEEYSEKFSEDAKSICRMLLTKNPKER 247
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
126-323 2.43e-11

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: 63.90  E-value: 2.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 126 QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRK--LRLIDWGLAEFYHPNQEYNVRVASRYFKGPELL 203
Cdd:cd14170   96 QAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNaiLKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVL 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 204 vDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHdnydqlvriakvlgtedlydyidkyNIELDPrfndilGRHSRKRWER 283
Cdd:cd14170  176 -GPEKYDKSCDMWSLGVIMYILLCGYPPFYSNH-------------------------GLAISP------GMKTRIRMGQ 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 528504250 284 FVHSENQ-HLVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14170  224 YEFPNPEwSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPW 264
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
141-233 2.43e-11

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: 63.62  E-value: 2.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 141 LKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYnvrVASRYFKGPE--LLVDYQMYDYSLDMWSL 218
Cdd:cd06607  111 LQGLAYLHSHNRIHRDVKAGNILLT-EPGTVKLADFGSASLVCPANSF---VGTPYWMAPEviLAMDEGQYDGKVDVWSL 186
                         90
                 ....*....|....*
gi 528504250 219 GCMLASMIFRKEPFF 233
Cdd:cd06607  187 GITCIELAERKPPLF 201
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
38-222 2.70e-11

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: 63.59  E-value: 2.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  38 DYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILE--------NLRGGPNIITLLDIIKDPVSRTp 109
Cdd:cd14052    1 RFANVELIGSGEFSQVYKVSERVPTGKVYAVKKLKPNYAGAKDRLRRLEevsilrelTLDGHDNIVQLIDSWEYHGHLY- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 110 aLVFEHVNNTD---FKQLY---QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYh 183
Cdd:cd14052   80 -IQTELCENGSldvFLSELgllGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLIT-FEGTLKIGDFGMATVW- 156
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528504250 184 PNQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCML 222
Cdd:cd14052  157 PLIRGIEREGDREYIAPEILSE-HMYDKPADIFSLGLIL 194
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
93-232 3.27e-11

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: 63.43  E-value: 3.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIKDPVSRTPALVFEHVNNTDFKQL--YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMI-DHEHr 169
Cdd:cd14200   84 NIVKLIEVLDDPAEDNLYMVFDLLRKGPVMEVpsDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLgDDGH- 162
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 170 kLRLIDWGLAEFYHPNQ-EYNVRVASRYFKGPELLVD--YQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14200  163 -VKIADFGVSNQFEGNDaLLSSTAGTPAFMAPETLSDsgQSFSGKALDVWAMGVTLYCFVYGKCPF 227
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
39-324 5.19e-11

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: 63.20  E-value: 5.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLR--GGPNIITLLD--IIKDPVsrtpALVFE 114
Cdd:cd06656   21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRenKNPNIVNYLDsyLVGDEL----WVVME 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 115 HVNNTDFKQLYQT--LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYHPNQ-EYNVR 191
Cdd:cd06656   97 YLAGGSLTDVVTEtcMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDG-SVKLTDFGFCAQITPEQsKRSTM 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 192 VASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFhgHDNYDQLVRIAKVLGTEDLydyidkynieldprfnd 271
Cdd:cd06656  176 VGTPYWMAPE-VVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL--NENPLRALYLIATNGTPEL----------------- 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528504250 272 ilgrhsrkrwerfvhsENQHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd06656  236 ----------------QNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 272
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
125-220 5.23e-11

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: 62.65  E-value: 5.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 125 YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLA-EFYHPNQEYNVRVASRYFKGPELL 203
Cdd:cd06609   92 PGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLS-EEGDVKLADFGVSgQLTSTMSKRNTFVGTPFWMAPEVI 170
                         90
                 ....*....|....*..
gi 528504250 204 VDyQMYDYSLDMWSLGC 220
Cdd:cd06609  171 KQ-SGYDEKADIWSLGI 186
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
37-236 5.55e-11

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: 62.70  E-value: 5.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILK--PVKKKKIKREIKILENLRGGPNIITLLDIIKDP---VSRTPAL 111
Cdd:cd06639   22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDpiSDVDEEIEAEYNILRSLPNHPNVVKFYGMFYKAdqyVGGQLWL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 VFEHVNNTDFKQLY-------QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGL-AEFYH 183
Cdd:cd06639  102 VLELCNGGSVTELVkgllkcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG-GVKLVDFGVsAQLTS 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 184 PNQEYNVRVASRYFKGPELLVDYQMYDYSL----DMWSLGCMLASMIFRKEPFFHGH 236
Cdd:cd06639  181 ARLRRNTSVGTPFWMAPEVIACEQQYDYSYdarcDVWSLGITAIELADGDPPLFDMH 237
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
111-233 6.81e-11

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: 63.09  E-value: 6.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFKQLyqtLSDYDI-----RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAefYHPN 185
Cdd:cd05621  129 MVMEYMPGGDLVNL---MSNYDVpekwaKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLD-KYGHLKLADFGTC--MKMD 202
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 186 QEYNVR----VASRYFKGPELLVDY---QMYDYSLDMWSLGCMLASMIFRKEPFF 233
Cdd:cd05621  203 ETGMVHcdtaVGTPDYISPEVLKSQggdGYYGRECDWWSVGVFLFEMLVGDTPFY 257
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
92-233 7.32e-11

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: 62.60  E-value: 7.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPvsRTPALVFEHVNNTDFKQL---YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE- 167
Cdd:cd05580   61 PFIVNLLGSFQDD--RNLYMVMEYVPGGELFSLlrrSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDg 138
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504250 168 HrkLRLIDWGLAEfyhpnqeynvRVASRYFK--------GPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFF 233
Cdd:cd05580  139 H--IKITDFGFAK----------RVKDRTYTlcgtpeylAPEIILS-KGHGKAVDWWALGILIYEMLAGYPPFF 199
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
92-234 7.33e-11

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: 62.42  E-value: 7.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDpvSRTPALVFEHVNNTD-FKQLYQT--LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEH 168
Cdd:cd14209   61 PFLVKLEYSFKD--NSNLYMVMEYVPGGEmFSHLRRIgrFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQG 138
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528504250 169 RkLRLIDWGLAEfyhpnqeynvRVASRYFK---GPELL----VDYQMYDYSLDMWSLGCMLASMIFRKEPFFH 234
Cdd:cd14209  139 Y-IKVTDFGFAK----------RVKGRTWTlcgTPEYLapeiILSKGYNKAVDWWALGVLIYEMAAGYPPFFA 200
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
123-324 7.45e-11

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: 62.25  E-value: 7.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 123 QLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHR--KLRLIDWGLAEFYHPNQEYNVRVASRYFKGP 200
Cdd:cd14198  102 DLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPlgDIKIVDFGMSRKIGHACELREIMGTPEYLAP 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 201 ELLvDYQMYDYSLDMWSLGcMLASMIFRKEPFFHGHDNYDQLVRIAKVlgtedlydyidkyNIEldprfndilgrHSRKR 280
Cdd:cd14198  182 EIL-NYDPITTATDMWNIG-VIAYMLLTHESPFVGEDNQETFLNISQV-------------NVD-----------YSEET 235
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 528504250 281 WERfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14198  236 FSS---------VSQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
140-324 8.53e-11

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: 62.31  E-value: 8.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 140 ILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGL-AEFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSL 218
Cdd:cd06659  126 VLQALAYLHSQGVIHRDIKSDSILLTLDGR-VKLSDFGFcAQISKDVPKRKSLVGTPYWMAPE-VISRCPYGTEVDIWSL 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 219 GCMLASMIFRKEPFFHghdnyDQLVRIAKvlgtedlydyidkynieldprfndilgrhsRKRWERFVHSENQHLVSTEAL 298
Cdd:cd06659  204 GIMVIEMVDGEPPYFS-----DSPVQAMK------------------------------RLRDSPPPKLKNSHKASPVLR 248
                        170       180
                 ....*....|....*....|....*.
gi 528504250 299 DFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd06659  249 DFLERMLVRDPQERATAQELLDHPFL 274
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
111-232 9.07e-11

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: 62.62  E-value: 9.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFKQLYQTLSDYD---IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE-HRKlrLIDWGLA-EFYHPN 185
Cdd:cd05590   73 FVMEFVNGGDLMFHIQKSRRFDearARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEgHCK--LADFGMCkEGIFNG 150
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 528504250 186 QEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd05590  151 KTTSTFCGTPDYIAPEILQE-MLYGPSVDWWAMGVLLYEMLCGHAPF 196
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
42-234 9.68e-11

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: 62.36  E-value: 9.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  42 VRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKR------EIKILENLRGgPNIITLLDI-IKDpvsRTPALVFE 114
Cdd:cd06633   26 LHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKwqdiikEVKFLQQLKH-PNTIEYKGCyLKD---HTAWLVME 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 115 HV--NNTDFKQLYQT-LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYnvr 191
Cdd:cd06633  102 YClgSASDLLEVHKKpLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLT-EPGQVKLADFGSASIASPANSF--- 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 528504250 192 VASRYFKGPE--LLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFH 234
Cdd:cd06633  178 VGTPYWMAPEviLAMDEGQYDGKVDIWSLGITCIELAERKPPLFN 222
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
92-323 1.12e-10

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: 61.59  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTpaLVFEHVNNTDFKQLYQTLSDY---DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMI---D 165
Cdd:cd14184   59 PNIIMLIEEMDTPAELY--LVMELVKGGDLFDAITSSTKYterDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceyP 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 166 HEHRKLRLIDWGLAEFYHpNQEYNVrVASRYFKGPELLVDyQMYDYSLDMWSLGcMLASMIFRKEPFFHGHDNYDqlvri 245
Cdd:cd14184  137 DGTKSLKLGDFGLATVVE-GPLYTV-CGTPTYVAPEIIAE-TGYGLKVDIWAAG-VITYILLCGFPPFRSENNLQ----- 207
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 246 akvlgtEDLYDYIDKYNIELDPRFndilgrhsrkrWERfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14184  208 ------EDLFDQILLGKLEFPSPY-----------WDN---------ITDSAKELISHMLQVNVEARYTAEQILSHPW 259
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
139-324 1.58e-10

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: 61.10  E-value: 1.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYHPNQ-EYNVRVASRYFKGPElLVDYQMYDYSLDMWS 217
Cdd:cd06647  111 ECLQALEFLHSNQVIHRDIKSDNILLGMDG-SVKLTDFGFCAQITPEQsKRSTMVGTPYWMAPE-VVTRKAYGPKVDIWS 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 218 LGCMLASMIFRKEPFFhgHDNYDQLVRIAKVLGTEDLydyidkynieldprfndilgrhsrkrwerfvhsENQHLVSTEA 297
Cdd:cd06647  189 LGIMAIEMVEGEPPYL--NENPLRALYLIATNGTPEL---------------------------------QNPEKLSAIF 233
                        170       180
                 ....*....|....*....|....*..
gi 528504250 298 LDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd06647  234 RDFLNRCLEMDVEKRGSAKELLQHPFL 260
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
39-324 1.68e-10

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: 61.66  E-value: 1.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLR--GGPNIITLLD--IIKDPVsrtpALVFE 114
Cdd:cd06654   22 YTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRenKNPNIVNYLDsyLVGDEL----WVVME 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 115 HVNNTDFKQLYQT--LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYHPNQ-EYNVR 191
Cdd:cd06654   98 YLAGGSLTDVVTEtcMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDG-SVKLTDFGFCAQITPEQsKRSTM 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 192 VASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFhgHDNYDQLVRIAKVLGTEDLydyidkynieldprfnd 271
Cdd:cd06654  177 VGTPYWMAPE-VVTRKAYGPKVDIWSLGIMAIEMIEGEPPYL--NENPLRALYLIATNGTPEL----------------- 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528504250 272 ilgrhsrkrwerfvhsENQHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd06654  237 ----------------QNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 273
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
92-232 1.93e-10

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: 60.93  E-value: 1.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRtpALVFEHVNNTDFKQLYQTLSD---YDIRF-YMYEILKALDYCHSM--GIMHRDVKPHNVMID 165
Cdd:cd13978   52 SYVLPLLGVCVERRSL--GLVMEYMENGSLKSLLEREIQdvpWSLRFrIIHEIALGMNFLHNMdpPLLHHDLKPENILLD 129
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504250 166 hEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKG------PELLVD-YQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd13978  130 -NHFHVKISDFGLSKLGMKSISANRRRGTENLGGtpiymaPEAFDDfNKKPTSKSDVYSFAIVIWAVLTRKEPF 202
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
92-275 1.98e-10

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: 61.28  E-value: 1.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLD--IIKDPVsrtpALVFEHVNNTDFKQLYQT--LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE 167
Cdd:cd06655   76 PNIVNFLDsfLVGDEL----FVVMEYLAGGSLTDVVTEtcMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMD 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 168 HrKLRLIDWGLAEFYHPNQ-EYNVRVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFhgHDNYDQLVRIA 246
Cdd:cd06655  152 G-SVKLTDFGFCAQITPEQsKRSTMVGTPYWMAPE-VVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL--NENPLRALYLI 227
                        170       180
                 ....*....|....*....|....*....
gi 528504250 247 KVLGTEDLYDyidkyNIELDPRFNDILGR 275
Cdd:cd06655  228 ATNGTPELQN-----PEKLSPIFRDFLNR 251
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
123-280 2.02e-10

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: 60.91  E-value: 2.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 123 QLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYhpNQEYNVR---VASRYFKG 199
Cdd:cd08221   93 QKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADL-VKLGDFGISKVL--DSESSMAesiVGTPYYMS 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 200 PElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFfhghDNYDQLvRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRK 279
Cdd:cd08221  170 PE-LVQGVKYNFKSDIWAVGCVLYELLTLKRTF----DATNPL-RLAVKIVQGEYEDIDEQYSEEIIQLVHDCLHQDPED 243

                 .
gi 528504250 280 R 280
Cdd:cd08221  244 R 244
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
134-233 2.08e-10

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: 61.30  E-value: 2.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHpNQEYNVRVASRYFkGPELLVDyQMYDYSL 213
Cdd:cd05612  104 LFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGH-IKLTDFGFAKKLR-DRTWTLCGTPEYL-APEVIQS-KGHNKAV 179
                         90       100
                 ....*....|....*....|
gi 528504250 214 DMWSLGCMLASMIFRKEPFF 233
Cdd:cd05612  180 DWWALGILIYEMLVGYPPFF 199
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
92-234 2.20e-10

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: 60.86  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTPALVFEHVNNTDFKQLYQTLSDYDIR----FYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE 167
Cdd:cd05038   66 EYIVKYKGVCESPGRRSLRLIMEYLPSGSLRDYLQRHRDQIDLkrllLFASQICKGMEYLGSQRYIHRDLAARNILVESE 145
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504250 168 HRkLRLIDWGLAEFYHPNQEY----NVRVASRYFKGPELLVDYQMYDYSlDMWSLGCMLASMIFRKEPFFH 234
Cdd:cd05038  146 DL-VKISDFGLAKVLPEDKEYyyvkEPGESPIFWYAPECLRESRFSSAS-DVWSFGVTLYELFTYGDPSQS 214
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
39-323 2.65e-10

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: 60.64  E-value: 2.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNekvvvkilkpvkkkkIKREIKILENLRGGPNIITLL----DIIK----------DP 104
Cdd:cd14097    3 YTFGRKLGQGSFGVVIEATHKETQ---------------TKWAIKKINREKAGSSAVKLLerevDILKhvnhahiihlEE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 105 VSRTPA---LVFEHVNNTDFKQLYQ---TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVM-----IDHEHR-KLR 172
Cdd:cd14097   68 VFETPKrmyLVMELCEDGELKELLLrkgFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILvkssiIDNNDKlNIK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 173 LIDWGLAEfyhpnQEYNVRVA-------SRYFKGPElLVDYQMYDYSLDMWSLGcMLASMIFRKEPFFHGHDNydqlvri 245
Cdd:cd14097  148 VTDFGLSV-----QKYGLGEDmlqetcgTPIYMAPE-VISAHGYSQQCDIWSIG-VIMYMLLCGEPPFVAKSE------- 213
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 246 akvlgtEDLYDYIDKYNIELdprfndilgrhSRKRWERfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14097  214 ------EKLFEEIRKGDLTF-----------TQSVWQS---------VSDAAKNVLQQLLKVDPAHRMTASELLDNPW 265
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
88-242 3.07e-10

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: 60.78  E-value: 3.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  88 LRGGPNIITLLDIIKDPVSRTpALVFEHVNNTDFKQLYQTLSDYD---IRFYMYEILKALDYCHSMGIMHRDVKPHNVMI 164
Cdd:cd05616   56 LSGKPPFLTQLHSCFQTMDRL-YFVMEYVNGGDLMYHIQQVGRFKephAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVML 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 165 DHEHRkLRLIDWGLAEfyhpnQEYNVRVASRYFKG------PELLVdYQMYDYSLDMWSLGCMLASMIFRKEPfFHGHDN 238
Cdd:cd05616  135 DSEGH-IKIADFGMCK-----ENIWDGVTTKTFCGtpdyiaPEIIA-YQPYGKSVDWWAFGVLLYEMLAGQAP-FEGEDE 206

                 ....
gi 528504250 239 yDQL 242
Cdd:cd05616  207 -DEL 209
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
39-182 3.15e-10

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: 60.16  E-value: 3.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVV-KILKPVKKKKIKREIKILENLRGGPNIITLLDIIKDpvSRTPALVFehvn 117
Cdd:cd14016    2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIkIEKKDSKHPQLEYEAKVYKLLQGGPGIPRLYWFGQE--GDYNVMVM---- 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 118 ntDF--KQLYQTLSDYDIRFYM-------YEILKALDYCHSMGIMHRDVKPHNVMIDHE--HRKLRLIDWGLAEFY 182
Cdd:cd14016   76 --DLlgPSLEDLFNKCGRKFSLktvlmlaDQMISRLEYLHSKGYIHRDIKPENFLMGLGknSNKVYLIDFGLAKKY 149
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
111-324 3.26e-10

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: 60.66  E-value: 3.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFKQLYQTLSDYDI---RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHPNQE 187
Cdd:cd05585   71 LVLAFINGGELFHHLQREGRFDLsraRFYTAELLCALECLHKFNVIYRDLKPENILLDYTGH-IALCDFGLCKLNMKDDD 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 188 -YNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFhgHDNYDQLVRiaKVLgTEDLydyidkynield 266
Cdd:cd05585  150 kTNTFCGTPEYLAPELLLG-HGYTKAVDWWTLGVLLYEMLTGLPPFY--DENTNEMYR--KIL-QEPL------------ 211
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504250 267 pRFNDILGRhsrkrwerfvhsenqhlvstEALDFLDKLLRYDHQARL---TAREAMDHSYF 324
Cdd:cd05585  212 -RFPDGFDR--------------------DAKDLLIGLLNRDPTKRLgynGAQEIKNHPFF 251
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
37-333 3.61e-10

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: 60.26  E-value: 3.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRKLGRGKYSEVFEAINITNN-----EKVVVKILKPVKKKKIKREIKILENLRGGPNIITLLDIIKDpvSRTPAL 111
Cdd:cd14117    6 DDFDIGRPLGKGKFGNVYLAREKQSKfivalKVLFKSQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHD--RKRIYL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 VFEHVNNTD-FKQL--YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAeFYHPNQEY 188
Cdd:cd14117   84 ILEYAPRGElYKELqkHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKG-ELKIADFGWS-VHAPSLRR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 189 NVRVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNydqlvriakvlgteDLYDYIDKYNIELDPr 268
Cdd:cd14117  162 RTMCGTLDYLPPE-MIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHT--------------ETYRRIVKVDLKFPP- 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 269 fndilgrhsrkrwerfvhsenqhLVSTEALDFLDKLLRYDHQARLTAREAMDHsyfyPIVKDQGR 333
Cdd:cd14117  226 -----------------------FLSDGSRDLISKLLRYHPSERLPLKGVMEH----PWVKANSR 263
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
123-323 3.61e-10

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: 60.43  E-value: 3.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 123 QLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGL-AEFYHPNQEYNVRVASRYFKGPE 201
Cdd:cd06643   95 ELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDG-DIKLADFGVsAKNTRTLQRRDSFIGTPYWMAPE 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 202 LLV----DYQMYDYSLDMWSLGCMLASMIfRKEPFFHGHDNYDQLVRIAKVlgtedlydyidkynielDPrfnDILGRHS 277
Cdd:cd06643  174 VVMcetsKDRPYDYKADVWSLGVTLIEMA-QIEPPHHELNPMRVLLKIAKS-----------------EP---PTLAQPS 232
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 528504250 278 rkRWerfvhsenqhlvSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd06643  233 --RW------------SPEFKDFLRKCLEKNVDARWTTSQLLQHPF 264
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
38-275 3.88e-10

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: 60.40  E-value: 3.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  38 DYQLVRKLGRGKYSEVFEAINITNNEK----------VVVKILKPVKKKKIKREIKILENLRGGPNIITLLDIIKDPVSR 107
Cdd:cd05613    1 NFELLKVLGTGAYGKVFLVRKVSGHDAgklyamkvlkKATIVQKAKTAEHTRTERQVLEHIRQSPFLVTLHYAFQTDTKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 108 tpALVFEHVNNTD-FKQLYQ--TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLA-EFYH 183
Cdd:cd05613   81 --HLILDYINGGElFTHLSQreRFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGH-VVLTDFGLSkEFLL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 184 PNQE--YNVRVASRYFkGPELLVDYQM-YDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEdlydyiDK 260
Cdd:cd05613  158 DENEraYSFCGTIEYM-APEIVRGGDSgHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSE------PP 230
                        250
                 ....*....|....*
gi 528504250 261 YNIELDPRFNDILGR 275
Cdd:cd05613  231 YPQEMSALAKDIIQR 245
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
121-233 3.90e-10

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: 60.43  E-value: 3.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 121 FKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYHP-NQEYNVRVASRYFKG 199
Cdd:cd08229  118 FKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATG-VVKLGDLGLGRFFSSkTTAAHSLVGTPYYMS 196
                         90       100       110
                 ....*....|....*....|....*....|....
gi 528504250 200 PELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFF 233
Cdd:cd08229  197 PERIHE-NGYNFKSDIWSLGCLLYEMAALQSPFY 229
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
39-243 4.16e-10

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: 59.97  E-value: 4.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEK-----VVVKILKPVKKKKIKREIKILENLRGgPNIITLLDIIKDpvSRTPALVF 113
Cdd:cd08225    2 YEIIKKIGEGSFGKIYLAKAKSDSEHcvikeIDLTKMPVKEKEASKKEVILLAKMKH-PNIVTFFASFQE--NGRLFIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 114 EHVNNTDFKQLYQT-----LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPNQEY 188
Cdd:cd08225   79 EYCDGGDLMKRINRqrgvlFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVAKLGDFGIARQLNDSMEL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 189 -NVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFfhGHDNYDQLV 243
Cdd:cd08225  159 aYTCVGTPYYLSPEICQN-RPYNNKTDIWSLGCVLYELCTLKHPF--EGNNLHQLV 211
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
128-231 4.18e-10

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: 60.09  E-value: 4.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQ-EYNVRVASRYFKGPElLVDY 206
Cdd:cd06641   98 LDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLS-EHGEVKLADFGVAGQLTDTQiKRN*FVGTPFWMAPE-VIKQ 175
                         90       100
                 ....*....|....*....|....*
gi 528504250 207 QMYDYSLDMWSLGcMLASMIFRKEP 231
Cdd:cd06641  176 SAYDSKADIWSLG-ITAIELARGEP 199
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
93-323 4.23e-10

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: 60.45  E-value: 4.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIKDPvsRTPALVFEHVNNTD-FKQLYQT--LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMI--DHE 167
Cdd:cd14168   69 NIVALEDIYESP--NHLYLVMQLVSGGElFDRIVEKgfYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsQDE 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 168 HRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNydqlvriak 247
Cdd:cd14168  147 ESKIMISDFGLSKMEGKGDVMSTACGTPGYVAPEVLAQ-KPYSKAVDCWSIGVIAYILLCGYPPFYDENDS--------- 216
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 248 vlgteDLYDYIDKYNIELD-PRFNDIlgrhsrkrwerfvhsenqhlvSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14168  217 -----KLFEQILKADYEFDsPYWDDI---------------------SDSAKDFIRNLMEKDPNKRYTCEQALRHPW 267
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
138-321 4.39e-10

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: 59.91  E-value: 4.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 138 YEILKALDYCHSM-GIMHRDVKPHNVMIDHEhRKLRLIDWGLAEFYHPNQEY-NVRVASRYFKGPELLvDYQMYDYSLDM 215
Cdd:cd06623  106 RQILKGLDYLHTKrHIIHRDIKPSNLLINSK-GEVKIADFGISKVLENTLDQcNTFVGTVTYMSPERI-QGESYSYAADI 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 216 WSLGCMLASMIFRKEPFFHghdnydqlvriAKVLGTEDLYDYI-DKYNIELDPrfndilgrhsrkrwerfvhsenqHLVS 294
Cdd:cd06623  184 WSLGLTLLECALGKFPFLP-----------PGQPSFFELMQAIcDGPPPSLPA-----------------------EEFS 229
                        170       180
                 ....*....|....*....|....*..
gi 528504250 295 TEALDFLDKLLRYDHQARLTAREAMDH 321
Cdd:cd06623  230 PEFRDFISACLQKDPKKRPSAAELLQH 256
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
92-232 4.84e-10

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: 59.49  E-value: 4.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDpvSRTPALVFEHVNNTD----FKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE 167
Cdd:cd14186   61 PSILELYNYFED--SNYVYLVLEMCHNGEmsryLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRN 138
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 168 hRKLRLIDWGLA-EFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14186  139 -MNIKIADFGLAtQLKMPHEKHFTMCGTPNYISPE-IATRSAHGLESDVWSLGCMFYTLLVGRPPF 202
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
93-323 5.47e-10

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: 60.01  E-value: 5.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIKdpvSRTP-ALVFEHVNNTD-FKQLYQ--TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVM--IDH 166
Cdd:cd14166   61 NIVTLEDIYE---STTHyYLVMQLVSGGElFDRILErgVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLylTPD 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 167 EHRKLRLIDWGLAEFyHPNQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNydqlvria 246
Cdd:cd14166  138 ENSKIMITDFGLSKM-EQNGIMSTACGTPGYVAPEVLAQ-KPYSKAVDCWSIGVITYILLCGYPPFYEETES-------- 207
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 247 kvlgteDLYDYIDKYNIELD-PRFNDIlgrhsrkrwerfvhsenqhlvSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14166  208 ------RLFEKIKEGYYEFEsPFWDDI---------------------SESAKDFIRHLLEKNPSKRYTCEKALSHPW 258
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
127-324 7.20e-10

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: 59.15  E-value: 7.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 127 TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV-MIDHEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPElLVD 205
Cdd:cd14108   93 TVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLlMADQKTDQVRICDFGNAQELTPNEPQYCKYGTPEFVAPE-IVN 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 206 YQMYDYSLDMWSLGCMLASMIFRKEPFFhGHDNYDQLVRIAkvlgtedlydyidKYNIELDPRFNDILGRhsrkrwerfv 285
Cdd:cd14108  172 QSPVSKVTDIWPVGVIAYLCLTGISPFV-GENDRTTLMNIR-------------NYNVAFEESMFKDLCR---------- 227
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528504250 286 hsenqhlvstEALDFLDKLLRYDhQARLTAREAMDHSYF 324
Cdd:cd14108  228 ----------EAKGFIIKVLVSD-RLRPDAEETLEHPWF 255
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
128-321 7.26e-10

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: 58.96  E-value: 7.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMI--DHEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVD 205
Cdd:cd14082  100 LPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLasAEPFPQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLRN 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 206 yQMYDYSLDMWSLGCMLASMIFRKEPFfhghdNYDqlvriakvlgtEDLYDYIDKYNIELDPrfndilgrhsrKRWErfv 285
Cdd:cd14082  180 -KGYNRSLDMWSVGVIIYVSLSGTFPF-----NED-----------EDINDQIQNAAFMYPP-----------NPWK--- 228
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 528504250 286 hsenqhLVSTEALDFLDKLLRYDHQARLTAREAMDH 321
Cdd:cd14082  229 ------EISPDAIDLINNLLQVKMRKRYSVDKSLSH 258
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
140-324 7.65e-10

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: 59.27  E-value: 7.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 140 ILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGL-AEFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSL 218
Cdd:cd06657  125 VLKALSVLHAQGVIHRDIKSDSILLTHDGR-VKLSDFGFcAQVSKEVPRRKSLVGTPYWMAPE-LISRLPYGPEVDIWSL 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 219 GCMLASMIFRKEPFFHghdnydqlvriakvlgtEDLYDYIDKYNIELDPRFndilgrhsrkrwerfvhsENQHLVSTEAL 298
Cdd:cd06657  203 GIMVIEMVDGEPPYFN-----------------EPPLKAMKMIRDNLPPKL------------------KNLHKVSPSLK 247
                        170       180
                 ....*....|....*....|....*.
gi 528504250 299 DFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd06657  248 GFLDRLLVRDPAQRATAAELLKHPFL 273
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
140-324 8.12e-10

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: 59.36  E-value: 8.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 140 ILKALDYCHS-MGIMHRDVKPHNVMIDHeHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELL---VDYQMYDYSLDM 215
Cdd:cd06617  112 IVKALEYLHSkLSVIHRDVKPSNVLINR-NGQVKLCDFGISGYLVDSVAKTIDAGCKPYMAPERInpeLNQKGYDVKSDV 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 216 WSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKvlgtedlydyidkyniELDPRFNDilgrhsrkrwERFvhsenqhlvST 295
Cdd:cd06617  191 WSLGITMIELATGRFPYDSWKTPFQQLKQVVE----------------EPSPQLPA----------EKF---------SP 235
                        170       180
                 ....*....|....*....|....*....
gi 528504250 296 EALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd06617  236 EFQDFVNKCLKKNYKERPNYPELLQHPFF 264
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
108-234 8.22e-10

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: 59.68  E-value: 8.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 108 TPALVFEHV--NNTDFKQLYQT-LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHP 184
Cdd:cd06635   99 TAWLVMEYClgSASDLLEVHKKpLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLT-EPGQVKLADFGSASIASP 177
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528504250 185 NQEYnvrVASRYFKGPE--LLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFH 234
Cdd:cd06635  178 ANSF---VGTPYWMAPEviLAMDEGQYDGKVDVWSLGITCIELAERKPPLFN 226
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
94-232 8.41e-10

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: 58.90  E-value: 8.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  94 IITLLDIIKDPVSRTPALVFEHVNNTDFK-QL--YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrK 170
Cdd:cd06652   66 IVQYYGCLRDPQERTLSIFMEYMPGGSIKdQLksYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVG-N 144
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 171 LRLIDWG----LAEFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd06652  145 VKLGDFGaskrLQTICLSGTGMKSVTGTPYWMSPE-VISGEGYGRKADIWSVGCTVVEMLTEKPPW 209
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
111-232 8.45e-10

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 60.42  E-value: 8.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDF-KQLYQTL------SDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIdHEHRKLRLIDWGLAEFYh 183
Cdd:PTZ00267 142 LIMEYGSGGDLnKQIKQRLkehlpfQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFL-MPTGIIKLGDFGFSKQY- 219
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528504250 184 pNQEYNVRVASR-----YFKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:PTZ00267 220 -SDSVSLDVASSfcgtpYYLAPELW-ERKRYSKKADMWSLGVILYELLTLHRPF 271
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
135-232 8.50e-10

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: 59.71  E-value: 8.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 135 FYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE-HRKlrlidwgLAEFYHPNQEYNVRVASRYFKG------PElLVDYQ 207
Cdd:cd05587  101 FYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEgHIK-------IADFGMCKEGIFGGKTTRTFCGtpdyiaPE-IIAYQ 172
                         90       100
                 ....*....|....*....|....*
gi 528504250 208 MYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd05587  173 PYGKSVDWWAYGVLLYEMLAGQPPF 197
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
134-233 8.85e-10

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: 59.51  E-value: 8.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEF-YHPNQEYNVRVASRYFKGPELLVDYQMYDYS 212
Cdd:cd05586   99 KFYIAELVLALEHLHKNDIVYRDLKPENILLDANGH-IALCDFGLSKAdLTDNKTTNTFCGTTEYLAPEVLLDEKGYTKM 177
                         90       100
                 ....*....|....*....|.
gi 528504250 213 LDMWSLGCMLASMIFRKEPFF 233
Cdd:cd05586  178 VDFWSLGVLVFEMCCGWSPFY 198
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
92-232 8.93e-10

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: 58.89  E-value: 8.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKdpvsrTPA---LVFEHVNNtdfKQLYQ------TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:cd14075   61 PNIIRLYEVVE-----TLSklhLVMEYASG---GELYTkistegKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENV 132
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 163 MIDHEHRkLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14075  133 FYASNNC-VKVGDFGFSTHAKRGETLNTFCGSPPYAAPELFKDEHYIGIYVDIWALGVLLYFMVTGVMPF 201
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
134-233 1.16e-09

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 59.06  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEfyhpnqeynvRVASRYFK---GPELL----VDY 206
Cdd:PTZ00263 121 KFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGH-VKVTDFGFAK----------KVPDRTFTlcgTPEYLapevIQS 189
                         90       100
                 ....*....|....*....|....*..
gi 528504250 207 QMYDYSLDMWSLGCMLASMIFRKEPFF 233
Cdd:PTZ00263 190 KGHGKAVDWWTMGVLLYEFIAGYPPFF 216
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
92-232 1.24e-09

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: 58.21  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDpvSRTPALVFEHV-NNTDFKQLYQT----LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDH 166
Cdd:cd08220   59 PNIIEYYESFLE--DKALMIVMEYApGGTLFEYIQQRkgslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNK 136
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 167 EHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd08220  137 KRTVVKIGDFGISKILSSKSKAYTVVGTPCYISPE-LCEGKPYNQKSDIWALGCVLYELASLKRAF 201
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
128-231 1.30e-09

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: 58.53  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQ-EYNVRVASRYFKGPElLVDY 206
Cdd:cd06640   98 FDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLS-EQGDVKLADFGVAGQLTDTQiKRNTFVGTPFWMAPE-VIQQ 175
                         90       100
                 ....*....|....*....|....*
gi 528504250 207 QMYDYSLDMWSLGcMLASMIFRKEP 231
Cdd:cd06640  176 SAYDSKADIWSLG-ITAIELAKGEP 199
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
142-234 1.34e-09

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: 58.22  E-value: 1.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 142 KALDYCHSMG---IMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHpNQEYNVRVASRYFkGPELLvDYQMYDYSLDMWSL 218
Cdd:cd14058  100 KGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTVLKICDFGTACDIS-THMTNNKGSAAWM-APEVF-EGSKYSEKCDVFSW 176
                         90
                 ....*....|....*.
gi 528504250 219 GCMLASMIFRKEPFFH 234
Cdd:cd14058  177 GIILWEVITRRKPFDH 192
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
137-325 1.49e-09

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: 58.44  E-value: 1.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 137 MYEILKALDYCHSMGIMHRDVKPHNVMID----HEHRKLRLIDWGLAEFYHPNQEYNVRVA----SRYFKGPELLVD--Y 206
Cdd:cd13982  105 LRQIASGLAHLHSLNIVHRDLKPQNILIStpnaHGNVRAMISDFGLCKKLDVGRSSFSRRSgvagTSGWIAPEMLSGstK 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 207 QMYDYSLDMWSLGCMlasmifrkepFF----HGHDNYDQlvriakvlgtedlyDYIDKYNIeldprfndILGRHSRKRwe 282
Cdd:cd13982  185 RRQTRAVDIFSLGCV----------FYyvlsGGSHPFGD--------------KLEREANI--------LKGKYSLDK-- 230
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 528504250 283 rfVHSENQHLVstEALDFLDKLLRYDHQARLTAREAMDHSYFY 325
Cdd:cd13982  231 --LLSLGEHGP--EAQDLIERMIDFDPEKRPSAEEVLNHPFFW 269
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
92-323 1.54e-09

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: 58.11  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIkdpVSRTPALVF------EHVNNTDFKQLYqtLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMID 165
Cdd:cd14088   59 PNILQLVDVF---ETRKEYFIFlelatgREVFDWILDQGY--YSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYY 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 166 H--EHRKLRLIDWGLAEFyhPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFfhghdnYDQLv 243
Cdd:cd14088  134 NrlKNSKIVISDFHLAKL--ENGLIKEPCGTPEYLAPE-VVGRQRYGRPVDCWAIGVIMYILLSGNPPF------YDEA- 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 244 riakvlgTEDLYDYIDKyNIeldprFNDILG---RHSRKRWERfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMD 320
Cdd:cd14088  204 -------EEDDYENHDK-NL-----FRKILAgdyEFDSPYWDD---------ISQAAKDLVTRLMEVEQDQRITAEEAIS 261

                 ...
gi 528504250 321 HSY 323
Cdd:cd14088  262 HEW 264
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
139-233 1.57e-09

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: 58.28  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCH-SMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYNVRVA-SRYFKGPElLVDYQMYDYSLDMW 216
Cdd:cd08528  121 QMVLALRYLHkEKQIVHRDLKPNNIMLG-EDDKVTITDFGLAKQKGPESSKMTSVVgTILYSCPE-IVQNEPYGEKADIW 198
                         90
                 ....*....|....*..
gi 528504250 217 SLGCMLASMIFRKEPFF 233
Cdd:cd08528  199 ALGCILYQMCTLQPPFY 215
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
39-324 1.63e-09

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. 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. 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: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 58.89  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNE--KVVVKILKPVKKKKIKREIKILENLRGG----PN---IITLLDIIK-DPVSRT 108
Cdd:cd14216   12 YHVIRKLGWGHFSTVWLSWDIQGKRfvAMKVVKSAEHYTETALDEIKLLKSVRNSdpndPNremVVQLLDDFKiSGVNGT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 109 P-ALVFE----HVNNTDFKQLYQTLSDYDIRFYMYEILKALDYCHSM-GIMHRDVKPHNVMI------------------ 164
Cdd:cd14216   92 HiCMVFEvlghHLLKWIIKSNYQGLPLPCVKKIIRQVLQGLDYLHTKcRIIHTDIKPENILLsvneqyirrlaaeatewq 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 165 -----------DHEHRKLRLIDWGLAEFYHpnQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCM---LASMIFRKE 230
Cdd:cd14216  172 rnflvnplepkNAEKLKVKIADLGNACWVH--KHFTEDIQTRQYRSLEVLIG-SGYNTPADIWSTACMafeLATGDYLFE 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 231 PffHGHDNY----DQLVRIAKVLGTEDLYDYI-DKYNIELDPRFNDILGRHSRKRWERF-VHSENQHLVSTEA---LDFL 301
Cdd:cd14216  249 P--HSGEDYsrdeDHIALIIELLGKVPRKLIVaGKYSKEFFTKKGDLKHITKLKPWGLFeVLVEKYEWSQEEAagfTDFL 326
                        330       340
                 ....*....|....*....|...
gi 528504250 302 DKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14216  327 LPMLELIPEKRATAAECLRHPWL 349
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
37-219 1.68e-09

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: 58.48  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILK--PVKKKKIKREIKILENLRGGPNIITLLDII--KDPVSRTPA-L 111
Cdd:cd06638   18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDpiHDIDEEIEAEYNILKALSDHPNVVKFYGMYykKDVKNGDQLwL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 VFEHVNN---TD----FKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGL-AEFYH 183
Cdd:cd06638   98 VLELCNGgsvTDlvkgFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEG-GVKLVDFGVsAQLTS 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 528504250 184 PNQEYNVRVASRYFKGPELLVDYQM----YDYSLDMWSLG 219
Cdd:cd06638  177 TRLRRNTSVGTPFWMAPEVIACEQQldstYDARCDVWSLG 216
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
112-242 1.81e-09

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: 58.66  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 VFEHVNNTDFKQLYQTLSDYD---IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE-HRKlrLIDWGLA-EFYHPNQ 186
Cdd:cd05591   74 VMEYVNGGDLMFQIQRARKFDeprARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEgHCK--LADFGMCkEGILNGK 151
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 187 EYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFfhGHDNYDQL 242
Cdd:cd05591  152 TTTTFCGTPDYIAPEILQE-LEYGPSVDWWALGVLMYEMMAGQPPF--EADNEDDL 204
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
38-248 1.83e-09

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: 58.11  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  38 DYQLVRKLGRGKYSEVFEAINI-TNNEKVVVKILKPVKKKKIKREIKILE-------NLRGgPNIITLLDIIKDPVSRTP 109
Cdd:cd06653    3 NWRLGKLLGRGAFGEVYLCYDAdTGRELAVKQVPFDPDSQETSKEVNALEceiqllkNLRH-DRIVQYYGCLRDPEEKKL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 110 ALVFEHVNNTDFK-QL--YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAE----FY 182
Cdd:cd06653   82 SIFVEYMPGGSVKdQLkaYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAG-NVKLGDFGASKriqtIC 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 183 HPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFfhghDNYDQLVRIAKV 248
Cdd:cd06653  161 MSGTGIKSVTGTPYWMSPE-VISGEGYGRKADVWSVACTVVEMLTEKPPW----AEYEAMAAIFKI 221
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
111-324 1.96e-09

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: 58.55  E-value: 1.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTD-FKQLYQ--TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLA-EFYHPNQ 186
Cdd:cd05593   92 FVMEYVNGGElFFHLSRerVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGH-IKITDFGLCkEGITDAA 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 187 EYNVRVASRYFKGPELLVDYQmYDYSLDMWSLGCMLASMIFRKEPFFhghdNYDQlvriakvlgtEDLYDYIDKYNIELd 266
Cdd:cd05593  171 TMKTFCGTPEYLAPEVLEDND-YGRAVDWWGLGVVMYEMMCGRLPFY----NQDH----------EKLFELILMEDIKF- 234
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528504250 267 PRfndilgrhsrkrwerfvhsenqhLVSTEALDFLDKLLRYDHQARL-----TAREAMDHSYF 324
Cdd:cd05593  235 PR-----------------------TLSADAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFF 274
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
136-167 2.15e-09

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 59.04  E-value: 2.15e-09
                         10        20        30
                 ....*....|....*....|....*....|..
gi 528504250 136 YMYEILKALDYCHSMGIMHRDVKPHNVMIDHE 167
Cdd:NF033483 112 IMIQILSALEHAHRNGIVHRDIKPQNILITKD 143
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
125-189 2.18e-09

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: 58.71  E-value: 2.18e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 125 YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE-HRKLRliDWGLAEFYHPNQEYN 189
Cdd:cd05629   95 YDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGgHIKLS--DFGLSTGFHKQHDSA 158
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
109-233 2.19e-09

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: 58.05  E-value: 2.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 109 PALVFEHVNNTDF-KQLYQT-----LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKL--RLIDWGLAE 180
Cdd:cd14038   73 PLLAMEYCQGGDLrKYLNQFenccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLihKIIDLGYAK 152
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528504250 181 FYHPNQEYNVRVASRYFKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPFF 233
Cdd:cd14038  153 ELDQGSLCTSFVGTLQYLAPELL-EQQKYTVTVDYWSFGTLAFECITGFRPFL 204
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
92-323 2.69e-09

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: 57.28  E-value: 2.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTpaLVFEHVNN---TDFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEH 168
Cdd:cd14115   49 PQYITLHDTYESPTSYI--LVLELMDDgrlLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRI 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 169 --RKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDYQMyDYSLDMWSLGCMLASMIFRKEPFFHgHDNYDQLVRIA 246
Cdd:cd14115  127 pvPRVKLIDLEDAVQISGHRHVHHLLGNPEFAAPEVIQGTPV-SLATDIWSIGVLTYVMLSGVSPFLD-ESKEETCINVC 204
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 247 KVlgtedLYDYIDKYnieldprFNDilgrhsrkrwerfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd14115  205 RV-----DFSFPDEY-------FGD---------------------VSQAARDFINVILQEDPRRRPTAATCLQHPW 248
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
125-233 2.84e-09

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: 58.01  E-value: 2.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 125 YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE-HRKLRliDWGLAEFYHPNQEYNVRVASRYFKGPELL 203
Cdd:cd05599   95 KDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARgHIKLS--DFGLCTGLKKSHLAYSTVGTPDYIAPEVF 172
                         90       100       110
                 ....*....|....*....|....*....|.
gi 528504250 204 VdyQM-YDYSLDMWSLGCMLASMIFRKEPFF 233
Cdd:cd05599  173 L--QKgYGKECDWWSLGVIMYEMLIGYPPFC 201
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
114-230 3.02e-09

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: 57.10  E-value: 3.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 114 EHVNNTDFKQLYQT---LSdYDIRFYM-YEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLI--DWGLAEFYHPNQE 187
Cdd:cd14155   68 EYINGGNLEQLLDSnepLS-WTVRVKLaLDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAVvgDFGLAEKIPDYSD 146
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 528504250 188 YNVR---VASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKE 230
Cdd:cd14155  147 GKEKlavVGSPYWMAPEVLRG-EPYNEKADVFSYGIILCEIIARIQ 191
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
134-233 3.12e-09

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: 58.10  E-value: 3.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHeHRKLRLIDWG--LAEFYHPNQEYNVRVASRYFKGPELLVDYQ---- 207
Cdd:cd05624  176 RFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDM-NGHIRLADFGscLKMNDDGTVQSSVAVGTPDYISPEILQAMEdgmg 254
                         90       100
                 ....*....|....*....|....*.
gi 528504250 208 MYDYSLDMWSLGCMLASMIFRKEPFF 233
Cdd:cd05624  255 KYGPECDWWSLGVCMYEMLYGETPFY 280
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
134-233 3.37e-09

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: 57.74  E-value: 3.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE-HrkLRLIDWG----LAEfyHPNQEYNVRVASRYFKGPELLVDYQ- 207
Cdd:cd05597  105 RFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNgH--IRLADFGsclkLRE--DGTVQSSVAVGTPDYISPEILQAMEd 180
                         90       100
                 ....*....|....*....|....*....
gi 528504250 208 ---MYDYSLDMWSLGCMLASMIFRKEPFF 233
Cdd:cd05597  181 gkgRYGPECDWWSLGVCMYEMLYGETPFY 209
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
92-222 4.05e-09

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: 56.95  E-value: 4.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIikdpvsrtpalVFEHVNNTDFKQLYQTLSD-YDI------------RFYMYEILKALDYCHSMGIMHRDVK 158
Cdd:cd13987   50 PHIIKTYDV-----------AFETEDYYVFAQEYAPYGDlFSIippqvglpeervKRCAAQLASALDFMHSKNLVHRDIK 118
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504250 159 PHNVMI-DHEHRKLRLIDWGLAEfyhpNQEYNVRVASRY--FKGPEL--LVDYQMY--DYSLDMWSLGCML 222
Cdd:cd13987  119 PENVLLfDKDCRRVKLCDFGLTR----RVGSTVKRVSGTipYTAPEVceAKKNEGFvvDPSIDVWAFGVLL 185
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
111-232 4.33e-09

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: 57.70  E-value: 4.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNNTDFKQLYQTLSDY---DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAefyhpnQE 187
Cdd:cd05615   88 FVMEYVNGGDLMYHIQQVGKFkepQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGH-IKIADFGMC------KE 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528504250 188 YNVR-VASRYFKG------PELLVdYQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd05615  161 HMVEgVTTRTFCGtpdyiaPEIIA-YQPYGRSVDWWAYGVLLYEMLAGQPPF 211
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
92-178 4.55e-09

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: 58.32  E-value: 4.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250    92 PNIITLLDIIKDPVSRTPAlVFEHVNNTDFKQLYQT---LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMI---- 164
Cdd:TIGR03903   38 PNIVALLDSGEAPPGLLFA-VFEYVPGRTLREVLAAdgaLPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVsqtg 116
                           90
                   ....*....|....
gi 528504250   165 DHEHRKlrLIDWGL 178
Cdd:TIGR03903  117 VRPHAK--VLDFGI 128
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
134-233 4.67e-09

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: 57.72  E-value: 4.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHeHRKLRLIDWG--LAEFYHPNQEYNVRVASRYFKGPELLVDYQ---- 207
Cdd:cd05623  176 RFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDM-NGHIRLADFGscLKLMEDGTVQSSVAVGTPDYISPEILQAMEdgkg 254
                         90       100
                 ....*....|....*....|....*.
gi 528504250 208 MYDYSLDMWSLGCMLASMIFRKEPFF 233
Cdd:cd05623  255 KYGPECDWWSLGVCMYEMLYGETPFY 280
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
119-324 4.89e-09

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: 56.54  E-value: 4.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 119 TDFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGL-AEFYHPNQEYNVRVASRYF 197
Cdd:cd06613   85 QDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLT-EDGDVKLADFGVsAQLTATIAKRKSFIGTPYW 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 198 KGPELLV--DYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHdnydqlvrIAKVLgtedlydYIDKYNIELDPRFNDilgr 275
Cdd:cd06613  164 MAPEVAAveRKGGYDGKCDIWALGITAIELAELQPPMFDLH--------PMRAL-------FLIPKSNFDPPKLKD---- 224
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 528504250 276 hsRKRWerfvhsenqhlvSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd06613  225 --KEKW------------SPDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
125-324 4.99e-09

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: 56.59  E-value: 4.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 125 YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLA---EFYHPNQEYNVRVASRYFKGPE 201
Cdd:cd06625   96 YGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRD-SNGNVKLGDFGASkrlQTICSSTGMKSVTGTPYWMSPE 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 202 lLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFhghdNYDQLVRIAKVLgtedlydyidkynieldprfndilgrhsrkrw 281
Cdd:cd06625  175 -VINGEGYGRKADIWSVGCTVVEMLTTKPPWA----EFEPMAAIFKIA-------------------------------- 217
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 528504250 282 erfVHSENQHL---VSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd06625  218 ---TQPTNPQLpphVSEDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
42-234 5.13e-09

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: 56.95  E-value: 5.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  42 VRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRggpniitLLDIIKDPVS----------RTPAL 111
Cdd:cd06634   20 LREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVK-------FLQKLRHPNTieyrgcylreHTAWL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 VFEHV--NNTDFKQLYQT-LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEY 188
Cdd:cd06634   93 VMEYClgSASDLLEVHKKpLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLT-EPGLVKLGDFGSASIMAPANSF 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 528504250 189 nvrVASRYFKGPE--LLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFH 234
Cdd:cd06634  172 ---VGTPYWMAPEviLAMDEGQYDGKVDVWSLGITCIELAERKPPLFN 216
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
128-232 5.19e-09

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: 57.25  E-value: 5.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIdHEHRKLRLIDWGLA---------EFYH---------PNQEYN 189
Cdd:cd05574  100 LPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILL-HESGHIMLTDFDLSkqssvtpppVRKSlrkgsrrssVKSIEK 178
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 190 VRVA------SRYFKG------PELLVDYQmYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd05574  179 ETFVaepsarSNSFVGteeyiaPEVIKGDG-HGSAVDWWTLGILLYEMLYGTTPF 232
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
124-327 5.60e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 57.31  E-value: 5.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 124 LYQTLSDY------DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAefyhpnqEYNVRV-ASRY 196
Cdd:PHA03212 169 LYCYLAAKrniaicDILAIERSVLRAIQYLHENRIIHRDIKAENIFINHPG-DVCLGDFGAA-------CFPVDInANKY 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 197 F--------KGPELLVDyQMYDYSLDMWSLGCMLASM------IFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYN 262
Cdd:PHA03212 241 YgwagtiatNAPELLAR-DPYGPAVDIWSAGIVLFEMatchdsLFEKDGLDGDCDSDRQIKLIIRRSGTHPNEFPIDAQA 319
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 263 iELDPRFNDILGRHSRKRWERFVHSeNQHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYFYPI 327
Cdd:PHA03212 320 -NLDEIYIGLAKKSSRKPGSRPLWT-NLYELPIDLEYLICKMLAFDAHHRPSAEALLDFAAFQDI 382
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
134-324 5.63e-09

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: 56.65  E-value: 5.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMID---HehrkLRLIDWGLA---------EFYHPNQEYNVRVAS------- 194
Cdd:cd05609  103 RMYFAETVLALEYLHSYGIVHRDLKPDNLLITsmgH----IKLTDFGLSkiglmslttNLYEGHIEKDTREFLdkqvcgt 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 195 -RYFkGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFHGhdnydqlvriakvlGTEDLYDYIDKYNIEldprfndil 273
Cdd:cd05609  179 pEYI-APEVILR-QGYGKPVDWWAMGIILYEFLVGCVPFFGD--------------TPEELFGQVISDEIE--------- 233
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528504250 274 grhsrkrWerfvhSENQHLVSTEALDFLDKLLRYDHQARL---TAREAMDHSYF 324
Cdd:cd05609  234 -------W-----PEGDDALPDDAQDLITRLLQQNPLERLgtgGAEEVKQHPFF 275
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
92-234 5.71e-09

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 56.85  E-value: 5.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKD---PVSRTPALVFEHVNNTDFKQLYQT------LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:cd14039   51 PNVVKACDVPEEmnfLVNDVPLLAMEYCSGGDLRKLLNKpenccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENI 130
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528504250 163 MIDHEHRKL--RLIDWGLAEFYHPNQEYNVRVASRYFKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKEPFFH 234
Cdd:cd14039  131 VLQEINGKIvhKIIDLGYAKDLDQGSLCTSFVGTLQYLAPELF-ENKSYTVTVDYWSFGTMVFECIAGFRPFLH 203
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
137-231 6.14e-09

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: 56.60  E-value: 6.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 137 MYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQ-EYNVRVASRYFKGPElLVDYQMYDYSLDM 215
Cdd:cd06642  107 LREILKGLDYLHSERKIHRDIKAANVLLS-EQGDVKLADFGVAGQLTDTQiKRNTFVGTPFWMAPE-VIKQSAYDFKADI 184
                         90
                 ....*....|....*.
gi 528504250 216 WSLGcMLASMIFRKEP 231
Cdd:cd06642  185 WSLG-ITAIELAKGEP 199
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
133-233 6.19e-09

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: 56.26  E-value: 6.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 133 IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWG----LAefyhpnqeyNVRVASRYFKG------PEL 202
Cdd:cd06624  110 IGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYSGVVKISDFGtskrLA---------GINPCTETFTGtlqymaPEV 180
                         90       100       110
                 ....*....|....*....|....*....|..
gi 528504250 203 LVDYQM-YDYSLDMWSLGCMLASMIFRKEPFF 233
Cdd:cd06624  181 IDKGQRgYGPPADIWSLGCTIIEMATGKPPFI 212
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
140-324 7.11e-09

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: 56.59  E-value: 7.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 140 ILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGL-AEFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSL 218
Cdd:cd06658  127 VLRALSYLHNQGVIHRDIKSDSILLTSDGR-IKLSDFGFcAQVSKEVPKRKSLVGTPYWMAPE-VISRLPYGTEVDIWSL 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 219 GCMLASMIFRKEPFFHghdnydqlvriakvlgtEDLYDYIDKYNIELDPRFNDIlgrhsrkrwerfvhsenqHLVSTEAL 298
Cdd:cd06658  205 GIMVIEMIDGEPPYFN-----------------EPPLQAMRRIRDNLPPRVKDS------------------HKVSSVLR 249
                        170       180
                 ....*....|....*....|....*.
gi 528504250 299 DFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd06658  250 GFLDLMLVREPSQRATAQELLQHPFL 275
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
128-323 7.66e-09

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: 56.26  E-value: 7.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEfyHPNQE----YNVRVASRYFKgPELL 203
Cdd:cd13974  129 LSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTRKITITNFCLGK--HLVSEddllKDQRGSPAYIS-PDVL 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 204 VDYQMYDYSLDMWSLGCMLASMIFRKEPFfhghdnYDQLVR--IAKVLGTEdlydyidkYNIELDPRfndilgrhsrkrw 281
Cdd:cd13974  206 SGKPYLGKPSDMWALGVVLFTMLYGQFPF------YDSIPQelFRKIKAAE--------YTIPEDGR------------- 258
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 528504250 282 erfvhsenqhlVSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd13974  259 -----------VSENTVCLIRKLLVLNPQKRLTASEVLDSLE 289
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
137-222 9.18e-09

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: 55.98  E-value: 9.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 137 MYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLA---EFYHPNQEYNV----------RVASRYFKGPELL 203
Cdd:cd14049  126 LQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDIHVRIGDFGLAcpdILQDGNDSTTMsrlnglthtsGVGTCLYAAPEQL 205
                         90
                 ....*....|....*....
gi 528504250 204 VDYQmYDYSLDMWSLGCML 222
Cdd:cd14049  206 EGSH-YDFKSDMYSIGVIL 223
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
135-226 9.22e-09

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: 55.98  E-value: 9.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 135 FYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPEL-----LVDYQMY 209
Cdd:cd13991  102 HYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDAFLCDFGHAECLDPDGLGKSLFTGDYIPGTEThmapeVVLGKPC 181
                         90
                 ....*....|....*..
gi 528504250 210 DYSLDMWSLGCMLASMI 226
Cdd:cd13991  182 DAKVDVWSSCCMMLHML 198
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
129-247 9.51e-09

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: 55.69  E-value: 9.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 129 SDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNvMIDHEHRKLRLIDWGLAEFYHPNQEYNVRVASRYF--KGPELLVDy 206
Cdd:cd14110   97 SEAEVTDYLWQILSAVDYLHSRRILHLDLRSEN-MIITEKNLLKIVDLGNAQPFNQGKVLMTDKKGDYVetMAPELLEG- 174
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 528504250 207 QMYDYSLDMWSLGCMLASMIFRKEPfFHGHDNYDQLVRIAK 247
Cdd:cd14110  175 QGAGPQTDIWAIGVTAFIMLSADYP-VSSDLNWERDRNIRK 214
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
92-222 1.04e-08

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: 55.62  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDpvSRTPALVFEHVNNTDFKQLYQTLSDYDIRF------------YMYEILKALDYCHSMGIMHRDVKP 159
Cdd:cd00192   56 PNVVRLLGVCTE--EEPLYLVMEYMEGGDLLDFLRKSRPVFPSPepstlslkdllsFAIQIAKGMEYLASKKFVHRDLAA 133
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528504250 160 HNVMIDhEHRKLRLIDWGLAEFYHPNQEYnvrvasrYFKG----------PELLVDyQMYDYSLDMWSLGCML 222
Cdd:cd00192  134 RNCLVG-EDLVVKISDFGLSRDIYDDDYY-------RKKTggklpirwmaPESLKD-GIFTSKSDVWSFGVLL 197
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
126-328 1.09e-08

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: 56.19  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 126 QTLSDYDIRFYMYEILKALDYCHS-MGIMHRDVKPHNVMIDHEHRkLRLIDWGLA-EFYHPNQEYNVRVASRYFKGPELL 203
Cdd:cd05594  120 RVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGH-IKITDFGLCkEGIKDGATMKTFCGTPEYLAPEVL 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 204 VDYQmYDYSLDMWSLGCMLASMIFRKEPFFhghdNYDQlvriakvlgtEDLYDYIdkynIELDPRFNDILGrhsrkrwer 283
Cdd:cd05594  199 EDND-YGRAVDWWGLGVVMYEMMCGRLPFY----NQDH----------EKLFELI----LMEEIRFPRTLS--------- 250
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 528504250 284 fvhsenqhlvsTEALDFLDKLLRYDHQARL-----TAREAMDHSYFYPIV 328
Cdd:cd05594  251 -----------PEAKSLLSGLLKKDPKQRLgggpdDAKEIMQHKFFAGIV 289
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
126-232 1.21e-08

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: 55.71  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 126 QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLA-EFYHPNQEYNVRVASRYFKGPELLV 204
Cdd:cd14187  102 KALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLN-DDMEVKIGDFGLAtKVEYDGERKKTLCGTPNYIAPEVLS 180
                         90       100
                 ....*....|....*....|....*...
gi 528504250 205 DyQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14187  181 K-KGHSFEVDIWSIGCIMYTLLVGKPPF 207
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
140-324 1.33e-08

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: 55.43  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 140 ILKALDYCHS-MGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEfYHPNQEYNVRVASRYFKGPELLVDYQmYDYSLDMWSL 218
Cdd:cd06605  108 VVKGLIYLHEkHKIIHRDVKPSNILVNSRG-QVKLCDFGVSG-QLVDSLAKTFVGTRSYMAPERISGGK-YTVKSDIWSL 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 219 GCMLASMIFRKEPFfhghDNYDQLVRIAKVlgteDLYDYIDKyniELDPRFndilgrhsrkrwerfvhseNQHLVSTEAL 298
Cdd:cd06605  185 GLSLVELATGRFPY----PPPNAKPSMMIF----ELLSYIVD---EPPPLL-------------------PSGKFSPDFQ 234
                        170       180
                 ....*....|....*....|....*.
gi 528504250 299 DFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd06605  235 DFVSQCLQKDPTERPSYKELMEHPFI 260
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
92-321 1.67e-08

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: 55.38  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLD--IIKD-PVSRTPALVF---------EHVNNTDFKQlyQTLSDYDIRFYMYEILKALDYCHSM---GIMHRD 156
Cdd:cd13986   57 PNILRLLDsqIVKEaGGKKEVYLLLpyykrgslqDEIERRLVKG--TFFPEDRILHIFLGICRGLKAMHEPelvPYAHRD 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 157 VKPHNVMIDHEHRKLrLIDWG-------LAEFYHPNQEYNVRVASR---YFKGPEL--LVDYQMYDYSLDMWSLGCMLAS 224
Cdd:cd13986  135 IKPGNVLLSEDDEPI-LMDLGsmnpariEIEGRREALALQDWAAEHctmPYRAPELfdVKSHCTIDEKTDIWSLGCTLYA 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 225 MIFRKEPFFHGHDNYDQlVRIAKVLGtedlydyidKYNIELDPRFndilgrhsrkrwerfvhsenqhlvSTEALDFLDKL 304
Cdd:cd13986  214 LMYGESPFERIFQKGDS-LALAVLSG---------NYSFPDNSRY------------------------SEELHQLVKSM 259
                        250
                 ....*....|....*..
gi 528504250 305 LRYDHQARLTAREAMDH 321
Cdd:cd13986  260 LVVNPAERPSIDDLLSR 276
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
85-248 3.26e-08

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: 54.32  E-value: 3.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  85 LENLRGgPNIITLLDIIKDPVSRTPALVFEHVNNTDFK---QLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHN 161
Cdd:cd06651   63 LKNLQH-ERIVQYYGCLRDRAEKTLTIFMEYMPGGSVKdqlKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGAN 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 162 VMIDHEHrKLRLIDWG----LAEFYHPNQEYNVRVASRYFKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPFfhghD 237
Cdd:cd06651  142 ILRDSAG-NVKLGDFGaskrLQTICMSGTGIRSVTGTPYWMSPE-VISGEGYGRKADVWSLGCTVVEMLTEKPPW----A 215
                        170
                 ....*....|.
gi 528504250 238 NYDQLVRIAKV 248
Cdd:cd06651  216 EYEAMAAIFKI 226
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
37-237 3.35e-08

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: 54.07  E-value: 3.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGG--PNIITLLDIIKDpvSRTPALVFE 114
Cdd:cd14112    3 GRFSFGSEIFRGRFSVIVKAVDSTTETDAHCAVKIFEVSDEASEAVREFESLRTLqhENVQRLIAAFKP--SNFAYLVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 115 HVNNTDFKqlYQTLSDY----DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHR-KLRLIDWGLAEFYHPNQEYN 189
Cdd:cd14112   81 KLQEDVFT--RFSSNDYyseeQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSwQVKLVDFGRAQKVSKLGKVP 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 528504250 190 VRVaSRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHD 237
Cdd:cd14112  159 VDG-DTDWASPEFHNPETPITVQSDIWGLGVLTFCLLSGFHPFTSEYD 205
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
127-331 3.65e-08

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: 54.34  E-value: 3.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 127 TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGL-AEFYHPNQEYNVRVASRYFKGPELLVD 205
Cdd:cd06637  107 TLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLT-ENAEVKLVDFGVsAQLDRTVGRRNTFIGTPYWMAPEVIAC 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 206 YQ----MYDYSLDMWSLGcmlasmifrkepffhghdnydqLVRIAKVLGTEDLYDYIDKYNIELDPRfnDILGRHSRKRW 281
Cdd:cd06637  186 DEnpdaTYDFKSDLWSLG----------------------ITAIEMAEGAPPLCDMHPMRALFLIPR--NPAPRLKSKKW 241
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 528504250 282 ERFVHSenqhlvstealdFLDKLLRYDHQARLTAREAMDHsyfyPIVKDQ 331
Cdd:cd06637  242 SKKFQS------------FIESCLVKNHSQRPSTEQLMKH----PFIRDQ 275
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
39-232 3.88e-08

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: 53.84  E-value: 3.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVKilkpvkkkkikreikiLENLRGGPN------IITLLDIIKDPVSRTPALV 112
Cdd:cd14163    2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIK----------------IIDKSGGPEefiqrfLPRELQIVERLDHKNIIHV 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 113 FEHVNNTDFK--QLYQTLSDYDI---------------RFYMYEILKALDYCHSMGIMHRDVKPHNVMIdhEHRKLRLID 175
Cdd:cd14163   66 YEMLESADGKiyLVMELAEDGDVfdcvlhggplpehraKALFRQLVEAIRYCHGCGVAHRDLKCENALL--QGFTLKLTD 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528504250 176 WGLAEFYHPNQeynvRVASRYFKG------PELLVDYQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14163  144 FGFAKQLPKGG----RELSQTFCGstayaaPEVLQGVPHDSRKGDIWSMGVVLYVMLCAQLPF 202
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
92-222 3.91e-08

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: 53.71  E-value: 3.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250    92 PNIITLLDIIKDPvsRTPALVFEHVNNTDFKQLYQTLSDYDIRF-----YMYEILKALDYCHSMGIMHRDVKPHNVMIDH 166
Cdd:smart00221  61 PNIVKLLGVCTEE--EPLMIVMEYMPGGDLLDYLRKNRPKELSLsdllsFALQIARGMEYLESKNFIHRDLAARNCLVGE 138
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250   167 EHRkLRLIDWGLAEFYHPNQEYNVRVASRYFK--GPELLvDYQMYDYSLDMWSLGCML 222
Cdd:smart00221 139 NLV-VKISDFGLSRDLYDDDYYKVKGGKLPIRwmAPESL-KEGKFTSKSDVWSFGVLL 194
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
133-225 4.02e-08

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: 54.24  E-value: 4.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 133 IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGL-AEFYHPNQEYNVRVASRYFKGPELLVDYQ---- 207
Cdd:cd06636  123 IAYICREILRGLAHLHAHKVIHRDIKGQNVLLT-ENAEVKLVDFGVsAQLDRTVGRRNTFIGTPYWMAPEVIACDEnpda 201
                         90
                 ....*....|....*...
gi 528504250 208 MYDYSLDMWSLGCMLASM 225
Cdd:cd06636  202 TYDYRSDIWSLGITAIEM 219
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
134-339 4.15e-08

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: 54.63  E-value: 4.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGL---------AEFY----HPNQE-----------YN 189
Cdd:cd05626  104 RFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGH-IKLTDFGLctgfrwthnSKYYqkgsHIRQDsmepsdlwddvSN 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 190 VRVASRY------------------------FKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLvri 245
Cdd:cd05626  183 CRCGDRLktleqratkqhqrclahslvgtpnYIAPEVLLR-KGYTQLCDWWSVGVILFEMLVGQPPFLAPTPTETQL--- 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 246 aKVLGTEDLYDYIDKynIELDPRFNDILGRHSRKRWERFVHSENQHLVST---EALDFLDKLLRYDHQARLTAREAMDHS 322
Cdd:cd05626  259 -KVINWENTLHIPPQ--VKLSPEAVDLITKLCCSAEERLGRNGADDIKAHpffSEVDFSSDIRTQPAPYVPKISHPMDTS 335
                        250
                 ....*....|....*..
gi 528504250 323 YFYPIVKDQGRGAPAAG 339
Cdd:cd05626  336 NFDPVEEESPWNDASGD 352
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
36-247 4.36e-08

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: 53.97  E-value: 4.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  36 QDDYQLVRKLGRGKYSEVFEAINIT-NNEKVVVKILKPVKKKKIKREIKILE------NLRGgPNIITLLDIIKDPvsrt 108
Cdd:cd05056    5 REDITLGRCIGEGQFGDVYQGVYMSpENEKIAVAVKTCKNCTSPSVREKFLQeayimrQFDH-PHIVKLIGVITEN---- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 109 PA-LVFEHVNNTDFKQLYQT----LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYH 183
Cdd:cd05056   80 PVwIVMELAPLGELRSYLQVnkysLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPD-CVKLGDFGLSRYME 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 184 PNQEYNVRVASRYFK--GPElLVDYQMYDYSLDMWSLG-CMLASMIFRKEPfFHGHDNYDQLVRIAK 247
Cdd:cd05056  159 DESYYKASKGKLPIKwmAPE-SINFRRFTSASDVWMFGvCMWEILMLGVKP-FQGVKNNDVIGRIEN 223
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
90-321 4.70e-08

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: 54.00  E-value: 4.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  90 GGPNIITLLDIIK-------DPVSRTPAL-VFEHVNNTD-FKQLYQT--LSDYDIRFYMYEILKALDYCHSMGIMHRDVK 158
Cdd:cd14171   57 GHPNIVQIYDVYAnsvqfpgESSPRARLLiVMELMEGGElFDRISQHrhFTEKQAAQYTKQIALAVQHCHSLNIAHRDLK 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 159 PHNVMI--DHEHRKLRLIDWGLAEFyhPNQEYNVRVASRYFKGPELLVDYQ----------------MYDYSLDMWSLGC 220
Cdd:cd14171  137 PENLLLkdNSEDAPIKLCDFGFAKV--DQGDLMTPQFTPYYVAPQVLEAQRrhrkersgiptsptpyTYDKSCDMWSLGV 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 221 MLASMIFRKEPFF--HGHDNYDQLVRiAKVLGTEdlYDYidkynieldprfndilgrhSRKRWERfvhsenqhlVSTEAL 298
Cdd:cd14171  215 IIYIMLCGYPPFYseHPSRTITKDMK-RKIMTGS--YEF-------------------PEEEWSQ---------ISEMAK 263
                        250       260
                 ....*....|....*....|...
gi 528504250 299 DFLDKLLRYDHQARLTAREAMDH 321
Cdd:cd14171  264 DIVRKLLCVDPEERMTIEEVLHH 286
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
45-228 5.20e-08

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: 53.65  E-value: 5.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  45 LGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLLDI-IKDpvsRTPALVFEHVNNTDFKQ 123
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSFLKEVKLMRRLSHPNILRFIGVcVKD---NKLNFITEYVNGGTLEE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 124 LYQTLSD---YDIRFYM-YEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLI--DWGLAEF---YHPNQ-----EYN 189
Cdd:cd14065   78 LLKSMDEqlpWSQRVSLaKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAVvaDFGLAREmpdEKTKKpdrkkRLT 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528504250 190 VrVASRYFKGPELLvDYQMYDYSLDMWSLGCMLASMIFR 228
Cdd:cd14065  158 V-VGSPYWMAPEML-RGESYDEKVDVFSFGIVLCEIIGR 194
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
36-236 6.88e-08

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: 53.49  E-value: 6.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  36 QDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLR--GGPNIITLLDiikDPVSRTPALV- 112
Cdd:cd06646    8 QHDYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSLIQQEIFMVKecKHCNIVAYFG---SYLSREKLWIc 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 113 FEHVNNTDFKQLYQT---LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGL-AEFYHPNQEY 188
Cdd:cd06646   85 MEYCGGGSLQDIYHVtgpLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLT-DNGDVKLADFGVaAKITATIAKR 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 528504250 189 NVRVASRYFKGPELLVDYQM--YDYSLDMWSLGCMLASMIFRKEPFFHGH 236
Cdd:cd06646  164 KSFIGTPYWMAPEVAAVEKNggYNQLCDIWAVGITAIELAELQPPMFDLH 213
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
111-180 7.63e-08

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: 53.73  E-value: 7.63e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528504250 111 LVFEHVNNTDFKQLYQTLSDYD---IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAE 180
Cdd:cd05610   81 LVMEYLIGGDVKSLLHIYGYFDeemAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGH-IKLTDFGLSK 152
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
136-323 9.22e-08

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: 52.82  E-value: 9.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 136 YMYEILKALDYCHSMGIMHRDVKPHNVMIdHEHRKLRLIDWG--------LAEFYHPNQEYNVRvASRYFKGPElLVDYQ 207
Cdd:cd06631  108 YTKQILEGVAYLHNNNVIHRDIKGNNIML-MPNGVIKLIDFGcakrlcinLSSGSQSQLLKSMR-GTPYWMAPE-VINET 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 208 MYDYSLDMWSLGCMLASMIFRKEPFFHghdnydqLVRIAKV--LGTEDlydyidkyniELDPRFNDilgrhsrkrweRFv 285
Cdd:cd06631  185 GHGRKSDIWSIGCTVFEMATGKPPWAD-------MNPMAAIfaIGSGR----------KPVPRLPD-----------KF- 235
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 528504250 286 hsenqhlvSTEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd06631  236 --------SPEARDFVHACLTRDQDERPSAEQLLKHPF 265
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
92-242 1.02e-07

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: 52.69  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTpaLVFEHVNNTDFKQLYQTLSDY---DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIdHEH 168
Cdd:cd14183   64 PNIVLLIEEMDMPTELY--LVMELVKGGDLFDAITSTNKYterDASGMLYNLASAIKYLHSLNIVHRDIKPENLLV-YEH 140
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 169 ----RKLRLIDWGLAEFYHpNQEYNVrVASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQL 242
Cdd:cd14183  141 qdgsKSLKLGDFGLATVVD-GPLYTV-CGTPTYVAPEIIAE-TGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVL 215
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
92-232 1.03e-07

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: 52.77  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTPALV-FEHVNNTDFKQL----YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDh 166
Cdd:cd13979   59 ENIVRVLAAETGTDFASLGLIiMEYCGNGTLQQLiyegSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILIS- 137
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528504250 167 EHRKLRLIDWG-------LAEFYHPnqEYNVRVASRYfKGPELLVDYQMYDYSlDMWSLGCMLASMIFRKEPF 232
Cdd:cd13979  138 EQGVCKLCDFGcsvklgeGNEVGTP--RSHIGGTYTY-RAPELLKGERVTPKA-DIYSFGITLWQMLTRELPY 206
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
92-260 1.05e-07

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: 52.66  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDpvSRTPALVFEHVNNTDfkqLYQTLS--------DYDIRFYM-YEILKALDYCHSMG---IMHRDVKP 159
Cdd:cd14066   50 PNLVRLLGYCLE--SDEKLLVYEYMPNGS---LEDRLHchkgspplPWPQRLKIaKGIARGLEYLHEECpppIIHGDIKS 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 160 HNVMIDhEHRKLRLIDWGLAEFYHPNQEYNVRVASRY---FKGPELLVDYQMYDYSlDMWSLGCMLASMIFRKEPFFHGH 236
Cdd:cd14066  125 SNILLD-EDFEPKLTDFGLARLIPPSESVSKTSAVKGtigYLAPEYIRTGRVSTKS-DVYSFGVVLLELLTGKPAVDENR 202
                        170       180
                 ....*....|....*....|....*.
gi 528504250 237 DNYDQ--LVRIAKVLGTEDLYDYIDK 260
Cdd:cd14066  203 ENASRkdLVEWVESKGKEELEDILDK 228
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
138-324 1.10e-07

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: 52.83  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 138 YEILKALDYCHSM-GIMHRDVKPHNVMIDHeHRKLRLIDWGLA-EFYhpNQEYNVRVASRYFKGPELLvdyQMYDYSL-- 213
Cdd:cd06620  111 VAVLEGLTYLYNVhRIIHRDIKPSNILVNS-KGQIKLCDFGVSgELI--NSIADTFVGTSTYMSPERI---QGGKYSVks 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 214 DMWSLGCMLASMIFRKEPFFHGHDNYDQLVriakvlGTEDLYDYIDKYNIELDPRFndilgrhsrkrwerfvhsENQHLV 293
Cdd:cd06620  185 DVWSLGLSIIELALGEFPFAGSNDDDDGYN------GPMGILDLLQRIVNEPPPRL------------------PKDRIF 240
                        170       180       190
                 ....*....|....*....|....*....|.
gi 528504250 294 STEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd06620  241 PKDLRDFVDRCLLKDPRERPSPQLLLDHDPF 271
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
139-230 1.12e-07

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: 52.51  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIdHEHRKLRLIDWGLAEFY----------------------HPNQEYNVrVASRY 196
Cdd:cd14154   99 DIASGMAYLHSMNIIHRDLNSHNCLV-REDKTVVVADFGLARLIveerlpsgnmspsetlrhlkspDRKKRYTV-VGNPY 176
                         90       100       110
                 ....*....|....*....|....*....|....
gi 528504250 197 FKGPELLvDYQMYDYSLDMWSLGCMLASMIFRKE 230
Cdd:cd14154  177 WMAPEML-NGRSYDEKVDIFSFGIVLCEIIGRVE 209
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
138-227 1.22e-07

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: 52.49  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 138 YEILKALDYCHSMGIMHRDVKPHNVMIDHEhRKLRLIDWGL-AEFYHPNQEYNVRVASRYFkGPElLVDYQMYDYSLDMW 216
Cdd:cd14047  124 EQITKGVEYIHSKKLIHRDLKPSNIFLVDT-GKVKIGDFGLvTSLKNDGKRTKSKGTLSYM-SPE-QISSQDYGKEVDIY 200
                         90
                 ....*....|.
gi 528504250 217 SLGCMLASMIF 227
Cdd:cd14047  201 ALGLILFELLH 211
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
138-323 1.31e-07

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: 52.76  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 138 YEILKALDYC-HSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLV--DYQMYDYSLD 214
Cdd:cd06618  121 VSIVKALHYLkEKHGVIHRDVKPSNILLD-ESGNVKLCDFGISGRLVDSKAKTRSAGCAAYMAPERIDppDNPKYDIRAD 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 215 MWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKvlgtEDLydyidkynIELDPRfndilgrhsrkrwERFvhsenqhlvS 294
Cdd:cd06618  200 VWSLGISLVELATGQFPYRNCKTEFEVLTKILN----EEP--------PSLPPN-------------EGF---------S 245
                        170       180
                 ....*....|....*....|....*....
gi 528504250 295 TEALDFLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd06618  246 PDFCSFVDLCLTKDHRYRPKYRELLQHPF 274
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
85-225 1.92e-07

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 52.24  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  85 LENLRGGPNIITLLDIIKD---PVSRTPALVFE----HVNNTDFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDV 157
Cdd:cd14020   57 LEQLQGHRNIVTLYGVFTNhysANVPSRCLLLElldvSVSELLLRSSNQGCSMWMIQHCARDVLEALAFLHHEGYVHADL 136
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 158 KPHNVMIDHEHRKLRLIDWGLAeFYHPNQEYNVrVASRYFKGPELLVDYQMYDYSL----------DMWSLGCMLASM 225
Cdd:cd14020  137 KPRNILWSAEDECFKLIDFGLS-FKEGNQDVKY-IQTDGYRAPEAELQNCLAQAGLqsetectsavDLWSLGIVLLEM 212
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
92-232 1.95e-07

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: 51.69  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRtpALVFEHVNNTD-FKQLYQT--LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMID-HE 167
Cdd:cd14662   56 PNIIRFKEVVLTPTHL--AIVMEYAAGGElFERICNAgrFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDgSP 133
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 168 HRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDYQmYDYSL-DMWSLGCMLASMIFRKEPF 232
Cdd:cd14662  134 APRLKICDFGYSKSSVLHSQPKSTVGTPAYIAPEVLSRKE-YDGKVaDVWSCGVTLYVMLVGAYPF 198
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
92-232 2.29e-07

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: 51.46  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTPALVFEHVNNTDFKQLYQTLSDYD---IRFYMYEILKALDYCHSMG--IMHRDVKPHNVMIDH 166
Cdd:cd13983   60 PNIIKFYDSWESKSKKEVIFITELMTSGTLKQYLKRFKRLKlkvIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFING 139
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 167 EHRKLRLIDWGLAEFYHPNQEYNVrVASRYFKGPELlvdYQ-MYDYSLDMWSLG-CMLaSMIFRKEPF 232
Cdd:cd13983  140 NTGEVKIGDLGLATLLRQSFAKSV-IGTPEFMAPEM---YEeHYDEKVDIYAFGmCLL-EMATGEYPY 202
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
139-280 2.53e-07

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: 51.66  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIdhEHRKLRLIDWGLAEFYHPNQEYNVRVA-SRYFKGPELLvDYQMYDYSLDMWS 217
Cdd:cd08222  114 QLLLAVQYMHERRILHRDLKAKNIFL--KNNVIKVGDFGISRILMGTSDLATTFTgTPYYMSPEVL-KHEGYNSKSDIWS 190
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528504250 218 LGCMLASMIFRKepffHGHDNYDQLVRIAKVLgTEDLYDYIDKYNIELDPRFNDILGRHSRKR 280
Cdd:cd08222  191 LGCILYEMCCLK----HAFDGQNLLSVMYKIV-EGETPSLPDKYSKELNAIYSRMLNKDPALR 248
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
128-324 2.72e-07

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 51.40  E-value: 2.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPNQEYNVRVAsrYFKgPELLVDyQ 207
Cdd:PHA03390 106 LSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDRIYLCDYGLCKIIGTPSCYDGTLD--YFS-PEKIKG-H 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 208 MYDYSLDMWSLGCMLASMIFRKEPFFHGHDNydqlvriakvlgtedlydyidkyniELDPrfNDILGRHSRKrwerFVHS 287
Cdd:PHA03390 182 NYDVSFDWWAVGVLTYELLTGKHPFKEDEDE-------------------------ELDL--ESLLKRQQKK----LPFI 230
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 528504250 288 ENqhlVSTEALDFLDKLLRYDHQARLTA-REAMDHSYF 324
Cdd:PHA03390 231 KN---VSKNANDFVQSMLKYNINYRLTNyNEIIKHPFL 265
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
139-228 2.81e-07

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: 51.50  E-value: 2.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIdHEHRKLRLIDWGLA-----EFYHPNQEYNVRVASR----------YFKGPElL 203
Cdd:cd14221   99 DIASGMAYLHSMNIIHRDLNSHNCLV-RENKSVVVADFGLArlmvdEKTQPEGLRSLKKPDRkkrytvvgnpYWMAPE-M 176
                         90       100
                 ....*....|....*....|....*
gi 528504250 204 VDYQMYDYSLDMWSLGCMLASMIFR 228
Cdd:cd14221  177 INGRSYDEKVDVFSFGIVLCEIIGR 201
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
110-199 3.02e-07

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 49.57  E-value: 3.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 110 ALVFEHVNNTDFKQLYQTLSDYDIrfYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEhrKLRLIDWGLAEFYHPN--QE 187
Cdd:COG3642   32 DLVMEYIEGETLADLLEEGELPPE--LLRELGRLLARLHRAGIVHGDLTTSNILVDDG--GVYLIDFGLARYSDPLedKA 107
                         90
                 ....*....|..
gi 528504250 188 YNVRVASRYFKG 199
Cdd:COG3642  108 VDLAVLKRSLES 119
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
138-236 3.06e-07

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: 51.46  E-value: 3.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 138 YEILKALDYCHSMGIMHRDVKPHNVMI----DHEHRKLRLIDWGLAEFYHPNQEYNVRvASRYFKGPELLVDYQMYDYSL 213
Cdd:cd14000  119 LQVADGLRYLHSAMIIYRDLKSHNVLVwtlyPNSAIIIKIADYGISRQCCRMGAKGSE-GTPGFRAPEIARGNVIYNEKV 197
                         90       100
                 ....*....|....*....|...
gi 528504250 214 DMWSLGCMLASMIFRKEPFFHGH 236
Cdd:cd14000  198 DVFSFGMLLYEILSGGAPMVGHL 220
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
140-232 3.07e-07

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: 51.65  E-value: 3.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 140 ILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLA-EFYhpNQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSL 218
Cdd:cd06621  114 VLKGLSYLHSRKIIHRDIKPSNILLTRKG-QVKLCDFGVSgELV--NSLAGTFTGTSYYMAPERIQG-GPYSITSDVWSL 189
                         90
                 ....*....|....
gi 528504250 219 GCMLASMIFRKEPF 232
Cdd:cd06621  190 GLTLLEVAQNRFPF 203
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
143-235 3.63e-07

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: 50.96  E-value: 3.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 143 ALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEY-NVRVASRYFKGPELlVDYQMYDYSLDMWSLGCM 221
Cdd:cd08218  113 ALKHVHDRKILHRDIKSQNIFLT-KDGIIKLGDFGIARVLNSTVELaRTCIGTPYYLSPEI-CENKPYNNKSDIWALGCV 190
                         90
                 ....*....|....
gi 528504250 222 LASMIFRKEPFFHG 235
Cdd:cd08218  191 LYEMCTLKHAFEAG 204
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
138-232 3.69e-07

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: 51.36  E-value: 3.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 138 YEILKALDYCH--SMGIMHRDVKPHNVMIDHEhRKLRLIDWGLA--EFYHPNQEYNV-----------RVASRYFKGPEL 202
Cdd:cd14036  115 YQTCRAVQHMHkqSPPIIHRDLKIENLLIGNQ-GQIKLCDFGSAttEAHYPDYSWSAqkrslvedeitRNTTPMYRTPEM 193
                         90       100       110
                 ....*....|....*....|....*....|..
gi 528504250 203 LVDYQMYDYS--LDMWSLGCMLASMIFRKEPF 232
Cdd:cd14036  194 IDLYSNYPIGekQDIWALGCILYLLCFRKHPF 225
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
39-323 3.99e-07

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: 51.17  E-value: 3.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILEN-LR--------GGPNIITLLDiikdpvsrtp 109
Cdd:cd13990    2 YLLLNLLGKGGFSEVYKAFDLVEQRYVACKIHQLNKDWSEEKKQNYIKHaLReyeihkslDHPRIVKLYD---------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 110 alVFEHVNNT-------------DF--KQlYQTLSDYDIRFYMYEILKALDYC--HSMGIMHRDVKPHNVMIDH--EHRK 170
Cdd:cd13990   72 --VFEIDTDSfctvleycdgndlDFylKQ-HKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSgnVSGE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 171 LRLIDWGLA------EFYHPNQEYNVRVASRY-FKGPELLV---DYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYD 240
Cdd:cd13990  149 IKITDFGLSkimddeSYNSDGMELTSQGAGTYwYLPPECFVvgkTPPKISSKVDVWSVGVIFYQMLYGRKPFGHNQSQEA 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 241 QLvriakvlgtedlydyidKYNIELdprfndilgrHSRKrwerfVHSENQHLVSTEALDFLDKLLRYDHQARLTAREAMD 320
Cdd:cd13990  229 IL-----------------EENTIL----------KATE-----VEFPSKPVVSSEAKDFIRRCLTYRKEDRPDVLQLAN 276

                 ...
gi 528504250 321 HSY 323
Cdd:cd13990  277 DPY 279
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
36-236 4.22e-07

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: 50.81  E-value: 4.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  36 QDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRG--GPNIITLLD--IIKDPVsrtpAL 111
Cdd:cd06645   10 QEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDckHSNIVAYFGsyLRRDKL----WI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 VFEHVNNTDFKQLYQT---LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMI-DHEHrkLRLIDWGL-AEFYHPNQ 186
Cdd:cd06645   86 CMEFCGGGSLQDIYHVtgpLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLtDNGH--VKLADFGVsAQITATIA 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528504250 187 EYNVRVASRYFKGPELLVDYQM--YDYSLDMWSLGCMLASMIFRKEPFFHGH 236
Cdd:cd06645  164 KRKSFIGTPYWMAPEVAAVERKggYNQLCDIWAVGITAIELAELQPPMFDLH 215
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
115-226 4.58e-07

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: 51.08  E-value: 4.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 115 HVNNTDFKQLYQtlsdydirfYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHPNQEYNV---- 190
Cdd:cd05079  102 NKNKINLKQQLK---------YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQ-VKIGDFGLTKAIETDKEYYTvkdd 171
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 528504250 191 RVASRYFKGPELLVDYQMYDYSlDMWSLGCMLASMI 226
Cdd:cd05079  172 LDSPVFWYAPECLIQSKFYIAS-DVWSFGVTLYELL 206
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
136-232 4.95e-07

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: 50.74  E-value: 4.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 136 YMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFY-HPNQEYNVRVASRYFKGPELLVDYQmYDYSLD 214
Cdd:cd08219  105 WFVQMCLGVQHIHEKRVLHRDIKSKNIFLT-QNGKVKLGDFGSARLLtSPGAYACTYVGTPYYVPPEIWENMP-YNNKSD 182
                         90
                 ....*....|....*...
gi 528504250 215 MWSLGCMLASMIFRKEPF 232
Cdd:cd08219  183 IWSLGCILYELCTLKHPF 200
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
134-324 5.41e-07

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: 50.76  E-value: 5.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLA-EFYHPNQEYNVRVASRYFKGPELLVDyQMYDYS 212
Cdd:cd05589  104 VFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY-VKIADFGLCkEGMGFGDRTSTFCGTPEFLAPEVLTD-TSYTRA 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 213 LDMWSLGCMLASMIFRKEPFfHGHDNydqlvriakvlgtEDLYDYIdkynieldprFNDILgrhsrkRWERFVhsenqhl 292
Cdd:cd05589  182 VDWWGLGVLIYEMLVGESPF-PGDDE-------------EEVFDSI----------VNDEV------RYPRFL------- 224
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 528504250 293 vSTEALDFLDKLLRYDHQARLTA--REAMD---HSYF 324
Cdd:cd05589  225 -STEAISIMRRLLRKNPERRLGAseRDAEDvkkQPFF 260
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
93-324 6.01e-07

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: 50.04  E-value: 6.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIkdpVSRTPALVFEHVNNTDFKQLYQT---LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHR 169
Cdd:cd14022   46 NINQITEII---LGETKAYVFFERSYGDMHSFVRTckkLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEER 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 170 KLRLIDwGLAEFY---HPNQEYNVRVASRYFKGPELLVDYQMYD-YSLDMWSLGCMLASMIFRKEPFfhgHDnydqlvri 245
Cdd:cd14022  123 TRVKLE-SLEDAYilrGHDDSLSDKHGCPAYVSPEILNTSGSYSgKAADVWSLGVMLYTMLVGRYPF---HD-------- 190
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528504250 246 akvlgtedlydyidkynIELDPRFNDIlgrhsrkrweRFVHSENQHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14022  191 -----------------IEPSSLFSKI----------RRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPWF 242
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
139-232 7.35e-07

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: 50.13  E-value: 7.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEY-NVRVASRYFKGPELLVDyQMYDYSLDMWS 217
Cdd:cd08223  110 QIAMALQYMHERNILHRDLKTQNIFLT-KSNIIKVGDLGIARVLESSSDMaTTLIGTPYYMSPELFSN-KPYNHKSDVWA 187
                         90
                 ....*....|....*
gi 528504250 218 LGCMLASMIFRKEPF 232
Cdd:cd08223  188 LGCCVYEMATLKHAF 202
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
92-226 9.31e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 50.26  E-value: 9.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLldiiKDPVSRTPA--LVFEHVNNtdfkQLYQTLSDYDIRFYM-------YEILKALDYCHSMGIMHRDVKPHNV 162
Cdd:PHA03209 117 PSVIRM----KDTLVSGAItcMVLPHYSS----DLYTYLTKRSRPLPIdqaliieKQILEGLRYLHAQRIIHRDVKTENI 188
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528504250 163 MIDHEHrKLRLIDWGLAEFyhpnqeynvRVASRYFKG---------PELLVDYQmYDYSLDMWSLGCMLASMI 226
Cdd:PHA03209 189 FINDVD-QVCIGDLGAAQF---------PVVAPAFLGlagtvetnaPEVLARDK-YNSKADIWSAGIVLFEML 250
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
124-243 1.00e-06

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: 50.03  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 124 LYQTLSDYDIRFYMYEIL-------KALDYCHSMGIMHRDVKPHNVMIdHEHRKLRLIDWGLAEF---YHPNQEYNVRVA 193
Cdd:cd14149   94 LYKHLHVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFL-HEGLTVKIGDFGLATVksrWSGSQQVEQPTG 172
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528504250 194 SRYFKGPEL--LVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHgHDNYDQLV 243
Cdd:cd14149  173 SILWMAPEVirMQDNNPFSFQSDVYSYGIVLYELMTGELPYSH-INNRDQII 223
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
107-232 1.21e-06

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: 50.06  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 107 RTPALVFEHVNNTDFKQLY---QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGL----- 178
Cdd:cd05627   75 RNLYLIMEFLPGGDMMTLLmkkDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGH-VKLSDFGLctglk 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 179 ----AEFY-----HPNQEYNVR----------------------VASRYFKGPELLVDyQMYDYSLDMWSLGCMLASMIF 227
Cdd:cd05627  154 kahrTEFYrnlthNPPSDFSFQnmnskrkaetwkknrrqlaystVGTPDYIAPEVFMQ-TGYNKLCDWWSLGVIMYEMLI 232

                 ....*
gi 528504250 228 RKEPF 232
Cdd:cd05627  233 GYPPF 237
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
92-232 1.27e-06

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: 49.66  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDI-IKDPvsrTPALVFEHVNNTDFKQLY-------QTLSDYDIrfymyEILKALDYCHSMGI---MHRDVKPH 160
Cdd:cd14145   65 PNIIALRGVcLKEP---NLCLVMEFARGGPLNRVLsgkrippDILVNWAV-----QIARGMNYLHCEAIvpvIHRDLKSS 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 161 NVMI-------DHEHRKLRLIDWGLAEFYHpnQEYNVRVASRY-FKGPElLVDYQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14145  137 NILIlekvengDLSNKILKITDFGLAREWH--RTTKMSAAGTYaWMAPE-VIRSSMFSKGSDVWSYGVLLWELLTGEVPF 213
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
133-247 1.31e-06

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 49.56  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 133 IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLrLIDWGLAEFYHPNQEYnvrvaSRYFKGPELLVDYQMYDYS 212
Cdd:PHA02882 128 IKNIMKDMLTTLEYIHEHGISHGDIKPENIMVDGNNRGY-IIDYGIASHFIIHGKH-----IEYSKEQKDLHRGTLYYAG 201
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 528504250 213 L------------DMWSLG-CMLaSMIFRKEPfFHGHDNYDQLVRIAK 247
Cdd:PHA02882 202 LdahngacvtrrgDLESLGyCML-KWAGIKLP-WKGFGHNGNLIHAAK 247
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
126-222 1.94e-06

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 49.24  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 126 QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEY----NVRVASRYFkGPE 201
Cdd:cd05098  130 EQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVT-EDNVMKIADFGLARDIHHIDYYkkttNGRLPVKWM-APE 207
                         90       100
                 ....*....|....*....|.
gi 528504250 202 LLVDyQMYDYSLDMWSLGCML 222
Cdd:cd05098  208 ALFD-RIYTHQSDVWSFGVLL 227
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
124-243 2.16e-06

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: 48.86  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 124 LYQTLSDYDIRFYMYEIL-------KALDYCHSMGIMHRDVKPHNVMIdHEHRKLRLIDWGLAEF---YHPNQEYNVRVA 193
Cdd:cd14150   82 LYRHLHVTETRFDTMQLIdvarqtaQGMDYLHAKNIIHRDLKSNNIFL-HEGLTVKIGDFGLATVktrWSGSQQVEQPSG 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528504250 194 SRYFKGPEL--LVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHgHDNYDQLV 243
Cdd:cd14150  161 SILWMAPEVirMQDTNPYSFQSDVYAYGVVLYELMSGTLPYSN-INNRDQII 211
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
140-233 2.39e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 49.07  E-value: 2.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 140 ILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLA--EFYHPN--QEYNvRVASRYFKGPELLVdYQMYDYSLDM 215
Cdd:PHA03207 194 LLEALAYLHGRGIIHRDVKTENIFLD-EPENAVLGDFGAAckLDAHPDtpQCYG-WSGTLETNSPELLA-LDPYCAKTDI 270
                         90
                 ....*....|....*...
gi 528504250 216 WSLGCMLASMIFRKEPFF 233
Cdd:PHA03207 271 WSAGLVLFEMSVKNVTLF 288
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
133-251 2.60e-06

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: 48.74  E-value: 2.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 133 IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEhRKLRLIDWGLAEFYHPNQEYnVRVASR-----YFKGPELLVDYQ 207
Cdd:cd05080  109 LLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDND-RLVKIGDFGLAKAVPEGHEY-YRVREDgdspvFWYAPECLKEYK 186
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 528504250 208 MYdYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGT 251
Cdd:cd05080  187 FY-YASDVWSFGVTLYELLTHCDSSQSPPTKFLEMIGIAQGQMT 229
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
127-232 2.75e-06

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: 48.88  E-value: 2.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 127 TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGL---------AEFYH------PN----QE 187
Cdd:cd05628   97 TLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGH-VKLSDFGLctglkkahrTEFYRnlnhslPSdftfQN 175
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528504250 188 YNVRVASRYFK-----------------GPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd05628  176 MNSKRKAETWKrnrrqlafstvgtpdyiAPEVFMQ-TGYNKLCDWWSLGVIMYEMLIGYPPF 236
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
124-243 3.21e-06

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: 48.16  E-value: 3.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 124 LYQTLSDYDIRFYMYEIL-------KALDYCHSMGIMHRDVKPHNVMIdHEHRKLRLIDWGLAEF---YHPNQEYNVRVA 193
Cdd:cd14062   75 LYKHLHVLETKFEMLQLIdiarqtaQGMDYLHAKNIIHRDLKSNNIFL-HEDLTVKIGDFGLATVktrWSGSQQFEQPTG 153
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528504250 194 SRYFKGPEL--LVDYQMYDYSLDMWSLGCMLASMIFRKEPfFHGHDNYDQLV 243
Cdd:cd14062  154 SILWMAPEVirMQDENPYSFQSDVYAFGIVLYELLTGQLP-YSHINNRDQIL 204
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
40-222 3.29e-06

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 47.91  E-value: 3.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250    40 QLVRKLGRGKYSEVFEAINITNNEKVVV--------KILKPVKKKKIKREIKILENLRgGPNIITLLDII--KDPvsrtP 109
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKLKGKGGKKKVevavktlkEDASEQQIEEFLREARIMRKLD-HPNVVKLLGVCteEEP----L 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250   110 ALVFEHVNNTDFKQLYQ----TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHPN 185
Cdd:smart00219  77 YIVMEYMEGGDLLSYLRknrpKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLV-VKISDFGLSRDLYDD 155
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 528504250   186 QEYNVRVASRYFK--GPELLvDYQMYDYSLDMWSLGCML 222
Cdd:smart00219 156 DYYRKRGGKLPIRwmAPESL-KEGKFTSKSDVWSFGVLL 193
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
105-267 3.36e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 48.92  E-value: 3.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 105 VSRTPALVFEHVNNTDFkQLYQTLSDYDI-----------RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRL 173
Cdd:PHA03210 231 ILRSEANTYMITQKYDF-DLYSFMYDEAFdwkdrpllkqtRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDG-KIVL 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 174 IDWGLAEFYHpnqeyNVRVASRY-------FKGPELLVDyQMYDYSLDMWSLGCMLASMIfRKE--PFFHGHDN-YDQLV 243
Cdd:PHA03210 309 GDFGTAMPFE-----KEREAFDYgwvgtvaTNSPEILAG-DGYCEITDIWSCGLILLDML-SHDfcPIGDGGGKpGKQLL 381
                        170       180       190
                 ....*....|....*....|....*....|...
gi 528504250 244 RIAKVLGTED---------LYDYIDKYNIELDP 267
Cdd:PHA03210 382 KIIDSLSVCDeefpdppckLFDYIDSAEIDHAG 414
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
126-222 3.45e-06

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They 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, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. 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. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR 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: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 48.18  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 126 QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYHPNQEYNVRVASRY---FKGPEL 202
Cdd:cd05053  128 EQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVTEDN-VMKIADFGLARDIHHIDYYRKTTNGRLpvkWMAPEA 206
                         90       100
                 ....*....|....*....|
gi 528504250 203 LVDyQMYDYSLDMWSLGCML 222
Cdd:cd05053  207 LFD-RVYTHQSDVWSFGVLL 225
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
139-232 3.63e-06

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 48.67  E-value: 3.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWG----LAEFYHPnqeYNVRVASRYFKGPELL---VDYQMYD- 210
Cdd:PLN00034 176 QILSGIAYLHRRHIVHRDIKPSNLLIN-SAKNVKIADFGvsriLAQTMDP---CNSSVGTIAYMSPERIntdLNHGAYDg 251
                         90       100
                 ....*....|....*....|..
gi 528504250 211 YSLDMWSLGCMLASMIFRKEPF 232
Cdd:PLN00034 252 YAGDIWSLGVSILEFYLGRFPF 273
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
85-232 3.80e-06

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: 48.05  E-value: 3.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  85 LENLRGGPNIITLLDiikDPVSRTPALVFE-----------HVNNTDFKQLYQTLSDYDIRFYMYEILKALDYCHSMG-- 151
Cdd:cd14037   54 MKRLSGHKNIVGYID---SSANRSGNGVYEvlllmeyckggGVIDLMNQRLQTGLTESEILKIFCDVCEAVAAMHYLKpp 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 152 IMHRDVKPHNVMIDHEhRKLRLIDWGLA--EFYHPNQEYNVRVA----SRY----FKGPELLVDY--QMYDYSLDMWSLG 219
Cdd:cd14037  131 LIHRDLKVENVLISDS-GNYKLCDFGSAttKILPPQTKQGVTYVeediKKYttlqYRAPEMIDLYrgKPITEKSDIWALG 209
                        170
                 ....*....|...
gi 528504250 220 CMLASMIFRKEPF 232
Cdd:cd14037  210 CLLYKLCFYTTPF 222
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
37-341 3.99e-06

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: 48.13  E-value: 3.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  37 DDYQLVRKLGRGKYSEVFEAINITNNEKVVVK---------ILKPVKKKKIKREIKILENLRGGPNIITLLDIIK-DPVS 106
Cdd:cd14041    6 DRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKihqlnknwrDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 107 RTPALVFEHVNNTDF--KQlYQTLSDYDIRFYMYEILKALDYCHSMG--IMHRDVKPHNVMIDHEHR--KLRLIDWGLAE 180
Cdd:cd14041   86 FCTVLEYCEGNDLDFylKQ-HKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTAcgEIKITDFGLSK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 181 FYHPNQEYNVR--------VASRYFKGPELLV---DYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVL 249
Cdd:cd14041  165 IMDDDSYNSVDgmeltsqgAGTYWYLPPECFVvgkEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTILK 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 250 GTEdlydyidkynIELDPRfndilgrhsrkrwerfvhsenqHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYFYPIVK 329
Cdd:cd14041  245 ATE----------VQFPPK----------------------PVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIR 292
                        330
                 ....*....|..
gi 528504250 330 DQGRGAPAAGMA 341
Cdd:cd14041  293 KSVSTSSPAGAA 304
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
128-233 4.23e-06

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 48.02  E-value: 4.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhehrklrliDWG---LAEF------YHPnqEYNVRVASRYFK 198
Cdd:cd13980   94 LNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVT---------SWNwvyLTDFasfkptYLP--EDNPADFSYFFD 162
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 199 ---------GPELLVDYQMYDY-----------SLDMWSLGCMLASMIFRKEPFF 233
Cdd:cd13980  163 tsrrrtcyiAPERFVDALTLDAeserrdgeltpAMDIFSLGCVIAELFTEGRPLF 217
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
133-324 5.22e-06

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: 47.67  E-value: 5.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 133 IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE-------HRKLRLID----WGLAEFYHPNQEYNvrvaSRYFKGPE 201
Cdd:cd08216  103 IAFILRDVLNALEYIHSKGYIHRSVKASHILISGDgkvvlsgLRYAYSMVkhgkRQRVVHDFPKSSEK----NLPWLSPE 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 202 LLV-DYQMYDYSLDMWSLG---CMLASMIfrkEPFFhghDNYDQLVRIAKVLGTedLYDYIDKYNIeldPRFNDILGRHS 277
Cdd:cd08216  179 VLQqNLLGYNEKSDIYSVGitaCELANGV---VPFS---DMPATQMLLEKVRGT--TPQLLDCSTY---PLEEDSMSQSE 247
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528504250 278 RKRWERFVHSENQHLVSTEAL-----DFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd08216  248 DSSTEHPNNRDTRDIPYQRTFseafhQFVELCLQRDPELRPSASQLLAHSFF 299
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
124-243 5.37e-06

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: 47.75  E-value: 5.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 124 LYQTLSDYDIRFYMYEIL-------KALDYCHSMGIMHRDVKPHNVMIdHEHRKLRLIDWGLAEF---YHPNQEYNVRVA 193
Cdd:cd14151   90 LYHHLHIIETKFEMIKLIdiarqtaQGMDYLHAKSIIHRDLKSNNIFL-HEDLTVKIGDFGLATVksrWSGSHQFEQLSG 168
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528504250 194 SRYFKGPEL--LVDYQMYDYSLDMWSLGCMLASMIFRKEPfFHGHDNYDQLV 243
Cdd:cd14151  169 SILWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQLP-YSNINNRDQII 219
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
134-227 7.40e-06

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: 47.18  E-value: 7.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 134 RFYMYEILK----ALDYCHSMGIMHRDVKPHNVMIDHEhRKLRLIDWGLAEfyHPNQ---EYNV------------RVAS 194
Cdd:cd14048  117 LFVCLNIFKqiasAVEYLHSKGLIHRDLKPSNVFFSLD-DVVKVGDFGLVT--AMDQgepEQTVltpmpayakhtgQVGT 193
                         90       100       110
                 ....*....|....*....|....*....|...
gi 528504250 195 RYFKGPELLvDYQMYDYSLDMWSLGCMLASMIF 227
Cdd:cd14048  194 RLYMSPEQI-HGNQYSEKVDIFALGLILFELIY 225
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
94-179 7.76e-06

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-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: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 47.10  E-value: 7.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  94 IITLLDIIKDPVsrtpALVFEHVNNTDFKQLYQTLS-DYDIRFYM-YEILKALDYCHSMG--IMHRDVKPHNVMID-HEH 168
Cdd:cd14025   57 ILPVYGICSEPV----GLVMEYMETGSLEKLLASEPlPWELRFRIiHETAVGMNFLHCMKppLLHLDLKPANILLDaHYH 132
                         90
                 ....*....|.
gi 528504250 169 RKLRliDWGLA 179
Cdd:cd14025  133 VKIS--DFGLA 141
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
128-224 9.78e-06

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. 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. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. 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. The STRAD alpha 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: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 47.24  E-value: 9.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHR--------KLRLIDWGL-AEFYHPNQEYNVRVASryFK 198
Cdd:cd08227   98 MSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKvylsglrsNLSMINHGQrLRVVHDFPKYSVKVLP--WL 175
                         90       100       110
                 ....*....|....*....|....*....|
gi 528504250 199 GPELL-VDYQMYDYSLDMWSLG---CMLAS 224
Cdd:cd08227  176 SPEVLqQNLQGYDAKSDIYSVGitaCELAN 205
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
128-225 9.82e-06

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: 46.54  E-value: 9.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIdhEHRKLRLIDWGLA-----EFYHPNqeyNVRvASRYFKGPEL 202
Cdd:cd13995   93 MREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVF--MSTKAVLVDFGLSvqmteDVYVPK---DLR-GTEIYMSPEV 166
                         90       100
                 ....*....|....*....|...
gi 528504250 203 LVdYQMYDYSLDMWSLGCMLASM 225
Cdd:cd13995  167 IL-CRGHNTKADIYSLGATIIHM 188
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
120-222 1.07e-05

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 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: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 46.92  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 120 DFKQLYQT-LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEY----NVRVAS 194
Cdd:cd14207  168 DSGDFYKRpLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLS-ENNVVKICDFGLARDIYKNPDYvrkgDARLPL 246
                         90       100
                 ....*....|....*....|....*...
gi 528504250 195 RYFkGPELLVDyQMYDYSLDMWSLGCML 222
Cdd:cd14207  247 KWM-APESIFD-KIYSTKSDVWSYGVLL 272
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
133-335 1.08e-05

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. 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. The STRAD-beta 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: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 46.79  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 133 IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE--------HRKLRLIDWG-LAEFYHPNQEYNVRVASryFKGPELL 203
Cdd:cd08226  103 IGNILYGAIKALNYLHQNGCIHRSVKASHILISGDglvslsglSHLYSMVTNGqRSKVVYDFPQFSTSVLP--WLSPELL 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 204 -VDYQMYDYSLDMWSLG---CMLASmifRKEPFfhgHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHS-- 277
Cdd:cd08226  181 rQDLHGYNVKSDIYSVGitaCELAR---GQVPF---QDMRRTQMLLQKLKGPPYSPLDIFPFPELESRMKNSQSGMDSgi 254
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 278 -----RKRWERFVHSENQHLVSTEAL-----DFLDKLLRYDHQARLTAREAMDHSYFYPiVKDQGRGA 335
Cdd:cd08226  255 gesvaTSSMTRTMTSERLQTPSSKTFspafhNLVELCLQQDPEKRPSASSLLSHSFFKQ-VKEQTQAS 321
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
138-225 1.09e-05

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: 46.66  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 138 YEILKALDYC---HSmgIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHpNQEYNVRVASRYFKGPELLVDYQmYDYSLD 214
Cdd:cd06615  106 IAVLRGLTYLrekHK--IMHRDVKPSNILVN-SRGEIKLCDFGVSGQLI-DSMANSFVGTRSYMSPERLQGTH-YTVQSD 180
                         90
                 ....*....|.
gi 528504250 215 MWSLGCMLASM 225
Cdd:cd06615  181 IWSLGLSLVEM 191
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
135-227 1.14e-05

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 46.58  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 135 FYMYEILKALDYCHSMGIMHRDVKPHNVMI--------------DHEHRKLRLIDWGLA---EFYHPNQEYNVRVASRYF 197
Cdd:cd13981  110 FFTIELLKVVEALHEVGIIHGDIKPDNFLLrleicadwpgegenGWLSKGLKLIDFGRSidmSLFPKNQSFKADWHTDSF 189
                         90       100       110
                 ....*....|....*....|....*....|
gi 528504250 198 KGPELLvDYQMYDYSLDMWSLGCMLASMIF 227
Cdd:cd13981  190 DCIEMR-EGRPWTYQIDYFGIAATIHVMLF 218
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
128-219 1.36e-05

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: 46.15  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGL-----AEFYHPNQEYNvrvaSRYFkGPEL 202
Cdd:cd14050   97 LPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGV-CKLGDFGLvveldKEDIHDAQEGD----PRYM-APEL 170
                         90
                 ....*....|....*..
gi 528504250 203 LvdYQMYDYSLDMWSLG 219
Cdd:cd14050  171 L--QGSFTKAADIFSLG 185
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
140-323 1.39e-05

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: 46.41  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 140 ILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEfYHPNQEYNVRVASRYFKGPELLVDYQmYDYSLDMWSLG 219
Cdd:cd06619  104 VVKGLTYLWSLKILHRDVKPSNMLVN-TRGQVKLCDFGVST-QLVNSIAKTYVGTNAYMAPERISGEQ-YGIHSDVWSLG 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 220 CMLASMIFRKEPFFHGHDNYDQLVRIakvlgtEDLYDYIDkyniELDPRFNDilGRHSrkrwERFVHsenqhlvsteald 299
Cdd:cd06619  181 ISFMELALGRFPYPQIQKNQGSLMPL------QLLQCIVD----EDPPVLPV--GQFS----EKFVH------------- 231
                        170       180
                 ....*....|....*....|....
gi 528504250 300 FLDKLLRYDHQARLTAREAMDHSY 323
Cdd:cd06619  232 FITQCMRKQPKERPAPENLMDHPF 255
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
126-222 1.48e-05

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: 46.55  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 126 QTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHpNQEY-----NVRVASRYFkGP 200
Cdd:cd05100  129 EQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT-EDNVMKIADFGLARDVH-NIDYykkttNGRLPVKWM-AP 205
                         90       100
                 ....*....|....*....|..
gi 528504250 201 ELLVDyQMYDYSLDMWSLGCML 222
Cdd:cd05100  206 EALFD-RVYTHQSDVWSFGVLL 226
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
132-226 1.59e-05

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: 46.11  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 132 DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIdHEHRKLRLIDWGLAEFYHPNQEYNVRVASRY---FKGPELLVDYqM 208
Cdd:cd05045  128 DLISFAWQISRGMQYLAEMKLVHRDLAARNVLV-AEGRKMKISDFGLSRDVYEEDSYVKRSKGRIpvkWMAIESLFDH-I 205
                         90
                 ....*....|....*...
gi 528504250 209 YDYSLDMWSLGCMLASMI 226
Cdd:cd05045  206 YTTQSDVWSFGVLLWEIV 223
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
139-232 1.63e-05

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: 46.13  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHS---MGIMHRDVKPHNVMI-------DHEHRKLRLIDWGLAEFYHPNQEynVRVASRY-FKGPElLVDYQ 207
Cdd:cd14148  100 QIARGMNYLHNeaiVPIIHRDLKSSNILIlepiendDLSGKTLKITDFGLAREWHKTTK--MSAAGTYaWMAPE-VIRLS 176
                         90       100
                 ....*....|....*....|....*
gi 528504250 208 MYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14148  177 LFSKSSDVWSFGVLLWELLTGEVPY 201
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
92-247 1.70e-05

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron 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: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 45.93  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPvSRTPALVFEHVNNTDFKQLYQTLSD----YDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhE 167
Cdd:cd05058   56 PNVLSLLGICLPS-EGSPLVVLPYMKHGDLRNFIRSETHnptvKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLD-E 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 168 HRKLRLIDWGLA------EFYHPNQEYNVRVASRYFKGPELlvDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQ 241
Cdd:cd05058  134 SFTVKVADFGLArdiydkEYYSVHNHTGAKLPVKWMALESL--QTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDI 211

                 ....*.
gi 528504250 242 LVRIAK 247
Cdd:cd05058  212 TVYLLQ 217
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
140-231 1.99e-05

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: 46.20  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 140 ILKALDYCHSM-GIMHRDVKPHNVMIDhEHRKLRLIDWGLAEfYHPNQEYNVRVASRYFKGPELLvdyQMYDYSL--DMW 216
Cdd:cd06650  112 VIKGLTYLREKhKIMHRDVKPSNILVN-SRGEIKLCDFGVSG-QLIDSMANSFVGTRSYMSPERL---QGTHYSVqsDIW 186
                         90
                 ....*....|....*
gi 528504250 217 SLGCMLASMIFRKEP 231
Cdd:cd06650  187 SMGLSLVEMAVGRYP 201
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
86-232 2.14e-05

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: 45.87  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  86 ENLRG--GPNIITLLD----IIKDpvSRTPALVFEHVNNTDFK---QLYQTLSDYDIRFYMYEILKALDYCHSMG--IMH 154
Cdd:cd14031   61 EMLKGlqHPNIVRFYDswesVLKG--KKCIVLVTELMTSGTLKtylKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIH 138
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 155 RDVKPHNVMIDHEHRKLRLIDWGLAEFYHPNQEYNVrVASRYFKGPELLVDYqmYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14031  139 RDLKCDNIFITGPTGSVKIGDLGLATLMRTSFAKSV-IGTPEFMAPEMYEEH--YDESVDVYAFGMCMLEMATSEYPY 213
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
138-222 2.34e-05

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: 45.73  E-value: 2.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 138 YEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEY----NVRVASRYFkGPELLVDyQMYDYSL 213
Cdd:cd05099  141 YQVARGMEYLESRRCIHRDLAARNVLVT-EDNVMKIADFGLARGVHDIDYYkktsNGRLPVKWM-APEALFD-RVYTHQS 217

                 ....*....
gi 528504250 214 DMWSLGCML 222
Cdd:cd05099  218 DVWSFGILM 226
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
114-222 2.36e-05

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 45.78  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 114 EHVNNTDFKQLYQtlsdydirfYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHPNQE-YNVRV 192
Cdd:cd14205  100 KHKERIDHIKLLQ---------YTSQICKGMEYLGTKRYIHRDLATRNILVENENR-VKIGDFGLTKVLPQDKEyYKVKE 169
                         90       100       110
                 ....*....|....*....|....*....|...
gi 528504250 193 ASR---YFKGPELLVDYQmYDYSLDMWSLGCML 222
Cdd:cd14205  170 PGEspiFWYAPESLTESK-FSVASDVWSFGVVL 201
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
94-232 2.48e-05

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 45.68  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  94 IITLLDIIKDPvsRTPALVFEHVNNTDFKQLYQTLSDYD-----IRF-YMYEILKALDYCHSMG--IMHRDVKPHNVMID 165
Cdd:cd14026   59 ILPILGICNEP--EFLGIVTEYMTNGSLNELLHEKDIYPdvawpLRLrILYEIALGVNYLHNMSppLLHHDLKTQNILLD 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 166 HEHRkLRLIDWGLAEF---------------------YHPNQEYNVRVASRyfkgpeLLVDYQMYDYSLDMWSLgcmlas 224
Cdd:cd14026  137 GEFH-VKIADFGLSKWrqlsisqsrssksapeggtiiYMPPEEYEPSQKRR------ASVKHDIYSYAIIMWEV------ 203

                 ....*...
gi 528504250 225 mIFRKEPF 232
Cdd:cd14026  204 -LSRKIPF 210
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
86-232 2.50e-05

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: 45.45  E-value: 2.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  86 ENLRG--GPNIITLLDIIKDPVS--RTPALVFEHVNNTDFK---QLYQTLSDYDIRFYMYEILKALDYCHSMG--IMHRD 156
Cdd:cd14032   52 EMLKGlqHPNIVRFYDFWESCAKgkRCIVLVTELMTSGTLKtylKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRD 131
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 157 VKPHNVMIDHEHRKLRLIDWGLAEFYHPNQEYNVrVASRYFKGPELLVDYqmYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14032  132 LKCDNIFITGPTGSVKIGDLGLATLKRASFAKSV-IGTPEFMAPEMYEEH--YDESVDVYAFGMCMLEMATSEYPY 204
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
139-247 2.70e-05

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: 45.42  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNqEYNVRVASRY---FKGPElLVDYQMYDYSLDM 215
Cdd:cd05072  112 QIAEGMAYIERKNYIHRDLRAANVLVS-ESLMCKIADFGLARVIEDN-EYTAREGAKFpikWTAPE-AINFGSFTIKSDV 188
                         90       100       110
                 ....*....|....*....|....*....|...
gi 528504250 216 WSLGCMLASMI-FRKEPfFHGHDNYDQLVRIAK 247
Cdd:cd05072  189 WSFGILLYEIVtYGKIP-YPGMSNSDVMSALQR 220
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
140-226 2.88e-05

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: 45.33  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 140 ILKALDYCHSMGIMHRDVKPHNVMI---DHEHRKLRLIDWGLA-EFYHPNQEYN------------VRVASRY-FKGPEL 202
Cdd:cd14017  106 ILKAIEDIHEVGFLHRDVKPSNFAIgrgPSDERTVYILDFGLArQYTNKDGEVErpprnaagfrgtVRYASVNaHRNKEQ 185
                         90       100
                 ....*....|....*....|....*
gi 528504250 203 -LVDyqmydyslDMWSLGCMLASMI 226
Cdd:cd14017  186 gRRD--------DLWSWFYMLIEFV 202
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
134-178 4.15e-05

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: 45.42  E-value: 4.15e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 528504250 134 RFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGL 178
Cdd:cd05625  104 RFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGH-IKLTDFGL 147
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
138-222 4.28e-05

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: 45.01  E-value: 4.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 138 YEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHpNQEY-----NVRVASRYFkGPELLVDyQMYDYS 212
Cdd:cd05101  153 YQLARGMEYLASQKCIHRDLAARNVLVT-ENNVMKIADFGLARDIN-NIDYykkttNGRLPVKWM-APEALFD-RVYTHQ 228
                         90
                 ....*....|
gi 528504250 213 LDMWSLGCML 222
Cdd:cd05101  229 SDVWSFGVLM 238
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
128-232 4.50e-05

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: 44.48  E-value: 4.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHN-VMIDHEHRKLRLIdwGLAEFY---HPNQEYNVRVASRYFKGPELL 203
Cdd:cd14024   81 LSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRfVFTDELRTKLVLV--NLEDSCplnGDDDSLTDKHGCPAYVGPEIL 158
                         90       100       110
                 ....*....|....*....|....*....|
gi 528504250 204 VDYQMYD-YSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14024  159 SSRRSYSgKAADVWSLGVCLYTMLLGRYPF 188
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
45-177 5.02e-05

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: 42.81  E-value: 5.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  45 LGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLR----GGPNIITLLDIIKdpVSRTPALVFEHVN--N 118
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLESEMDILRrlkgLELNIPKVLVTED--VDGPNILLMELVKggT 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528504250 119 TDFKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWG 177
Cdd:cd13968   79 LIAYTQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDG-NVKLIDFG 136
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
39-186 5.13e-05

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; 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. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 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: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 44.42  E-value: 5.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEkvvvkilkpvkkkkikREIKILENLRggpniitlldiikdpvSRTPALVFEHvnn 118
Cdd:cd14128    2 YRLVRKIGSGSFGDIYLGINITNGE----------------EVAVKLESQK----------------ARHPQLLYES--- 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 119 tdfkQLYQTLS---------------DYDI-------------------RFYMYEILKALD-------YCHSMGIMHRDV 157
Cdd:cd14128   47 ----KLYKILQggvgiphirwygqekDYNVlvmdllgpsledlfnfcsrRFTMKTVLMLADqmigrieYVHNKNFIHRDI 122
                        170       180       190
                 ....*....|....*....|....*....|.
gi 528504250 158 KPHNVM--IDHEHRKLRLIDWGLAEFYHPNQ 186
Cdd:cd14128  123 KPDNFLmgIGRHCNKLFLIDFGLAKKYRDSR 153
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
139-232 5.98e-05

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: 44.25  E-value: 5.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGI---MHRDVKPHNVMI-------DHEHRKLRLIDWGLAEFYHPNQEynVRVASRY-FKGPElLVDYQ 207
Cdd:cd14147  109 QIARGMHYLHCEALvpvIHRDLKSNNILLlqpiendDMEHKTLKITDFGLAREWHKTTQ--MSAAGTYaWMAPE-VIKAS 185
                         90       100
                 ....*....|....*....|....*
gi 528504250 208 MYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14147  186 TFSKGSDVWSFGVLLWELLTGEVPY 210
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
138-242 6.05e-05

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: 44.28  E-value: 6.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 138 YEILKALDYC-HSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELL---VDYQMYDYSL 213
Cdd:cd06616  116 VATVKALNYLkEELKIIHRDVKPSNILLD-RNGNIKLCDFGISGQLVDSIAKTRDAGCRPYMAPERIdpsASRDGYDVRS 194
                         90       100
                 ....*....|....*....|....*....
gi 528504250 214 DMWSLGCMLASMIFRKEPFFHGHDNYDQL 242
Cdd:cd06616  195 DVWSLGITLYEVATGKFPYPKWNSVFDQL 223
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
92-267 7.08e-05

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: 44.24  E-value: 7.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLD----------IIKDPVSRTPALVFEHVNNTDFK----QLYQtLSDYDIRFYMYEILKALDYCH-SMGIMHRD 156
Cdd:cd14011   62 PRILTVQHpleesreslaFATEPVFASLANVLGERDNMPSPppelQDYK-LYDVEIKYGLLQISEALSFLHnDVKLVHGN 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 157 VKPHNVMIDhEHRklrliDWGLAEFYHPNQEYNVRVASRYFKGPE--------LLVDY--------QMYDYSLDMWSLGC 220
Cdd:cd14011  141 ICPESVVIN-SNG-----EWKLAGFDFCISSEQATDQFPYFREYDpnlpplaqPNLNYlapeyilsKTCDPASDMFSLGV 214
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 528504250 221 MLASMIFRKEPFFHGHDNYDQLVRIAKVLGT----------EDLYDYIdKYNIELDP 267
Cdd:cd14011  215 LIYAIYNKGKPLFDCVNNLLSYKKNSNQLRQlslsllekvpEELRDHV-KTLLNVTP 270
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
110-232 7.23e-05

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 44.86  E-value: 7.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 110 ALVFEHVNNTDFKQLYQTLSDYDIRFYMYE-------ILKALDYCHSMGIMHRDVKPHNVMIdHEHRKLRLIDWGLAEFY 182
Cdd:PTZ00283 115 ALVLDYANAGDLRQEIKSRAKTNRTFREHEagllfiqVLLAVHHVHSKHMIHRDIKSANILL-CSNGLVKLGDFGFSKMY 193
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 183 HPNQEYNVR---VASRYFKGPELlvdYQMYDYS--LDMWSLGCMLASMIFRKEPF 232
Cdd:PTZ00283 194 AATVSDDVGrtfCGTPYYVAPEI---WRRKPYSkkADMFSLGVLLYELLTLKRPF 245
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
93-277 8.97e-05

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. 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 STK_BAK1-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: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 43.64  E-value: 8.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIKDPVSRTpaLVFEHVNNTDFKQLYQTLS------DYDIRFYM-YEILKALDYCH---SMGIMHRDVKPHNV 162
Cdd:cd14664   51 NIVRLRGYCSNPTTNL--LVYEYMPNGSLGELLHSRPesqpplDWETRQRIaLGSARGLAYLHhdcSPLIIHRDVKSNNI 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 163 MIDHEHRKlRLIDWGLAEFYHPNQ-EYNVRVASRY-FKGPELLVDYQMYDYSlDMWSLGCMLASMIFRKEPF--FHGHDN 238
Cdd:cd14664  129 LLDEEFEA-HVADFGLAKLMDDKDsHVMSSVAGSYgYIAPEYAYTGKVSEKS-DVYSYGVVLLELITGKRPFdeAFLDDG 206
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528504250 239 YDqLVRIAKVLGTEDLYDYIdkynieLDPRFNDILGRHS 277
Cdd:cd14664  207 VD-IVDWVRGLLEEKKVEAL------VDPDLQGVYKLEE 238
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
139-232 9.05e-05

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: 43.87  E-value: 9.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHS---MGIMHRDVKPHNVM----IDHE---HRKLRLIDWGLAEFYHpnQEYNVRVASRY-FKGPElLVDYQ 207
Cdd:cd14146  110 QIARGMLYLHEeavVPILHRDLKSSNILllekIEHDdicNKTLKITDFGLAREWH--RTTKMSAAGTYaWMAPE-VIKSS 186
                         90       100
                 ....*....|....*....|....*
gi 528504250 208 MYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14146  187 LFSKGSDIWSYGVLLWELLTGEVPY 211
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
92-229 9.20e-05

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: 43.84  E-value: 9.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVS--RTPALVFEHVNNTDFKQLYQTLSDYDIRF---YMYEILKALDYCHSMG--IMHRDVKPHNVMI 164
Cdd:cd14033   60 PNIVRFYDSWKSTVRghKCIILVTELMTSGTLKTYLKRFREMKLKLlqrWSRQILKGLHFLHSRCppILHRDLKCDNIFI 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 165 DHEHRKLRLIDWGLAEFYHPNQEYNVrVASRYFKGPELLvdYQMYDYSLDMWSLG-CML--------------ASMIFRK 229
Cdd:cd14033  140 TGPTGSVKIGDLGLATLKRASFAKSV-IGTPEFMAPEMY--EEKYDEAVDVYAFGmCILematseypysecqnAAQIYRK 216
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
135-233 9.80e-05

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 44.20  E-value: 9.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 135 FYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHpNQEYNVRVASRYFkGPELLVDYQmYDYSLD 214
Cdd:PTZ00426 135 FYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGF-IKMTDFGFAKVVD-TRTYTLCGTPEYI-APEILLNVG-HGKAAD 210
                         90
                 ....*....|....*....
gi 528504250 215 MWSLGCMLASMIFRKEPFF 233
Cdd:PTZ00426 211 WWTLGIFIYEILVGCPPFY 229
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
138-232 9.85e-05

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: 43.57  E-value: 9.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 138 YEILKALDYCHSMGIMHRDVKPHN-VMIDHEHRKLRL-------IDWGlaefyhPNQEYNVRVASRYFKGPELLVDYQMY 209
Cdd:cd13976   91 RQIASAVAHCHRNGIVLRDLKLRKfVFADEERTKLRLesledavILEG------EDDSLSDKHGCPAYVSPEILNSGATY 164
                         90       100
                 ....*....|....*....|....
gi 528504250 210 D-YSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd13976  165 SgKAADVWSLGVILYTMLVGRYPF 188
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
111-222 1.09e-04

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: 43.73  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFEHVNN---TDFKQLYQT-LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEFYHPNQ 186
Cdd:cd05081   84 LVMEYLPSgclRDFLQRHRArLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAH-VKIADFGLAKLLPLDK 162
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 528504250 187 EYNV----RVASRYFKGPELLVDyQMYDYSLDMWSLGCML 222
Cdd:cd05081  163 DYYVvrepGQSPIFWYAPESLSD-NIFSRQSDVWSFGVVL 201
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
39-324 1.16e-04

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. 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. 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: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 43.85  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNE--KVVVKILKPVKKKKIKREIKILENLRGG----PNIITLLDIIKD-PVSRTPA- 110
Cdd:cd14218   12 YHVVRKLGWGHFSTVWLCWDIQRKRfvALKVVKSAVHYTETAVDEIKLLKCVRDSdpsdPKRETIVQLIDDfKISGVNGv 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 ---LVFEHVNNTDFKQL----YQTLSDYDIRFYMYEILKALDYCHSM-GIMHRDVKPHNVMIDHEHRKLR---------- 172
Cdd:cd14218   92 hvcMVLEVLGHQLLKWIiksnYQGLPLPCVKSILRQVLQGLDYLHTKcKIIHTDIKPENILMCVDEGYVRrlaaeatiwq 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 173 ----------LIDWGLAEFY-HPNQEYN-----VRVA-----------------SRYFKGPELLVDYQmYDYSLDMWSLG 219
Cdd:cd14218  172 qagapppsgsSVSFGASDFLvNPLEPQNadkirVKIAdlgnacwvhkhftediqTRQYRALEVLIGAE-YGTPADIWSTA 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 220 CM---LASMIFRKEPffHGHDNY----DQLVRIAKVLG-TEDLYDYIDKYNIELDPRFNDILGRHSRKRW-------ERF 284
Cdd:cd14218  251 CMafeLATGDYLFEP--HSGEDYtrdeDHIAHIVELLGdIPPHFALSGRYSREYFNRRGELRHIKNLKHWglyevlvEKY 328
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 528504250 285 VHSENQhlvSTEALDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14218  329 EWPLEQ---AAQFTDFLLPMMEFLPEKRATAAQCLQHPWL 365
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
93-245 1.56e-04

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: 43.25  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  93 NIITLLDIIKDPVSRTPALVFEHVNNTdfkQLYQTLSD---------YDIRFYMYEILKALDYCHSMGIMHRDVKPHNVM 163
Cdd:cd13988   52 NIVKLFAIEEELTTRHKVLVMELCPCG---SLYTVLEEpsnayglpeSEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIM 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 164 --IDHEHRKL-RLIDWGLAEFYHPNQEYNVRVASRYFKGPE------LLVDYQ-MYDYSLDMWSLGCML-----ASMIFR 228
Cdd:cd13988  129 rvIGEDGQSVyKLTDFGAARELEDDEQFVSLYGTEEYLHPDmyeravLRKDHQkKYGATVDLWSIGVTFyhaatGSLPFR 208
                        170
                 ....*....|....*..
gi 528504250 229 kePFFHGHDNYDQLVRI 245
Cdd:cd13988  209 --PFEGPRRNKEVMYKI 223
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
139-222 1.56e-04

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: 42.86  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIDHEHRKlRLIDWGlaeFYHPNQEYNVR-VASRYFKGPELLVDYqmYDYSLDMWS 217
Cdd:cd13975  110 DVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRA-KITDLG---FCKPEAMMSGSiVGTPIHMAPELFSGK--YDNSVDVYA 183

                 ....*
gi 528504250 218 LGCML 222
Cdd:cd13975  184 FGILF 188
pknD PRK13184
serine/threonine-protein kinase PknD;
140-187 1.60e-04

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 43.99  E-value: 1.60e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 528504250 140 ILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQE 187
Cdd:PRK13184 122 ICATIEYVHSKGVLHRDLKPDNILLG-LFGEVVILDWGAAIFKKLEEE 168
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
92-262 1.65e-04

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl 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 its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl 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: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 43.07  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSR----TPALVFEHVNNTDFKQ--LYQTLSDYDIRF-------YMYEILKALDYCHSMGIMHRDVK 158
Cdd:cd05075   61 PNVMRLIGVCLQNTESegypSPVVILPFMKHGDLHSflLYSRLGDCPVYLptqmlvkFMTDIASGMEYLSSKNFIHRDLA 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 159 PHNVMIDhEHRKLRLIDWGLA-EFYHPNQEYNVRVASRYFK--GPELLVDyQMYDYSLDMWSLGCMLASMIFRKEPFFHG 235
Cdd:cd05075  141 ARNCMLN-ENMNVCVADFGLSkKIYNGDYYRQGRISKMPVKwiAIESLAD-RVYTTKSDVWSFGVTMWEIATRGQTPYPG 218
                        170       180
                 ....*....|....*....|....*..
gi 528504250 236 HDNydqlvriakvlgtEDLYDYIDKYN 262
Cdd:cd05075  219 VEN-------------SEIYDYLRQGN 232
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
132-222 1.79e-04

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 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: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 43.05  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 132 DIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEY----NVRVASRYFkGPELLVDyQ 207
Cdd:cd05103  180 DLICYSFQVAKGMEFLASRKCIHRDLAARNILLS-ENNVVKICDFGLARDIYKDPDYvrkgDARLPLKWM-APETIFD-R 256
                         90
                 ....*....|....*
gi 528504250 208 MYDYSLDMWSLGCML 222
Cdd:cd05103  257 VYTIQSDVWSFGVLL 271
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
92-222 2.08e-04

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: 42.73  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVS--RTPALVFEHVNNTDFK---QLYQTLSDYDIRFYMYEILKALDYCHSMG--IMHRDVKPHNVMI 164
Cdd:cd14030   84 PNIVRFYDSWESTVKgkKCIVLVTELMTSGTLKtylKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFI 163
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528504250 165 DHEHRKLRLIDWGLAEFYHPNQEYNVrVASRYFKGPELLvdYQMYDYSLDMWSLG-CML 222
Cdd:cd14030  164 TGPTGSVKIGDLGLATLKRASFAKSV-IGTPEFMAPEMY--EEKYDESVDVYAFGmCML 219
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
139-222 2.13e-04

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: 42.63  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLI----DWGLAEfYHPNQEYNVRVASRYFKGPELLVDYQMYDYSLD 214
Cdd:cd14068   94 HVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCAIIakiaDYGIAQ-YCCRMGIKTSEGTPGFRAPEVARGNVIYNQQAD 172

                 ....*...
gi 528504250 215 MWSLGCML 222
Cdd:cd14068  173 VYSFGLLL 180
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
148-228 2.16e-04

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) 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. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors 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. The ACVR2b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 42.71  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 148 HSMGIMHRDVKPHNVMIDHEHRKLrLIDWGLAEFYHPNQ---EYNVRVASRYFKGPELL---VDYQMYDY-SLDMWSLGC 220
Cdd:cd14140  120 HKPAIAHRDFKSKNVLLKNDLTAV-LADFGLAVRFEPGKppgDTHGQVGTRRYMAPEVLegaINFQRDSFlRIDMYAMGL 198

                 ....*...
gi 528504250 221 MLASMIFR 228
Cdd:cd14140  199 VLWELVSR 206
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
136-232 2.53e-04

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 42.38  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 136 YMYEILKALDYCH-SMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEF-----YHPNQEYNVRvASRYFKGPELLVDY--- 206
Cdd:cd13992  102 FIKDIVKGMNYLHsSSIGYHGRLKSSNCLVD-SRWVVKLTDFGLRNLleeqtNHQLDEDAQH-KKLLWTAPELLRGSlle 179
                         90       100
                 ....*....|....*....|....*.
gi 528504250 207 QMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd13992  180 VRGTQKGDVYSFAIILYEILFRSDPF 205
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
139-247 2.56e-04

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 42.21  E-value: 2.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNqEYNVRVASRY---FKGPELLVdYQMYDYSLDM 215
Cdd:cd14203   99 QIASGMAYIERMNYIHRDLRAANILVG-DNLVCKIADFGLARLIEDN-EYTARQGAKFpikWTAPEAAL-YGRFTIKSDV 175
                         90       100       110
                 ....*....|....*....|....*....|..
gi 528504250 216 WSLGCMLASMIFRKEPFFHGHDNYDQLVRIAK 247
Cdd:cd14203  176 WSFGILLTELVTKGRVPYPGMNNREVLEQVER 207
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
92-219 2.93e-04

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: 42.10  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250   92 PNIITLLDIIKDpvSRTPALVFEHVNNTDFK----QLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHE 167
Cdd:pfam07714  61 PNIVKLLGVCTQ--GEPLYIVTEYMPGGDLLdflrKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSEN 138
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504250  168 HrKLRLIDWGLAEFYHPNQEYNVR---------VAsryfkgPELLVDYQMYDYSlDMWSLG 219
Cdd:pfam07714 139 L-VVKISDFGLSRDIYDDDYYRKRgggklpikwMA------PESLKDGKFTSKS-DVWSFG 191
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
39-232 3.33e-04

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; 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. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 41.96  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAIN-ITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLLDIIKDPVSRTPALVFEHVN 117
Cdd:cd14129    2 WKVLRKIGGGGFGEIYDALDlLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNDRFNYVVMQLQGRN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 118 NTDFKQlYQTLSDYDIRFYMY---EILKALDYCHSMGIMHRDVKPHNVMIDH---EHRKLRLIDWGLAEFYhPNQEYNVR 191
Cdd:cd14129   82 LADLRR-SQSRGTFTISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAMGRfpsTCRKCYMLDFGLARQF-TNSCGDVR 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 528504250 192 vASRYFKGPELLVDYQMYDYSL--------DMWSLGCMLASMIFRKEPF 232
Cdd:cd14129  160 -PPRAVAGFRGTVRYASINAHRnremgrhdDLWSLFYMLVEFVVGQLPW 207
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
136-228 3.81e-04

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: 42.16  E-value: 3.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 136 YMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRK--LRLIDWGLAEFYH---PNQEYNVRV---------ASRYFKGPE 201
Cdd:cd13977  139 FMLQLSSALAFLHRNQIVHRDLKPDNILISHKRGEpiLKVADFGLSKVCSgsgLNPEEPANVnkhflssacGSDFYMAPE 218
                         90       100
                 ....*....|....*....|....*..
gi 528504250 202 LLVDYqmYDYSLDMWSLGCMLASMIFR 228
Cdd:cd13977  219 VWEGH--YTAKADIFALGIIIWAMVER 243
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
99-222 4.11e-04

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha 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: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 42.32  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  99 DIIKDPVSRTPAlvFEHVNNTDFKQL-----YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHeHRKLRL 173
Cdd:cd05105  202 DIQRSNYDRPAS--YKGSNDSEVKNLlsddgSEGLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQ-GKIVKI 278
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528504250 174 IDWGLAEFYHPNQEYnVRVASRY----FKGPELLVDyQMYDYSLDMWSLGCML 222
Cdd:cd05105  279 CDFGLARDIMHDSNY-VSKGSTFlpvkWMAPESIFD-NLYTTLSDVWSYGILL 329
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
140-226 4.11e-04

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: 41.85  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 140 ILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLrLIDWGLAEFY-----------HPNQEYNVR----------VASRYFK 198
Cdd:cd14222   99 IASGMAYLHSMSIIHRDLNSHNCLIKLDKTVV-VADFGLSRLIveekkkpppdkPTTKKRTLRkndrkkrytvVGNPYWM 177
                         90       100
                 ....*....|....*....|....*...
gi 528504250 199 GPELLvDYQMYDYSLDMWSLGCMLASMI 226
Cdd:cd14222  178 APEML-NGKSYDEKVDIFSFGIVLCEII 204
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
146-226 4.16e-04

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. 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 Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 41.62  E-value: 4.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 146 YCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYNVRVASRY---FKGPElLVDYQMYDYSLDMWSLGCML 222
Cdd:cd05068  119 YLESQNYIHRDLAARNVLVG-ENNICKVADFGLARVIKVEDEYEAREGAKFpikWTAPE-AANYNRFSIKSDVWSFGILL 196

                 ....
gi 528504250 223 ASMI 226
Cdd:cd05068  197 TEIV 200
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
92-280 4.90e-04

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: 41.54  E-value: 4.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDII--KDPVsrtpALVFEHVNNTDFKQLY--------------------QTLSDYDIRFYMYEILKALDYCHS 149
Cdd:cd05090   67 PNIVCLLGVVtqEQPV----CMLFEFMNQGDLHEFLimrsphsdvgcssdedgtvkSSLDHGDFLHIAIQIAAGMEYLSS 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 150 MGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYNVRVAS----RYFkgPELLVDYQMYDYSLDMWSLGCMLASM 225
Cdd:cd05090  143 HFFVHKDLAARNILVG-EQLHVKISDLGLSREIYSSDYYRVQNKSllpiRWM--PPEAIMYGKFSSDSDIWSFGVVLWEI 219
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528504250 226 I-FRKEPFFhGHDNYD--QLVRIAKVLG-TED----LYDYIDKYNIELD---PRFNDIlgrHSRKR 280
Cdd:cd05090  220 FsFGLQPYY-GFSNQEviEMVRKRQLLPcSEDcpprMYSLMTECWQEIPsrrPRFKDI---HARLR 281
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
139-247 5.34e-04

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 41.60  E-value: 5.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNqEYNVRVASRY---FKGPELLVdYQMYDYSLDM 215
Cdd:cd05069  116 QIADGMAYIERMNYIHRDLRAANILVG-DNLVCKIADFGLARLIEDN-EYTARQGAKFpikWTAPEAAL-YGRFTIKSDV 192
                         90       100       110
                 ....*....|....*....|....*....|..
gi 528504250 216 WSLGCMLASMIFRKEPFFHGHDNYDQLVRIAK 247
Cdd:cd05069  193 WSFGILLTELVTKGRVPYPGMVNREVLEQVER 224
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
109-232 6.18e-04

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-2D subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 41.24  E-value: 6.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 109 PALVFEHVNNTDFKQLyqtLSDYDIRF-YMY------EILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEF 181
Cdd:cd14043   71 LAIVSEHCSRGSLEDL---LRNDDMKLdWMFksslllDLIKGMRYLHHRGIVHGRLKSRNCVVDGRF-VLKITDYGYNEI 146
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250 182 YH----PNQEYNVRvaSRYFKGPELLVDYQMY---DYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14043  147 LEaqnlPLPEPAPE--ELLWTAPELLRDPRLErrgTFPGDVFSFAIIMQEVIVRGAPY 202
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
139-216 6.38e-04

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 40.95  E-value: 6.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528504250  139 EILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPNQEYNVRVASRYFKGPELLVDYQMYDYSLDMW 216
Cdd:pfam01636 156 ALLALLPAELPPVLVHGDLHPGNLLVDPGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGAFGY 233
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
139-232 6.80e-04

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: 40.84  E-value: 6.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHS---MGIMHRDVKPHNVMI-------DHEHRKLRLIDWGLA-EFYHPNQeynVRVASRY-FKGPElLVDY 206
Cdd:cd14061  100 QIARGMNYLHNeapVPIIHRDLKSSNILIleaieneDLENKTLKITDFGLArEWHKTTR---MSAAGTYaWMAPE-VIKS 175
                         90       100
                 ....*....|....*....|....*.
gi 528504250 207 QMYDYSLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14061  176 STFSKASDVWSYGVLLWELLTGEVPY 201
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
111-181 7.57e-04

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 41.41  E-value: 7.57e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504250 111 LVFEHVNNTDFKQLYQTLSDYdirfyMYEILKALDYCHSMGIMHRDVKPHNVMIDHEhrKLRLIDWGLAEF 181
Cdd:PRK09605 413 IVMEYIGGKDLKDVLEGNPEL-----VRKVGEIVAKLHKAGIVHGDLTTSNFIVRDD--RLYLIDFGLGKY 476
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
140-231 9.67e-04

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: 40.80  E-value: 9.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 140 ILKALDYCHSM-GIMHRDVKPHNVMIDhEHRKLRLIDWGLAEfYHPNQEYNVRVASRYFKGPELLVDYQmYDYSLDMWSL 218
Cdd:cd06649  112 VLRGLAYLREKhQIMHRDVKPSNILVN-SRGEIKLCDFGVSG-QLIDSMANSFVGTRSYMSPERLQGTH-YSVQSDIWSM 188
                         90
                 ....*....|...
gi 528504250 219 GCMLASMIFRKEP 231
Cdd:cd06649  189 GLSLVELAIGRYP 201
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
39-326 1.01e-03

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: 40.81  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVK---------ILKPVKKKKIKREIKILENLRGGPNIITLLDIIK-DPVSRT 108
Cdd:cd14040    8 YLLLHLLGRGGFSEVYKAFDLYEQRYAAVKihqlnkswrDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDTFC 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 109 PALVFEHVNNTDF--KQlYQTLSDYDIRFYMYEILKALDYCHSMG--IMHRDVKPHNVMI--DHEHRKLRLIDWGLAEFY 182
Cdd:cd14040   88 TVLEYCEGNDLDFylKQ-HKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdGTACGEIKITDFGLSKIM 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 183 HpNQEYNVR--------VASRYFKGPELLV---DYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGT 251
Cdd:cd14040  167 D-DDSYGVDgmdltsqgAGTYWYLPPECFVvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKAT 245
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 252 EdlydyidkynieldprfndilgrhsrkrwerfVHSENQHLVSTEALDFLDKLLRYDHQARLTAREAMDHSYFYP 326
Cdd:cd14040  246 E--------------------------------VQFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYLLP 288
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
139-247 1.13e-03

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 40.44  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIDHeHRKLRLIDWGLAEFYHPNqEYNVRVASRY---FKGPELLVdYQMYDYSLDM 215
Cdd:cd05070  113 QVAAGMAYIERMNYIHRDLRSANILVGN-GLICKIADFGLARLIEDN-EYTARQGAKFpikWTAPEAAL-YGRFTIKSDV 189
                         90       100       110
                 ....*....|....*....|....*....|..
gi 528504250 216 WSLGCMLASMIFRKEPFFHGHDNYDQLVRIAK 247
Cdd:cd05070  190 WSFGILLTELVTKGRVPYPGMNNREVLEQVER 221
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
88-181 1.24e-03

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine. [Unknown function, General]


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 39.89  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250   88 LRGGPNIITLLDIikDPVSRTpaLVFEHVNNTDFKQLYQTLSDYdirfYMYEILKALDYCHSMGIMHRDVKPHNVMIDhe 167
Cdd:TIGR03724  55 RKAGVNTPVIYDV--DPDNKT--IVMEYIEGKPLKDVIEENGDE----LAREIGRLVGKLHKAGIVHGDLTTSNIIVR-- 124
                          90
                  ....*....|....
gi 528504250  168 HRKLRLIDWGLAEF 181
Cdd:TIGR03724 125 DDKVYLIDFGLGKY 138
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
110-181 1.36e-03

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: 40.18  E-value: 1.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 110 ALVFEHVNNTDFKQLYQTLS---DYDIRFYMyEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAEF 181
Cdd:cd14027   67 SLVMEYMEKGNLMHVLKKVSvplSVKGRIIL-EIIEGMAYLHGKGVIHKDLKPENILVDNDFH-IKIADLGLASF 139
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
133-179 1.38e-03

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 40.82  E-value: 1.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 528504250 133 IRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLA 179
Cdd:PLN03224 311 IKGVMRQVLTGLRKLHRIGIVHRDIKPENLLVTVDG-QVKIIDFGAA 356
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
139-247 1.41e-03

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing 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 with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src 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: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 40.06  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNqEYNVRVASRY---FKGPELLVdYQMYDYSLDM 215
Cdd:cd05071  113 QIASGMAYVERMNYVHRDLRAANILVG-ENLVCKVADFGLARLIEDN-EYTARQGAKFpikWTAPEAAL-YGRFTIKSDV 189
                         90       100       110
                 ....*....|....*....|....*....|..
gi 528504250 216 WSLGCMLASMIFRKEPFFHGHDNYDQLVRIAK 247
Cdd:cd05071  190 WSFGILLTELTTKGRVPYPGMVNREVLDQVER 221
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
92-234 1.46e-03

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting 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. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K 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: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 39.82  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIIKDPVSRTpALVFEHVNNTD-FKQLYQTLSDYDIRFYM---YEILKALDYCHSMG--IMHRDVKPHNVMId 165
Cdd:cd14064   51 PCVIQFVGACLDDPSQF-AIVTQYVSGGSlFSLLHEQKRVIDLQSKLiiaVDVAKGMEYLHNLTqpIIHRDLNSHNILL- 128
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504250 166 HEHRKLRLIDWGLAEFYHPNQEYNV--RVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFH 234
Cdd:cd14064  129 YEDGHAVVADFGESRFLQSLDEDNMtkQPGNLRWMAPEVFTQCTRYSIKADVFSYALCLWELLTGEIPFAH 199
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
127-222 1.46e-03

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. 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. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit 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: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 40.27  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 127 TLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHeHRKLRLIDWGLAEFYHPNQEYNVRVASRY---FKGPELL 203
Cdd:cd05104  210 ALDTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTH-GRITKICDFGLARDIRNDSNYVVKGNARLpvkWMAPESI 288
                         90
                 ....*....|....*....
gi 528504250 204 VDYqMYDYSLDMWSLGCML 222
Cdd:cd05104  289 FEC-VYTFESDVWSYGILL 306
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
139-232 1.69e-03

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: 39.79  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAefyhpnQEYNVRVASRYFKG------PELLVDyQMYDYS 212
Cdd:cd14059   89 QIASGMNYLHLHKIIHRDLKSPNVLVTYND-VLKISDFGTS------KELSEKSTKMSFAGtvawmaPEVIRN-EPCSEK 160
                         90       100
                 ....*....|....*....|
gi 528504250 213 LDMWSLGCMLASMIFRKEPF 232
Cdd:cd14059  161 VDIWSFGVVLWELLTGEIPY 180
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
92-219 1.71e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 40.26  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  92 PNIITLLDIikDPVSRTPALVFEHVNNTDFKQL---YQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEh 168
Cdd:PHA03211 220 PAVLALLDV--RVVGGLTCLVLPKYRSDLYTYLgarLRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGP- 296
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528504250 169 RKLRLIDWGLAEFYHPNQE----YNVrVASRYFKGPELLVDyQMYDYSLDMWSLG 219
Cdd:PHA03211 297 EDICLGDFGAACFARGSWStpfhYGI-AGTVDTNAPEVLAG-DPYTPSVDIWSAG 349
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
39-182 1.76e-03

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; 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. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 39.62  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250  39 YQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVK-KKKIKREIKILENLRGGPNIITLLDIIKDPVSRTPALVFEHVN 117
Cdd:cd14130    2 WKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQpKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGRN 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 118 NTDFK--QLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDH---EHRKLRLIDWGLAEFY 182
Cdd:cd14130   82 LADLRrsQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpsTYRKCYMLDFGLARQY 151
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
112-232 2.04e-03

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: 39.56  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 112 VFEHVNNTDFKQLyqtlsDYD-IRFYMYEILKALDYCHS---MGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYHPNQE 187
Cdd:cd14060   69 LFDYLNSNESEEM-----DMDqIMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVIAADG-VLKICDFGASRFHSHTTH 142
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 528504250 188 YNVrVASRYFKGPELLVDYQMYDySLDMWSLGCMLASMIFRKEPF 232
Cdd:cd14060  143 MSL-VGTFPWMAPEVIQSLPVSE-TCDTYSYGVVLWEMLTREVPF 185
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
139-228 2.14e-03

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: 39.42  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLI--DWGLAEFY------HPNQEYNVrVASRYFKGPELLVDyQMYD 210
Cdd:cd14156   97 DISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAVvtDFGLAREVgempanDPERKLSL-VGSAFWMAPEMLRG-EPYD 174
                         90
                 ....*....|....*...
gi 528504250 211 YSLDMWSLGCMLASMIFR 228
Cdd:cd14156  175 RKVDVFSFGIVLCEILAR 192
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
126-256 2.81e-03

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: 39.13  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 126 QTLsdydIRFyMYEILKALDYCHSMGIMHRDVKPHNVMIDhEHRKLRLIDWGLAEFYHPNQEYNVRVASRY---FKGPEL 202
Cdd:cd05074  123 QTL----VRF-MIDIASGMEYLSSKNFIHRDLAARNCMLN-ENMTVCVADFGLSKKIYSGDYYRQGCASKLpvkWLALES 196
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528504250 203 LVDyQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDN---YDQLV---RIAKVLGT-EDLYD 256
Cdd:cd05074  197 LAD-NVYTTHSDVWAFGVTMWEIMTRGQTPYAGVENseiYNYLIkgnRLKQPPDClEDVYE 256
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
104-222 2.86e-03

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R 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: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 39.44  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 104 PVSRTPALVFEHVNNTDfKQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYH 183
Cdd:cd05106  186 PVSSSSSQSSDSKDEED-TEDSWPLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGR-VAKICDFGLARDIM 263
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 528504250 184 PNQEYNVRVASRY---FKGPELLVDYqMYDYSLDMWSLGCML 222
Cdd:cd05106  264 NDSNYVVKGNARLpvkWMAPESIFDC-VYTVQSDVWSYGILL 304
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
128-222 3.26e-03

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: 39.01  E-value: 3.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 128 LSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHrKLRLIDWGLAEFYHPNQEYNVRVASRY---FKGPELLV 204
Cdd:cd05055  138 LTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGK-IVKICDFGLARDIMNDSNYVVKGNARLpvkWMAPESIF 216
                         90
                 ....*....|....*...
gi 528504250 205 DyQMYDYSLDMWSLGCML 222
Cdd:cd05055  217 N-CVYTFESDVWSYGILL 233
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
140-185 3.39e-03

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins (VRK1, VRK2, and VRK3) while invertebrates, specifically fruit flies and nematodes, seem to carry only a single ortholog. Mutations of VRK in Drosophila and Caenorhabditis elegans showed varying phenotypes ranging from embryonic lethality to mitotic and meiotic defects resulting in sterility. In vertebrates, VRK1 is implicated in cell cycle progression and proliferation, nuclear envelope assembly, and chromatin condensation. VRK2 is involved in modulating JNK signaling. VRK3 is an inactive pseudokinase that inhibits ERK signaling. The VRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 39.19  E-value: 3.39e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 528504250 140 ILKALDYCHSMGIMHRDVKPHNVMID--HEHRKLRLIDWGLAEFYHPN 185
Cdd:cd14015  136 ILDVLEYIHENGYVHADIKASNLLLGfgKNKDQVYLVDYGLASRYCPN 183
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
111-324 3.66e-03

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK2 mediates neuronal cell cycle and cell death through regulation of nuclear cyclin D1. It has also been found to promote leukemia cell proliferation by regulating cyclin A1. SRPK2 also plays a role in regulating pre-mRNA splicing and is required for spliceosomal B complex formation. 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. 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: 271119 [Multi-domain]  Cd Length: 366  Bit Score: 39.24  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 111 LVFE----HVNNTDFKQLYQTLSDYDIRFYMYEILKALDYCHSM-GIMHRDVKPHNVMI--------------------- 164
Cdd:cd14217   97 MVFEvlghHLLKWIIKSNYQGLPIRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMcvddayvrrmaaeatewqkag 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 165 -----------------------DHEHRKLRLIDWGLAEFYHpnQEYNVRVASRYFKGPELLVDyQMYDYSLDMWSLGCM 221
Cdd:cd14217  177 apppsgsavstapdllvnpldprNADKIRVKIADLGNACWVH--KHFTEDIQTRQYRSIEVLIG-AGYSTPADIWSTACM 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 222 ---LASMIFRKEPffHGHDNY----DQLVRIAKVLGT-EDLYDYIDKYNIELDPRFNDILGRHSRKRWERF-VHSENQHL 292
Cdd:cd14217  254 afeLATGDYLFEP--HSGEDYsrdeDHIAHIIELLGCiPRHFALSGKYSREFFNRRGELRHITKLKPWSLFdVLVEKYGW 331
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 528504250 293 VSTEA---LDFLDKLLRYDHQARLTAREAMDHSYF 324
Cdd:cd14217  332 PHEDAaqfTDFLIPMLEMVPEKRASAGECLRHPWL 366
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
133-178 4.00e-03

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 38.80  E-value: 4.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 528504250 133 IRFYMYEILKALDYCHSMGIMHRDVKPHNVMidHEHRKLRLIDWGL 178
Cdd:cd14152   99 TRQIAQEIIKGMGYLHAKGIVHKDLKSKNVF--YDNGKVVITDFGL 142
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
122-222 4.04e-03

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 38.59  E-value: 4.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 122 KQLYQTLSDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRkLRLIDWGLAE--F---YH---PNQEYNVRVA 193
Cdd:cd05043  107 ANNPQALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQ-VKITDNALSRdlFpmdYHclgDNENRPIKWM 185
                         90       100
                 ....*....|....*....|....*....
gi 528504250 194 SryfkgPELLVDyQMYDYSLDMWSLGCML 222
Cdd:cd05043  186 S-----LESLVN-KEYSSASDVWSFGVLL 208
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
139-182 5.05e-03

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; 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. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 38.50  E-value: 5.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIDHEHR--KLRLIDWGLAEFY 182
Cdd:cd14125  104 QMISRIEYVHSKNFIHRDIKPDNFLMGLGKKgnLVYIIDFGLAKKY 149
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
139-182 6.15e-03

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; 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. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271028 [Multi-domain]  Cd Length: 288  Bit Score: 38.18  E-value: 6.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIDHEHRK----LRLIDWGLAEFY 182
Cdd:cd14126  104 QLISRIEYVHSKHLIYRDVKPENFLIGRQSTKkqhvIHIIDFGLAKEY 151
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
137-226 7.50e-03

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: 37.76  E-value: 7.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528504250 137 MYEILKALDYCHSMG-IMHRDVKPHNVMIDHEHRKLRLIDWG--------LAEFYHPNQEYnvrVASRYFKGPELLVDYQ 207
Cdd:cd14001  116 ALSIARALEYLHNEKkILHGDIKSGNVLIKGDFESVKLCDFGvslpltenLEVDSDPKAQY---VGTEPWKAKEALEEGG 192
                         90
                 ....*....|....*....
gi 528504250 208 MYDYSLDMWSLGCMLASMI 226
Cdd:cd14001  193 VITDKADIFAYGLVLWEMM 211
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
139-178 7.57e-03

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function 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. The KSR2 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: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 37.68  E-value: 7.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 528504250 139 EILKALDYCHSMGIMHRDVKPHNVMIDHEhrKLRLIDWGL 178
Cdd:cd14153  105 EIVKGMGYLHAKGILHKDLKSKNVFYDNG--KVVITDFGL 142
 
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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