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Conserved domains on  [gi|27229182|ref|NP_083054|]
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NUAK family SNF1-like kinase 2 isoform B [Mus musculus]

Protein Classification

NUAK family SNF1-like kinase 2( domain architecture ID 10197672)

NUAK family SNF1-like kinase 2 (NUAK2) is a serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
53-307 0e+00

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: 563.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd14161   1 LKHRYEFLETLGKGTYGRVKKARDSSGRLVAIKSIRKDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQT 212
Cdd:cd14161  81 MEYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQDKFLQT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDACGLIRWLLMVNP 292
Cdd:cd14161 161 YCGSPLYASPEIVNGRPYIGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPSDACGLIRWLLMVNP 240
                       250
                ....*....|....*
gi 27229182 293 TRRATLEDVASHWWV 307
Cdd:cd14161 241 ERRATLEDVASHWWV 255
 
Name Accession Description Interval E-value
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
53-307 0e+00

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: 563.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd14161   1 LKHRYEFLETLGKGTYGRVKKARDSSGRLVAIKSIRKDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQT 212
Cdd:cd14161  81 MEYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQDKFLQT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDACGLIRWLLMVNP 292
Cdd:cd14161 161 YCGSPLYASPEIVNGRPYIGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPSDACGLIRWLLMVNP 240
                       250
                ....*....|....*
gi 27229182 293 TRRATLEDVASHWWV 307
Cdd:cd14161 241 ERRATLEDVASHWWV 255
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
57-307 8.69e-113

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 337.97  E-value: 8.69e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182     57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDkKTGKLVAIKVIKKKKIKKDRE--RILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182    136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCG 215
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182    216 SPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDH-KTLVKQISNGAYREPPK----PSDACGLIRWLLMV 290
Cdd:smart00220 159 TPEYMAPEVLLGKGY-GKAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPPPewdiSPEAKDLIRKLLVK 237
                          250
                   ....*....|....*..
gi 27229182    291 NPTRRATLEDVASHWWV 307
Cdd:smart00220 238 DPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
57-307 2.92e-69

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 224.05  E-value: 2.92e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182    57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLlHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHrDTGKIVAIKKIKKEKIKKKKDK-NILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   136 ASRGDLYDYISERPRLSERDARHFFRQIVSALhychqngivhrdlklenilldangnikiadfglsnlyHKGKFLQTFCG 215
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGL-------------------------------------ESGSSLTTFVG 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   216 SPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKP----SDACGLIRWLLMVN 291
Cdd:pfam00069 123 TPWYMAPEVLGGNPY-GPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPsnlsEEAKDLLKKLLKKD 201
                         250
                  ....*....|....*.
gi 27229182   292 PTRRATLEDVASHWWV 307
Cdd:pfam00069 202 PSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
53-302 5.67e-67

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 226.82  E-value: 5.67e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVI 131
Cdd:COG0515   5 LLGRYRILRLLGRGGMGVVYLARdLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQ 211
Cdd:COG0515  85 VMEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQ 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 T--FCGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK-----PSDACGLI 284
Cdd:COG0515 165 TgtVVGTPGYMAPEQARGEP-VDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSElrpdlPPALDAIV 243
                       250
                ....*....|....*....
gi 27229182 285 RWLLMVNPTRR-ATLEDVA 302
Cdd:COG0515 244 LRALAKDPEERyQSAAELA 262
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
55-309 7.54e-44

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 159.98  E-value: 7.54e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   55 HRYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:PTZ00263  18 SDFEMGETLGTGSFGRVRIAKhKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  134 EYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFlqTF 213
Cdd:PTZ00263  98 EFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTF--TL 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  214 CGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF-DGQDHKTLVKqISNGAYREPP-KPSDACGLIRWLLMVN 291
Cdd:PTZ00263 176 CGTPEYLAPEVIQSKGH-GKAVDWWTMGVLLYEFIAGYPPFfDDTPFRIYEK-ILAGRLKFPNwFDGRARDLVKGLLQTD 253
                        250       260
                 ....*....|....*....|....*.
gi 27229182  292 PTRR-ATL----EDVASHWW---VNW 309
Cdd:PTZ00263 254 HTKRlGTLkggvADVKNHPYfhgANW 279
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
56-279 7.79e-41

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 156.49  E-value: 7.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   56 RYEFLETLGKGTYGKVKKARESS-GRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:NF033483   8 RYEIGERIGRGGMAEVYLAKDTRlDRDVAVKVLRPDLARDPEFVARFRREAQSAASLSHPNIVSVYDVGEDGGIPYIVME 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL------SNLYHKGK 208
Cdd:NF033483  88 YVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIaralssTTMTQTNS 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27229182  209 FLqtfcGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQdhkTLVkQIsngAYR----EPPKPSD 279
Cdd:NF033483 168 VL----GTVHYLSPEQARGGT-VDARSDIYSLGIVLYEMLTGRPPFDGD---SPV-SV---AYKhvqeDPPPPSE 230
 
Name Accession Description Interval E-value
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
53-307 0e+00

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: 563.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd14161   1 LKHRYEFLETLGKGTYGRVKKARDSSGRLVAIKSIRKDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQT 212
Cdd:cd14161  81 MEYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQDKFLQT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDACGLIRWLLMVNP 292
Cdd:cd14161 161 YCGSPLYASPEIVNGRPYIGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPSDACGLIRWLLMVNP 240
                       250
                ....*....|....*
gi 27229182 293 TRRATLEDVASHWWV 307
Cdd:cd14161 241 ERRATLEDVASHWWV 255
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
55-307 0e+00

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: 556.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  55 HRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd14073   1 HRYELLETLGKGTYGKVKLAIErATGREVAIKSIKKDKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTF 213
Cdd:cd14073  81 EYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKDKLLQTF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDACGLIRWLLMVNPT 293
Cdd:cd14073 161 CGSPLYASPEIVNGTPYQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPSDASGLIRWMLTVNPK 240
                       250
                ....*....|....
gi 27229182 294 RRATLEDVASHWWV 307
Cdd:cd14073 241 RRATIEDIANHWWV 254
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
56-306 1.73e-139

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: 406.52  E-value: 1.73e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLlHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARhKLTGEKVAIKIIDKSKLKEEIEE-KIKREIEIMKLLNHPNIIKLYEVIETENKIYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFC 214
Cdd:cd14003  80 YASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGSLLKTFC 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 215 GSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK-PSDACGLIRWLLMVNPT 293
Cdd:cd14003 160 GTPAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHlSPDARDLIRRMLVVDPS 239
                       250
                ....*....|...
gi 27229182 294 RRATLEDVASHWW 306
Cdd:cd14003 240 KRITIEEILNHPW 252
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
57-307 8.69e-113

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 337.97  E-value: 8.69e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182     57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDkKTGKLVAIKVIKKKKIKKDRE--RILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182    136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCG 215
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182    216 SPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDH-KTLVKQISNGAYREPPK----PSDACGLIRWLLMV 290
Cdd:smart00220 159 TPEYMAPEVLLGKGY-GKAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPPPewdiSPEAKDLIRKLLVK 237
                          250
                   ....*....|....*..
gi 27229182    291 NPTRRATLEDVASHWWV 307
Cdd:smart00220 238 DPEKRLTAEEALQHPFF 254
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
56-306 3.75e-110

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: 331.36  E-value: 3.75e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHkKTGEEYAVKIIDKKKLKSEDEEM-LRREIEILKRLDHPNIVKLYEVFEDDKNLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL---DANGNIKIADFGLSNLYHKGKFLQ 211
Cdd:cd05117  80 LCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKIFEEGEKLK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKP----SDAC-GLIRW 286
Cdd:cd05117 160 TVCGTPYYVAPEVLKGKGY-GKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEwknvSEEAkDLIKR 238
                       250       260
                ....*....|....*....|
gi 27229182 287 LLMVNPTRRATLEDVASHWW 306
Cdd:cd05117 239 LLVVDPKKRLTAAEALNHPW 258
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
57-306 1.14e-106

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: 322.68  E-value: 1.14e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14079   4 YILGKTLGVGSFGKVKLAeHELTGHKVAVKILNRQKIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCG 215
Cdd:cd14079  84 VSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDGEFLKTSCG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 216 SPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-DACGLIRWLLMVNPTR 294
Cdd:cd14079 164 SPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSHLSpGARDLIKRMLVVDPLK 243
                       250
                ....*....|..
gi 27229182 295 RATLEDVASHWW 306
Cdd:cd14079 244 RITIPEIRQHPW 255
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
57-307 3.04e-100

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: 306.03  E-value: 3.04e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA---RESSGRLVAIKSIRKDKIKDeqDLLH--IRREIEIMSSLNHPHIIAIHEVFENSSKIVI 131
Cdd:cd14080   2 YRLGKTIGEGSYSKVKLAeytKSGLKEKVACKIIDKKKAPK--DFLEkfLPRELEILRKLRHPNIIQVYSIFERGSKVFI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFL- 210
Cdd:cd14080  80 FMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDDGDv 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 --QTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPP---KPSDAC-GLI 284
Cdd:cd14080 160 lsKTFCGSAAYAAPEILQGIPYDPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPSsvkKLSPECkDLI 239
                       250       260
                ....*....|....*....|...
gi 27229182 285 RWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14080 240 DQLLEPDPTKRATIEEILNHPWL 262
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
57-307 2.57e-99

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: 303.24  E-value: 2.57e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKdEQDLLH-IRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14007   2 FEIGKPLGKGKFGNVYLAREkKSGFIVALKVISKSQLQ-KSGLEHqLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNlYHKGKFLQTFC 214
Cdd:cd14007  81 YAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSV-HAPSNRRKTFC 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 215 GSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-DACGLIRWLLMVNPT 293
Cdd:cd14007 160 GTLDYLPPEMVEGKEY-DYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSpEAKDLISKLLQKDPS 238
                       250
                ....*....|....
gi 27229182 294 RRATLEDVASHWWV 307
Cdd:cd14007 239 KRLSLEQVLNHPWI 252
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
57-306 1.87e-98

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: 301.23  E-value: 1.87e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARESSGRL-VAIKSIRKDKIkDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14071   2 YDIERTIGKGNFAVVKLARHRITKTeVAIKIIDKSQL-DEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCG 215
Cdd:cd14071  81 ASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGELLKTWCG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 216 SPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDAC-GLIRWLLMVNPTR 294
Cdd:cd14071 161 SPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCeHLIRRMLVLDPSK 240
                       250
                ....*....|..
gi 27229182 295 RATLEDVASHWW 306
Cdd:cd14071 241 RLTIEQIKKHKW 252
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
57-307 2.58e-98

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: 301.09  E-value: 2.58e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14081   3 YRLGKTLGKGQTGLVKLAKHCvTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCG 215
Cdd:cd14081  83 VSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQPEGSLLETSCG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 216 SPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK-PSDACGLIRWLLMVNPTR 294
Cdd:cd14081 163 SPHYACPEVIKGEKYDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFiSPDAQDLLRRMLEVNPEK 242
                       250
                ....*....|...
gi 27229182 295 RATLEDVASHWWV 307
Cdd:cd14081 243 RITIEEIKKHPWF 255
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
56-307 5.06e-96

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: 294.81  E-value: 5.06e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDeQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14072   1 NYRLLKTIGKGNFAKVKLARHvLTGREVAIKIIDKTQLNP-SSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFC 214
Cdd:cd14072  80 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKLDTFC 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 215 GSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDAC-GLIRWLLMVNPT 293
Cdd:cd14072 160 GSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCeNLLKKFLVLNPS 239
                       250
                ....*....|....
gi 27229182 294 RRATLEDVASHWWV 307
Cdd:cd14072 240 KRGTLEQIMKDRWM 253
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
56-306 2.24e-92

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: 285.84  E-value: 2.24e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14663   1 RYELGRTLGEGTFAKVKFARNTkTGESVAIKIIDKEQVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGK---FLQ 211
Cdd:cd14663  81 LVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALSEQFRqdgLLH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK-PSDACGLIRWLLMV 290
Cdd:cd14663 161 TTCGTPNYVAPEVLARRGYDGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWfSPGAKSLIKRILDP 240
                       250
                ....*....|....*.
gi 27229182 291 NPTRRATLEDVASHWW 306
Cdd:cd14663 241 NPSTRITVEQIMASPW 256
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
53-307 5.71e-90

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: 279.65  E-value: 5.71e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDeqDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVI 131
Cdd:cd14078   1 LLKYYELHETIGSGGFAKVKLATHiLTGEKVAIKIMDKKALGD--DLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGK--F 209
Cdd:cd14078  79 VLEYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGMdhH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 210 LQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-DACGLIRWLL 288
Cdd:cd14078 159 LETCCGSPAYAAPELIQGKPYIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPEWLSpSSKLLLDQML 238
                       250
                ....*....|....*....
gi 27229182 289 MVNPTRRATLEDVASHWWV 307
Cdd:cd14078 239 QVDPKKRITVKELLNHPWV 257
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
57-307 1.22e-86

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: 271.24  E-value: 1.22e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSI------------RKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVF 123
Cdd:cd14077   3 WEFVKTIGAGSMGKVKLAKhIRTGEKCAIKIIprasnaglkkerEKRLEKEISRDIRTIREAALSSLLNHPHICRLRDFL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 124 ENSSKIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL 203
Cdd:cd14077  83 RTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSNL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 204 YHKGKFLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-DACG 282
Cdd:cd14077 163 YDPRRLLRTFCGSLYFAAPELLQAQPYTGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLSsECKS 242
                       250       260
                ....*....|....*....|....*
gi 27229182 283 LIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14077 243 LISRMLVVDPKKRATLEQVLNHPWM 267
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
63-304 3.23e-80

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: 253.98  E-value: 3.23e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd05123   1 LGKGSFGKVLLVRKkDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN-LYHKGKFLQTFCGSPLYA 220
Cdd:cd05123  81 FSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKeLSSDGDRTYTFCGTPEYL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 221 SPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-DACGLIRWLLMVNPTRR---A 296
Cdd:cd05123 161 APEVLLGKGY-GKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSpEAKSLISGLLQKDPTKRlgsG 239

                ....*...
gi 27229182 297 TLEDVASH 304
Cdd:cd05123 240 GAEEIKAH 247
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
57-307 3.78e-80

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: 254.14  E-value: 3.78e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14162   2 YIVGKTLGHGSYAVVKKAYsTKHKCKVAIKIVSKKKAPEDYLQKFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIMEL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHK-----GKFL 210
Cdd:cd14162  82 AENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGVMKtkdgkPKLS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 QTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNG-AYREPPKPSDAC-GLIRWLL 288
Cdd:cd14162 162 ETYCGSYAYASPEILRGIPYDPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQRRvVFPKNPTVSEECkDLILRML 241
                       250
                ....*....|....*....
gi 27229182 289 mVNPTRRATLEDVASHWWV 307
Cdd:cd14162 242 -SPVKKRITIEEIKRDPWF 259
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
57-307 1.47e-79

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: 252.33  E-value: 1.47e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIkDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14074   5 YDLEETLGRGHFAVVKLARHVfTGEKVAVKVIDKTKL-DDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILEL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL-DANGNIKIADFGLSNLYHKGKFLQTF 213
Cdd:cd14074  84 GDGGDMYDYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGEKLETS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPF-DGQDHKTLVKqISNGAYREPPKPSDAC-GLIRWLLMVN 291
Cdd:cd14074 164 CGSLAYSAPEILLGDEYDAPAVDIWSLGVILYMLVCGQPPFqEANDSETLTM-IMDCKYTVPAHVSPECkDLIRRMLIRD 242
                       250
                ....*....|....*.
gi 27229182 292 PTRRATLEDVASHWWV 307
Cdd:cd14074 243 PKKRASLEEIENHPWL 258
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
57-307 2.65e-79

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: 251.49  E-value: 2.65e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARESSGR-LVAIKSIRKDKIkDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14075   4 YRIRGELGSGNFSQVKLGIHQLTKeKVAIKILDKTKL-DQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCG 215
Cdd:cd14075  83 ASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGETLNTFCG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 216 SPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDACG-LIRWLLMVNPTR 294
Cdd:cd14075 163 SPPYAAPELFKDEHYIGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPSYVSEPCQeLIRGILQPVPSD 242
                       250
                ....*....|...
gi 27229182 295 RATLEDVASHWWV 307
Cdd:cd14075 243 RYSIDEIKNSEWL 255
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
55-306 5.51e-77

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: 245.54  E-value: 5.51e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  55 HRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd14099   1 KRYRRGKFLGKGGFAKCYEVTDmSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-NLYHKGKFLQT 212
Cdd:cd14099  81 ELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAaRLEYDGERKKT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKP--SDACG-LIRWLLM 289
Cdd:cd14099 161 LCGTPNYIAPEVLEKKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHLsiSDEAKdLIRSMLQ 240
                       250
                ....*....|....*..
gi 27229182 290 VNPTRRATLEDVASHWW 306
Cdd:cd14099 241 PDPTKRPSLDEILSHPF 257
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
56-305 2.31e-76

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: 243.91  E-value: 2.31e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIkDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRkSDGKLYVLKEIDLSNM-SEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPR----LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLY-HKGKF 209
Cdd:cd08215  80 YADGGDLAQKIKKQKKkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLeSTTDL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 210 LQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK--PSDACGLIRWL 287
Cdd:cd08215 160 AKTVVGTPYYLSPELCENKPY-NYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIPSqySSELRDLVNSM 238
                       250
                ....*....|....*...
gi 27229182 288 LMVNPTRRATLEDVASHW 305
Cdd:cd08215 239 LQKDPEKRPSANEILSSP 256
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
63-307 6.54e-75

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: 240.53  E-value: 6.54e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIK-----------DEQDLLHIRREIEIMSSLNHPHIIAIHEVFEN--SSK 128
Cdd:cd14008   1 LGRGSFGKVKLALdTETGQLYAIKIFNKSRLRkrregkndrgkIKNALDDVRREIAIMKKLDHPNIVRLYEVIDDpeSDK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IVIVMEYASRGDLYDYIS--ERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHK 206
Cdd:cd14008  81 LYLVLEYCEGGPVMELDSgdRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMFED 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 207 GK-FLQTFCGSPLYASPEI--VNGKPYVGPEVDSWSLGVLLYILVHGTMPFDG-----QDHKTlvkQISNGAYREPPKPS 278
Cdd:cd14008 161 GNdTLQKTAGTPAFLAPELcdGDSKTYSGKAADIWALGVTLYCLVFGRLPFNGdnileLYEAI---QNQNDEFPIPPELS 237
                       250       260       270
                ....*....|....*....|....*....|
gi 27229182 279 DAC-GLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14008 238 PELkDLLRRMLEKDPEKRITLKEIKEHPWV 267
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
63-304 7.42e-75

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: 238.71  E-value: 7.42e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd00180   1 LGKGSFGKVYKARdKETGKKVAVKVIPKEKLKKLLE--ELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERP-RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCG---SP 217
Cdd:cd00180  79 KDLLKENKgPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGgttPP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 218 LYASPEIVNGKPYvGPEVDSWSLGVLLYILvhgtmpfdgqdhktlvkqisngayreppkpSDACGLIRWLLMVNPTRRAT 297
Cdd:cd00180 159 YYAPPELLGGRYY-GPKVDIWSLGVILYEL------------------------------EELKDLIRRMLQYDPKKRPS 207

                ....*..
gi 27229182 298 LEDVASH 304
Cdd:cd00180 208 AKELLEH 214
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
63-306 9.23e-72

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: 231.73  E-value: 9.23e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKSI-RKDKIKDEQDLLhiRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGD 140
Cdd:cd14009   1 IGRGSFATVWKGRhKQTGEVVAIKEIsRKKLNKKLQENL--ESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 141 LYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN---IKIADFGLSNLYHKGKFLQTFCGSP 217
Cdd:cd14009  79 LSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFARSLQPASMAETLCGSP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 218 LYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQI-SNGAYREPPKPSDACG----LIRWLLMVNP 292
Cdd:cd14009 159 LYMAPEILQFQKY-DAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIeRSDAVIPFPIAAQLSPdckdLLRRLLRRDP 237
                       250
                ....*....|....
gi 27229182 293 TRRATLEDVASHWW 306
Cdd:cd14009 238 AERISFEEFFAHPF 251
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
56-306 8.02e-71

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: 230.05  E-value: 8.02e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIK-DEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd14098   1 KYQIIDRLGSGTFAEVKKAVEvETGKMRAIKQIVKRKVAgNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN--IKIADFGLSNLYHKGKFLQ 211
Cdd:cd14098  81 EYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPviVKISDFGLAKVIHTGTFLV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKPYVGPE-----VDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-----DAC 281
Cdd:cd14098 161 TFCGTMAYLAPEILMSKEQNLQGgysnlVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVDfniseEAI 240
                       250       260
                ....*....|....*....|....*
gi 27229182 282 GLIRWLLMVNPTRRATLEDVASHWW 306
Cdd:cd14098 241 DFILRLLDVDPEKRMTAAQALDHPW 265
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
57-306 2.76e-70

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: 228.51  E-value: 2.76e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIrkDKIKDEQDLLH--IRREIEIMSSLNHPHIIAIHEVFENSS-KIVIV 132
Cdd:cd14165   3 YILGINLGEGSYAKVKSAySERLKCNVAIKII--DKKKAPDDFVEkfLPRELEILARLNHKSIIKTYEIFETSDgKVYIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS---NLYHKGKF 209
Cdd:cd14165  81 MELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSkrcLRDENGRI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 210 L--QTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDAC---GLI 284
Cdd:cd14165 161 VlsKTFCGSAAYAAPEVLQGIPYDPRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSKNLTSeckDLI 240
                       250       260
                ....*....|....*....|..
gi 27229182 285 RWLLMVNPTRRATLEDVASHWW 306
Cdd:cd14165 241 YRLLQPDVSQRLCIDEVLSHPW 262
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
53-307 4.94e-70

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


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 228.05  E-value: 4.94e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLETLGKGTYGKVKKARESSGR-LVAIKSIRKDK-----IKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENS 126
Cdd:cd14084   4 LRKKYIMSRTLGSGACGEVKLAYDKSTCkKVAIKIINKRKftigsRREINKPRNIETEIEILKKLSHPCIIKIEDFFDAE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 127 SKIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN---IKIADFGLSNL 203
Cdd:cd14084  84 DDYYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeclIKITDFGLSKI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 204 YHKGKFLQTFCGSPLYASPEIVNGKPYVG--PEVDSWSLGVLLYILVHGTMPFDGQDHKTLVK-QISNGAYREPPK---- 276
Cdd:cd14084 164 LGETSLMKTLCGTPTYLAPEVLRSFGTEGytRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKeQILSGKYTFIPKawkn 243
                       250       260       270
                ....*....|....*....|....*....|..
gi 27229182 277 -PSDACGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14084 244 vSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
56-303 6.15e-70

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: 227.47  E-value: 6.15e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARdTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQT-- 212
Cdd:cd14014  81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTgs 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPP-----KPSDACGLIRWL 287
Cdd:cd14014 161 VLGTPAYMAPEQARGGP-VDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSplnpdVPPALDAIILRA 239
                       250
                ....*....|....*..
gi 27229182 288 LMVNPTRR-ATLEDVAS 303
Cdd:cd14014 240 LAKDPEERpQSAAELLA 256
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
57-307 7.00e-70

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: 227.75  E-value: 7.00e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVK------KARESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIV 130
Cdd:cd14076   3 YILGRTLGEGEFGKVKlgwplpKANHRSGVQVAIKLIRRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 IVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLY--HKGK 208
Cdd:cd14076  83 IVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFdhFNGD 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTFCGSPLYASPEIVNGK-PYVGPEVDSWSLGVLLYILVHGTMPFD-------GQDHKTLVKQISNGAYREP----PK 276
Cdd:cd14076 163 LMSTSCGSPCYAAPELVVSDsMYAGRKADIWSCGVILYAMLAGYLPFDddphnpnGDNVPRLYRYICNTPLIFPeyvtPK 242
                       250       260       270
                ....*....|....*....|....*....|.
gi 27229182 277 PSDacgLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14076 243 ARD---LLRRILVPNPRKRIRLSAIMRHAWL 270
Pkinase pfam00069
Protein kinase domain;
57-307 2.92e-69

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 224.05  E-value: 2.92e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182    57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLlHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHrDTGKIVAIKKIKKEKIKKKKDK-NILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   136 ASRGDLYDYISERPRLSERDARHFFRQIVSALhychqngivhrdlklenilldangnikiadfglsnlyHKGKFLQTFCG 215
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGL-------------------------------------ESGSSLTTFVG 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   216 SPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKP----SDACGLIRWLLMVN 291
Cdd:pfam00069 123 TPWYMAPEVLGGNPY-GPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPsnlsEEAKDLLKKLLKKD 201
                         250
                  ....*....|....*.
gi 27229182   292 PTRRATLEDVASHWWV 307
Cdd:pfam00069 202 PSKRLTATQALQHPWF 217
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-306 6.73e-69

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


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 224.56  E-value: 6.73e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHirREIEIMSSLNHPHIIAIHEVFENSSKIVI 131
Cdd:cd14083   1 IRDKYEFKEVLGTGAFSEVVLAEDkATGKLVAIKCIDKKALKGKEDSLE--NEIAVLRKIKHPNIVQLLDIYESKSHLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENIL---LDANGNIKIADFGLSNLYHKGk 208
Cdd:cd14083  79 VMELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSKMEDSG- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF-DGQDHKtLVKQISNGAYrEPPKP-----SD-AC 281
Cdd:cd14083 158 VMSTACGTPGYVAPEVLAQKPY-GKAVDCWSIGVISYILLCGYPPFyDENDSK-LFAQILKAEY-EFDSPywddiSDsAK 234
                       250       260
                ....*....|....*....|....*
gi 27229182 282 GLIRWLLMVNPTRRATLEDVASHWW 306
Cdd:cd14083 235 DFIRHLMEKDPNKRYTCEQALEHPW 259
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
55-303 4.15e-68

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: 223.25  E-value: 4.15e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  55 HRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd05581   1 NDFKFGKPLGEGSYSTVVLAKEkETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYH-------- 205
Cdd:cd05581  81 EYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGpdsspest 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 206 ----------KGKFLQTFCGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPP 275
Cdd:cd05581 161 kgdadsqiayNQARAASFVGTAEYVSPELLNEKP-AGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFPE 239
                       250       260
                ....*....|....*....|....*....
gi 27229182 276 K-PSDACGLIRWLLMVNPTRRATLEDVAS 303
Cdd:cd05581 240 NfPPDAKDLIQKLLVLDPSKRLGVNENGG 268
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
63-306 4.53e-68

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: 222.14  E-value: 4.53e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQdllhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd14006   1 LGRGRFGVVKRCIEkATGREFAAKFIPKRDKKKEA----VLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGEL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLD--ANGNIKIADFGLSNLYHKGKFLQTFCGSPLY 219
Cdd:cd14006  77 LDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLARKLNPGEELKEIFGTPEF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 220 ASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYR-EPPKPSD----ACGLIRWLLMVNPTR 294
Cdd:cd14006 157 VAPEIVNGEP-VSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDfSEEYFSSvsqeAKDFIRKLLVKEPRK 235
                       250
                ....*....|..
gi 27229182 295 RATLEDVASHWW 306
Cdd:cd14006 236 RPTAQEALQHPW 247
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
53-302 5.67e-67

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 226.82  E-value: 5.67e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVI 131
Cdd:COG0515   5 LLGRYRILRLLGRGGMGVVYLARdLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQ 211
Cdd:COG0515  85 VMEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQ 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 T--FCGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK-----PSDACGLI 284
Cdd:COG0515 165 TgtVVGTPGYMAPEQARGEP-VDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSElrpdlPPALDAIV 243
                       250
                ....*....|....*....
gi 27229182 285 RWLLMVNPTRR-ATLEDVA 302
Cdd:COG0515 244 LRALAKDPEERyQSAAELA 262
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
57-307 2.05e-66

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: 218.02  E-value: 2.05e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKI-----KDEQDLLHIRREIEIMSSLN---HPHIIAIHEVFENSS 127
Cdd:cd14004   2 YTILKEMGEGAYGQVNLAiYKSKGKEVVIKFIFKERIlvdtwVRDRKLGTVPLEIHILDTLNkrsHPNIVKLLDFFEDDE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 128 KIVIVMEYASRG-DLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHK 206
Cdd:cd14004  82 FYYLVMEKHGSGmDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAYIKS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 207 GKFlQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHktlvkqISNGAYREPPKPSDAC-GLIR 285
Cdd:cd14004 162 GPF-DTFVGTIDYAAPEVLRGNPYGGKEQDIWALGVLLYTLVFKENPFYNIEE------ILEADLRIPYAVSEDLiDLIS 234
                       250       260
                ....*....|....*....|..
gi 27229182 286 WLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14004 235 RMLNRDVGDRPTIEELLTDPWL 256
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
56-304 6.87e-66

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: 216.35  E-value: 6.87e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKdKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14002   2 NYHVLELIGEGSFGKVYKGRRKyTGQVVALKFIPK-RGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YAsRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-NLYHKGKFLQTF 213
Cdd:cd14002  81 YA-QGELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFArAMSCNTLVLTSI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDAC-GLIRWLLMVNP 292
Cdd:cd14002 160 KGTPLYMAPELVQEQPY-DHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFkSFLQGLLNKDP 238
                       250
                ....*....|..
gi 27229182 293 TRRATLEDVASH 304
Cdd:cd14002 239 SKRLSWPDLLEH 250
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
63-295 6.14e-64

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: 213.62  E-value: 6.14e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMS-SLNHPHIIAIHEVFENSSKIVIVMEYASRGD 140
Cdd:cd05570   3 LGKGSFGKVMLAeRKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLAlANRHPFLTGLHACFQTEDRLYFVMEYVNGGD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 141 LYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS--NLYHkGKFLQTFCGSPL 218
Cdd:cd05570  83 LMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCkeGIWG-GNTTSTFCGTPD 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27229182 219 YASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK-PSDACGLIRWLLMVNPTRR 295
Cdd:cd05570 162 YIAPEILREQDY-GFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWlSREAVSILKGLLTKDPARR 238
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
57-304 8.32e-64

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: 211.25  E-value: 8.32e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKD-EQDLLHIrrEIEIMSSLNHPHIIAI--HEVFENSSKIVIV 132
Cdd:cd08217   2 YEVLETIGKGSFGTVRKVrRKSDGKILVWKEIDYGKMSEkEKQQLVS--EVNILRELKHPNIVRYydRIVDRANTTLYIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYI----SERPRLSERDARHFFRQIVSALHYCH-----QNGIVHRDLKLENILLDANGNIKIADFGLS-N 202
Cdd:cd08217  80 MEYCEGGDLAQLIkkckKENQYIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDNNVKLGDFGLArV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 203 LYHKGKFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK--PSDA 280
Cdd:cd08217 160 LSHDSSFAKTYVGTPYYMSPELLNEQSY-DEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPRIPSrySSEL 238
                       250       260
                ....*....|....*....|....
gi 27229182 281 CGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd08217 239 NEVIKSMLNVDPDKRPSVEELLQL 262
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
65-309 8.43e-61

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: 203.60  E-value: 8.43e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  65 KGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDLYD 143
Cdd:cd05579   3 RGAYGRVYLAKkKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLYS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 144 YISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN--LYHKGKFLQ---------- 211
Cdd:cd05579  83 LLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKvgLVRRQIKLSiqkksngape 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 ----TFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS---DACGLI 284
Cdd:cd05579 163 kedrRIVGTPDYLAPEILLGQGH-GKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEDPEvsdEAKDLI 241
                       250       260       270
                ....*....|....*....|....*....|.
gi 27229182 285 RWLLMVNPTRRA---TLEDVASHWW---VNW 309
Cdd:cd05579 242 SKLLTPDPEKRLgakGIEEIKNHPFfkgIDW 272
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
56-307 9.82e-60

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: 200.16  E-value: 9.82e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARESSGRL-VAIKSIRKDKIKDEQDLLHIRR---EIEIM---SSLNHPHIIAIHEVFENSSK 128
Cdd:cd14005   1 QYEVGDLLGKGGFGTVYSGVRIRDGLpVAVKFVPKSRVTEWAMINGPVPvplEIALLlkaSKPGVPGVIRLLDWYERPDG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IVIVMEYASRG-DLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDAN-GNIKIADFGLSNLYHK 206
Cdd:cd14005  81 FLLIMERPEPCqDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRtGEVKLIDFGCGALLKD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 207 GKFlQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFdgqdHKTLvKQISNGAYREPPKPSDACGLIRW 286
Cdd:cd14005 161 SVY-TDFDGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGDIPF----ENDE-QILRGNVLFRPRLSKECCDLISR 234
                       250       260
                ....*....|....*....|.
gi 27229182 287 LLMVNPTRRATLEDVASHWWV 307
Cdd:cd14005 235 CLQFDPSKRPSLEQILSHPWF 255
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
56-306 2.14e-59

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


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 199.89  E-value: 2.14e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKA-RESSGRLVAIKSI-----RKDKIKDEQDLLHIRREIEIMSSLN-HPHIIAIHEVFENSSK 128
Cdd:cd14093   4 KYEPKEILGRGVSSTVRRCiEKETGQEFAVKIIditgeKSSENEAEELREATRREIEILRQVSgHPNIIELHDVFESPTF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGK 208
Cdd:cd14093  84 IFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTFCGSPLYASPEIV-----NGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYrEPPKP------ 277
Cdd:cd14093 164 KLRELCGTPGYLAPEVLkcsmyDNAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKY-EFGSPewddis 242
                       250       260
                ....*....|....*....|....*....
gi 27229182 278 SDACGLIRWLLMVNPTRRATLEDVASHWW 306
Cdd:cd14093 243 DTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
52-307 2.26e-59

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


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 199.64  E-value: 2.26e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  52 NLRHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQ---DLLHIRREIEIMSSLNHPHIIAIHEVFENSS 127
Cdd:cd14105   2 NVEDFYDIGEELGSGQFAVVKKCREkSTGLEYAAKFIKKRRSKASRrgvSREDIEREVSILRQVLHPNIITLHDVFENKT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 128 KIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENI-LLDAN---GNIKIADFGLSNL 203
Cdd:cd14105  82 DVVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENImLLDKNvpiPRIKLIDFGLAHK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 204 YHKGKFLQTFCGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAY----REPPKPSD 279
Cdd:cd14105 162 IEDGNEFKNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYdfddEYFSNTSE 240
                       250       260
                ....*....|....*....|....*....
gi 27229182 280 -ACGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14105 241 lAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
56-304 2.38e-59

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: 199.15  E-value: 2.38e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKA-RESSGRLVAIKSI--RKDKIKDEQDLLHirrEIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd08530   1 DFKVLKKLGKGSYGSVYKVkRLSDNQVYALKEVnlGSLSQKEREDSVN---EIRLLASVNHPNIIRYKEAFLDGNRLCIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISERPR----LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGk 208
Cdd:cd08530  78 MEYAPFGDLSKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKN- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTFCGSPLYASPEIVNGKPYVGPEvDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYrePPKPS----DACGLI 284
Cdd:cd08530 157 LAKTQIGTPLYAAPEVWKGRPYDYKS-DIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKF--PPIPPvysqDLQQII 233
                       250       260
                ....*....|....*....|
gi 27229182 285 RWLLMVNPTRRATLEDVASH 304
Cdd:cd08530 234 RSLLQVNPKKRPSCDKLLQS 253
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
63-307 2.61e-59

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: 199.02  E-value: 2.61e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARES-SGRLVAIKSIRKDKIKD----EQDllhIRREIEIMSSLNHPHIIAIHEVF--ENSSKIVIVMEY 135
Cdd:cd14119   1 LGEGSYGKVKEVLDTeTLCRRAVKILKKRKLRRipngEAN---VKREIQILRRLNHRNVIKLVDVLynEEKQKLYMVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASrGDLYDYISERP--RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS---NLYHKGKFL 210
Cdd:cd14119  78 CV-GGLQEMLDSAPdkRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAealDLFAEDDTC 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 QTFCGSPLYASPEIVNGKPYV-GPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK-PSDACGLIRWLL 288
Cdd:cd14119 157 TTSQGSPAFQPPEIANGQDSFsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDvDPDLQDLLRGML 236
                       250
                ....*....|....*....
gi 27229182 289 MVNPTRRATLEDVASHWWV 307
Cdd:cd14119 237 EKDPEKRFTIEQIRQHPWF 255
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
57-307 3.07e-59

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: 199.09  E-value: 3.07e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEqDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14069   3 WDLVQTLGEGAFGEVFLAvNRNTEEAVAVKFVDMKRAPGD-CPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLY-HKGK--FLQT 212
Cdd:cd14069  82 ASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFrYKGKerLLNK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTlvkqISNGAYREPPKP---------SDACGL 283
Cdd:cd14069 162 MCGTLPYVAPELLAKKKYRAEPVDVWSCGIVLFAMLAGELPWDQPSDSC----QEYSDWKENKKTyltpwkkidTAALSL 237
                       250       260
                ....*....|....*....|....
gi 27229182 284 IRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14069 238 LRKILTENPNKRITIEDIKKHPWY 261
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
57-307 1.36e-58

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: 197.04  E-value: 1.36e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIrkdKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd05122   2 FEILEKIGKGGFGVVYKARhKKTGQIVAIKKI---NLESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFC 214
Cdd:cd05122  79 CSGGSLKDLLKNTNKtLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTRNTFV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 215 GSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF-DGQDHKTLVKQISNGAY--REPPKPSD------ACGLIR 285
Cdd:cd05122 159 GTPYWMAPEVIQGKPY-GFKADIWSLGITAIEMAEGKPPYsELPPMKALFLIATNGPPglRNPKKWSKefkdflKKCLQK 237
                       250       260
                ....*....|....*....|..
gi 27229182 286 wllmvNPTRRATLEDVASHWWV 307
Cdd:cd05122 238 -----DPEKRPTAEQLLKHPFI 254
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
63-307 3.63e-58

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: 196.37  E-value: 3.63e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARES---SGRLVAIKSIRKDKiKDEQDLLHIRR---EIEIMSSLNHPHIIAIHEVFEN-SSKIVIVMEY 135
Cdd:cd13994   1 IGKGATSVVRIVTKKnprSGVLYAVKEYRRRD-DESKRKDYVKRltsEYIISSKLHHPNIVKVLDLCQDlHGKWCLVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQT--- 212
Cdd:cd13994  80 CPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMPAEKESpms 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 --FCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPF-----DGQDHKTLVKQ--ISNGAYrEPP---KPSDA 280
Cdd:cd13994 160 agLCGSEPYMAPEVFTSGSYDGRAVDVWSCGIVLFALFTGRFPWrsakkSDSAYKAYEKSgdFTNGPY-EPIenlLPSEC 238
                       250       260
                ....*....|....*....|....*..
gi 27229182 281 CGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd13994 239 RRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-308 5.44e-58

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: 196.75  E-value: 5.44e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLlhiRREIEIMSSLNHPHIIAIHEVFENSSKIVI 131
Cdd:cd14166   1 IRETFIFMEVLGSGAFSEVYLVKQrSTGKLYALKCIKKSPLSRDSSL---ENEIAVLKRIKHENIVTLEDIYESTTHYYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL---DANGNIKIADFGLSNLYHKGk 208
Cdd:cd14166  78 VMQLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSKMEQNG- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYR-EPPKPSD----ACGL 283
Cdd:cd14166 157 IMSTACGTPGYVAPEVLAQKPY-SKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEfESPFWDDisesAKDF 235
                       250       260
                ....*....|....*....|....*
gi 27229182 284 IRWLLMVNPTRRATLEDVASHWWVN 308
Cdd:cd14166 236 IRHLLEKNPSKRYTCEKALSHPWII 260
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
57-309 8.58e-58

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: 196.26  E-value: 8.58e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd05580   3 FEFLKTLGTGSFGRVRLVKhKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSnlyhkgKFL----Q 211
Cdd:cd05580  83 VPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFA------KRVkdrtY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDAC-GLIRWLLMV 290
Cdd:cd05580 157 TLCGTPEYLAPEIILSKGH-GKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAkDLIKRLLVV 235
                       250       260
                ....*....|....*....|....*..
gi 27229182 291 NPTRR-----ATLEDVASHWW---VNW 309
Cdd:cd05580 236 DLTKRlgnlkNGVEDIKNHPWfagIDW 262
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
63-306 1.01e-57

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: 194.75  E-value: 1.01e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDllhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd14103   1 LGRGKFGTVYRCVEkATGKELAAKFIKCRKAKDRED---VRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGEL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YD-YISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENIL-LDANGN-IKIADFGLSNLYHKGKFLQTFCGSPL 218
Cdd:cd14103  78 FErVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARKYDPDKKLKVLFGTPE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 219 YASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQ-DHKTLV--------------KQISngayreppkpSDACGL 283
Cdd:cd14103 158 FVAPEVVNYEP-ISYATDMWSVGVICYVLLSGLSPFMGDnDAETLAnvtrakwdfddeafDDIS----------DEAKDF 226
                       250       260
                ....*....|....*....|...
gi 27229182 284 IRWLLMVNPTRRATLEDVASHWW 306
Cdd:cd14103 227 ISKLLVKDPRKRMSAAQCLQHPW 249
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
56-307 1.98e-57

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: 195.33  E-value: 1.98e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKdEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14086   2 EYDLKEELGKGAFSVVRRCvQKSTGQEFAAKIINTKKLS-ARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL---DANGNIKIADFGLS---NLYHKGK 208
Cdd:cd14086  81 LVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAievQGDQQAW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FlqTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSD-----ACGL 283
Cdd:cd14086 161 F--GFAGTPGYLSPEVLRKDPY-GKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDtvtpeAKDL 237
                       250       260
                ....*....|....*....|....
gi 27229182 284 IRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14086 238 INQMLTVNPAKRITAAEALKHPWI 261
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
57-307 3.12e-57

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: 193.54  E-value: 3.12e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARESSGRL-VAIKSIrkDKIKDEQDLLH--IRREIEIMSSLNHPHIIAIHEVFENSSKIV-IV 132
Cdd:cd14164   2 YTLGTTIGEGSFSKVKLATSQKYCCkVAIKIV--DRRRASPDFVQkfLPRELSILRRVNHPNIVQMFECIEVANGRLyIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRgDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANG-NIKIADFGLSNLYHKGKFLQ 211
Cdd:cd14164  80 MEAAAT-DLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDYPELS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 -TFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDAC-GLIRWLLM 289
Cdd:cd14164 159 tTFCGSRAYTPPEVILGTPYDPKKYDVWSLGVVLYVMVTGTMPFDETNVRRLRLQQRGVLYPSGVALEEPCrALIRTLLQ 238
                       250
                ....*....|....*...
gi 27229182 290 VNPTRRATLEDVASHWWV 307
Cdd:cd14164 239 FNPSTRPSIQQVAGNSWL 256
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
56-306 5.40e-57

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: 192.93  E-value: 5.40e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLlhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14095   1 KYDIGRVIGDGNFAVVKECRDkATDKEYALKIIDKAKCKGKEHM--IENEVAILRRVKHPNIVQLIEEYDTDTELYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN----IKIADFGLSNlyHKGKFL 210
Cdd:cd14095  79 LVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDgsksLKLADFGLAT--EVKEPL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 QTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF--DGQDHKTLVKQISNGAYrEPPKPS------DACG 282
Cdd:cd14095 157 FTVCGTPTYVAPEILAETGY-GLKVDIWAAGVITYILLCGFPPFrsPDRDQEELFDLILAGEF-EFLSPYwdnisdSAKD 234
                       250       260
                ....*....|....*....|....
gi 27229182 283 LIRWLLMVNPTRRATLEDVASHWW 306
Cdd:cd14095 235 LISRMLVVDPEKRYSAGQVLDHPW 258
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-307 3.19e-56

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: 191.39  E-value: 3.19e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVI 131
Cdd:cd14167   1 IRDIYDFREVLGTGAFSEVVLAEEkRTQKLVAIKCIAKKALEGKET--SIENEIAVLHKIKHPNIVALDDIYESGGHLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENIL---LDANGNIKIADFGLSNLYHKGK 208
Cdd:cd14167  79 IMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKIEGSGS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYR-EPPKPSD----ACGL 283
Cdd:cd14167 159 VMSTACGTPGYVAPEVLAQKPY-SKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEfDSPYWDDisdsAKDF 237
                       250       260
                ....*....|....*....|....
gi 27229182 284 IRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14167 238 IQHLMEKDPEKRFTCEQALQHPWI 261
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
63-309 5.66e-56

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: 190.51  E-value: 5.66e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd05572   1 LGVGGFGRVELVQLkSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCGSPLYAS 221
Cdd:cd05572  81 WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGRKTWTFCGTPEYVA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 222 PEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLV--KQI--SNGAYREPPK-PSDACGLIRWLLMVNPTRR- 295
Cdd:cd05572 161 PEIILNKGY-DFSVDYWSLGILLYELLTGRPPFGGDDEDPMKiyNIIlkGIDKIEFPKYiDKNAKNLIKQLLRRNPEERl 239
                       250       260
                ....*....|....*....|.
gi 27229182 296 ----ATLEDVASHWW---VNW 309
Cdd:cd05572 240 gylkGGIRDIKKHKWfegFDW 260
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
61-307 9.38e-56

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: 190.25  E-value: 9.38e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKikDEQDLLH-IRREIEI-MSSLNHPHIIAIHEVFENSSKIVIVMEYAS 137
Cdd:cd14106  14 TPLGRGKFAVVRKCIHkETGKEYAAKFLRKRR--RGQDCRNeILHEIAVlELCKDCPRVVNLHEVYETRSELILILELAA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 138 RGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL---DANGNIKIADFGLSNLYHKGKFLQTFC 214
Cdd:cd14106  92 GGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtseFPLGDIKLCDFGISRVIGEGEEIREIL 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 215 GSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK-----PSDACGLIRWLLM 289
Cdd:cd14106 172 GTPDYVAPEILSYEP-ISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEElfkdvSPLAIDFIKRLLV 250
                       250
                ....*....|....*...
gi 27229182 290 VNPTRRATLEDVASHWWV 307
Cdd:cd14106 251 KDPEKRLTAKECLEHPWL 268
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
61-304 9.80e-56

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: 189.42  E-value: 9.80e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARESSG--RLVAIKSIRKDKIKDE--QDLLHirrEIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYA 136
Cdd:cd14121   1 EKLGSGTYATVYKAYRKSGarEVVAVKCVSKSSLNKAstENLLT---EIELLKKLKHPHIVELKDFQWDEEHIYLIMEYC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 137 SRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN--IKIADFGLSNLYHKGKFLQTFC 214
Cdd:cd14121  78 SGGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNpvLKLADFGFAQHLKPNDEAHSLR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 215 GSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQI-SNGAYREPPKP--SDAC-GLIRWLLMV 290
Cdd:cd14121 158 GSPLYMAPEMILKKKY-DARVDLWSVGVILYECLFGRAPFASRSFEELEEKIrSSKPIEIPTRPelSADCrDLLLRLLQR 236
                       250
                ....*....|....
gi 27229182 291 NPTRRATLEDVASH 304
Cdd:cd14121 237 DPDRRISFEEFFAH 250
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
61-307 1.33e-55

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: 189.27  E-value: 1.33e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQdLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRG 139
Cdd:cd06606   6 ELLGKGSFGSVYLALNlDTGELMAVKEVELSGDSEEE-LEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS---NLYHKGKFLQTFCGS 216
Cdd:cd06606  85 SLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAkrlAEIATGEGTKSLRGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 217 PLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF-DGQDHKTLVKQISNGayREPPK-----PSDACGLIRWLLMV 290
Cdd:cd06606 165 PYWMAPEVIRGEGY-GRAADIWSLGCTVIEMATGKPPWsELGNPVAALFKIGSS--GEPPPipehlSEEAKDFLRKCLQR 241
                       250
                ....*....|....*..
gi 27229182 291 NPTRRATLEDVASHWWV 307
Cdd:cd06606 242 DPKKRPTADELLQHPFL 258
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
63-309 1.37e-55

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: 191.42  E-value: 1.37e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd05571   3 LGKGTFGKVILCREkATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGGEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSnlyhK-----GKFLQTFCGS 216
Cdd:cd05571  83 FFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLC----KeeisyGATTKTFCGT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 217 PLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSD-ACGLIRWLLMVNPTRR 295
Cdd:cd05571 159 PEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPeAKSLLAGLLKKDPKKR 237
                       250       260
                ....*....|....*....|..
gi 27229182 296 -----ATLEDVASHWW---VNW 309
Cdd:cd05571 238 lgggpRDAKEIMEHPFfasINW 259
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
52-307 1.39e-55

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: 189.84  E-value: 1.39e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  52 NLRHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLL---HIRREIEIMSSLNHPHIIAIHEVFENSS 127
Cdd:cd14194   2 NVDDYYDTGEELGSGQFAVVKKCREkSTGLQYAAKFIKKRRTKSSRRGVsreDIEREVSILKEIQHPNVITLHEVYENKT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 128 KIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENI-LLDANG---NIKIADFGLSNL 203
Cdd:cd14194  82 DVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENImLLDRNVpkpRIKIIDFGLAHK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 204 YHKGKFLQTFCGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYR-EPPKPSDACG 282
Cdd:cd14194 162 IDFGNEFKNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEfEDEYFSNTSA 240
                       250       260
                ....*....|....*....|....*....
gi 27229182 283 L----IRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14194 241 LakdfIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
57-306 1.16e-54

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: 187.69  E-value: 1.16e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDE--QDLLhirREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKdKKTGEIVALKKIRLDNEEEGipSTAL---REISLLKELKHPNIVKLLDVIHTENKLYLVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRgDLYDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYhkgkflqt 212
Cdd:cd07829  78 EYCDQ-DLKKYLDKRPGpLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAF-------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 fcGSPL-----------YASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQI--------------- 266
Cdd:cd07829 149 --GIPLrtythevvtlwYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIfqilgtpteeswpgv 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27229182 267 -SNGAYRE-----PPKP---------SDACGLIRWLLMVNPTRRATLEDVASHWW 306
Cdd:cd07829 227 tKLPDYKPtfpkwPKNDlekvlprldPEGIDLLSKMLQYNPAKRISAKEALKHPY 281
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
57-301 1.29e-54

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: 186.46  E-value: 1.29e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSI--RKDKIKDEQDLLHirrEIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd08529   2 FEILNKLGKGSFGVVYKVvRKVDGRVYALKQIdiSRMSRKMREEAID---EARVLSKLNSPYVIKYYDSFVDKGKLNIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYI-SERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN-LYHKGKFL 210
Cdd:cd08529  79 EYAENGDLHSLIkSQRGRpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKiLSDTTNFA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 QTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYrePPKPS----DACGLIRW 286
Cdd:cd08529 159 QTIVGTPYYLSPELCEDKPY-NEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKY--PPISAsysqDLSQLIDS 235
                       250
                ....*....|....*
gi 27229182 287 LLMVNPTRRATLEDV 301
Cdd:cd08529 236 CLTKDYRQRPDTTEL 250
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
56-306 1.86e-54

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: 186.13  E-value: 1.86e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEqdllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14662   1 RYELVKDIGSGNFGVARLMRNkETKELVAVKYIERGLKIDE----NVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDAN--GNIKIADFGlsnlYHKGKFL-- 210
Cdd:cd14662  77 YAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpaPRLKICDFG----YSKSSVLhs 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 --QTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQD-----HKTlVKQISNGAYREPP--KPSDAC 281
Cdd:cd14662 153 qpKSTVGTPAYIAPEVLSRKEYDGKVADVWSCGVTLYVMLVGAYPFEDPDdpknfRKT-IQRIMSVQYKIPDyvRVSQDC 231
                       250       260
                ....*....|....*....|....*.
gi 27229182 282 G-LIRWLLMVNPTRRATLEDVASHWW 306
Cdd:cd14662 232 RhLLSRIFVANPAKRITIPEIKNHPW 257
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
57-307 2.34e-54

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: 186.63  E-value: 2.34e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHirREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14169   5 YELKEKLGEGAFSEVVLAQErGSQRLVALKCIPKKALRGKEAMVE--NEIAVLRRINHENIVSLEDIYESPTHLYLAMEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDA---NGNIKIADFGLSNLYHKGkFLQT 212
Cdd:cd14169  83 VTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDFGLSKIEAQG-MLST 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYR-EPPKPSD----ACGLIRWL 287
Cdd:cd14169 162 ACGTPGYVAPELLEQKPY-GKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEfDSPYWDDisesAKDFIRHL 240
                       250       260
                ....*....|....*....|
gi 27229182 288 LMVNPTRRATLEDVASHWWV 307
Cdd:cd14169 241 LERDPEKRFTCEQALQHPWI 260
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
56-307 1.15e-53

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


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 184.27  E-value: 1.15e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARESSGRL-VAIKSIRKDKIKDEQdllhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14087   2 KYDIKALIGRGSFSRVVRVEHRVTRQpYAIKMIETKCRGREV----CESELNVLRRVRHTNIIQLIEVFETKERVYMVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN---IKIADFGLSNLYHKGK--F 209
Cdd:cd14087  78 LATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLASTRKKGPncL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 210 LQTFCGSPLYASPEIVNGKPYVGpEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKP-SDACGL----I 284
Cdd:cd14087 158 MKTTCGTPEYIAPEILLRKPYTQ-SVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEPwPSVSNLakdfI 236
                       250       260
                ....*....|....*....|...
gi 27229182 285 RWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14087 237 DRLLTVNPGERLSATQALKHPWI 259
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
57-306 2.76e-53

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: 183.23  E-value: 2.76e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLlhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14185   2 YEIGRTIGDGNFAVVKECRHwNENQEYAMKIIDKSKLKGKEDM--IESEILIIKSLSHPNIVKLFEVYETEKEIYLILEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL----DANGNIKIADFGLSNLYHKGKFlq 211
Cdd:cd14185  80 VRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVTGPIF-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQ--DHKTLVKQISNGAYREPPKPSD-----ACGLI 284
Cdd:cd14185 158 TVCGTPTYVAPEILSEKGY-GLEVDMWAAGVILYILLCGFPPFRSPerDQEELFQIIQLGHYEFLPPYWDniseaAKDLI 236
                       250       260
                ....*....|....*....|..
gi 27229182 285 RWLLMVNPTRRATLEDVASHWW 306
Cdd:cd14185 237 SRLLVVDPEKRYTAKQVLQHPW 258
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
63-309 4.58e-53

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: 184.82  E-value: 4.58e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd05595   3 LGKGTFGKVILVREkATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL-YHKGKFLQTFCGSPLYA 220
Cdd:cd05595  83 FFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEgITDGATMKTFCGTPEYL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 221 SPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-DACGLIRWLLMVNPTRR---- 295
Cdd:cd05595 163 APEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSpEAKSLLAGLLKKDPKQRlggg 241
                       250
                ....*....|....*...
gi 27229182 296 -ATLEDVASHWW---VNW 309
Cdd:cd05595 242 pSDAKEVMEHRFflsINW 259
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
57-307 1.94e-52

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: 180.96  E-value: 1.94e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSS-KIVIVME 134
Cdd:cd14163   2 YQLGKTIGEGTYSKVKEAfSKKHQRKVAIKIIDKSGGPEEFIQRFLPRELQIVERLDHKNIIHVYEMLESADgKIYLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANgNIKIADFGLSNLYHKG--KFLQT 212
Cdd:cd14163  82 LAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGF-TLKLTDFGFAKQLPKGgrELSQT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQD-HKTLVKQISNGAYREPPKPSDAC-GLIRWLLMV 290
Cdd:cd14163 161 FCGSTAYAAPEVLQGVPHDSRKGDIWSMGVVLYVMLCAQLPFDDTDiPKMLCQQQKGVSLPGHLGVSRTCqDLLKRLLEP 240
                       250
                ....*....|....*..
gi 27229182 291 NPTRRATLEDVASHWWV 307
Cdd:cd14163 241 DMVLRPSIEEVSWHPWL 257
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
63-277 6.73e-52

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: 178.89  E-value: 6.73e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAReSSGRLVAIKSIRKDKiKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDLY 142
Cdd:cd13999   1 IGSGSFGEVYKGK-WRGTDVAIKKLKVED-DNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 143 DYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQT-FCGSPLYA 220
Cdd:cd13999  79 DLLHKkKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTgVVGTPRWM 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 27229182 221 SPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDhktlVKQISNGAYREPPKP 277
Cdd:cd13999 159 APEVLRGEPY-TEKADVYSFGIVLWELLTGEVPFKELS----PIQIAAAVVQKGLRP 210
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
62-307 6.97e-52

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: 179.63  E-value: 6.97e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  62 TLGKGTYGKVKKARES-SGRLVAIKSIRKDKIK-DEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRG 139
Cdd:cd14070   9 KLGEGSFAKVREGLHAvTGEKVAIKVIDKKKAKkDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPGG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHK---GKFLQTFCGS 216
Cdd:cd14070  89 NLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGIlgySDPFSTQCGS 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 217 PLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQ-------DHKTLVKQISngayrepPKPSD----ACGLIR 285
Cdd:cd14070 169 PAYAAPELLARKKY-GPKVDVWSIGVNMYAMLTGTLPFTVEpfslralHQKMVDKEMN-------PLPTDlspgAISFLR 240
                       250       260
                ....*....|....*....|..
gi 27229182 286 WLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14070 241 SLLEPDPLKRPNIKQALANRWL 262
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
56-306 7.15e-52

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: 179.41  E-value: 7.15e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSI-RKDKIkDEqdllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd14665   1 RYELVKDIGSGNFGVARLMRDkQTKELVAVKYIeRGEKI-DE----NVQREIINHRSLRHPNIVRFKEVILTPTHLAIVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANG--NIKIADFGlsnlYHKGKFL- 210
Cdd:cd14665  76 EYAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFG----YSKSSVLh 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 ---QTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPF----DGQDHKTLVKQISNGAYREPPK---PSDA 280
Cdd:cd14665 152 sqpKSTVGTPAYIAPEVLLKKEYDGKIADVWSCGVTLYVMLVGAYPFedpeEPRNFRKTIQRILSVQYSIPDYvhiSPEC 231
                       250       260
                ....*....|....*....|....*.
gi 27229182 281 CGLIRWLLMVNPTRRATLEDVASHWW 306
Cdd:cd14665 232 RHLISRIFVADPATRITIPEIRNHEW 257
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
57-306 1.32e-51

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: 178.60  E-value: 1.32e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARESSGRLV-AIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd05578   2 FQILRVIGKGSFGKVCIVQKKDTKKMfAMKYMNKQKCIEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCG 215
Cdd:cd05578  82 LLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTLATSTSG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 216 SPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKT----LVKQISNGAYREPPKPSDACGLIRWLLMVN 291
Cdd:cd05578 162 TKPYMAPEVFMRAGY-SFAVDWWSLGVTAYEMLRGKRPYEIHSRTSieeiRAKFETASVLYPAGWSEEAIDLINKLLERD 240
                       250
                ....*....|....*.
gi 27229182 292 PTRR-ATLEDVASHWW 306
Cdd:cd05578 241 PQKRlGDLSDLKNHPY 256
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-307 2.47e-51

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: 179.25  E-value: 2.47e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLETLGKGTYGKVKKARES-SGRLVAIKsirkdKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVI 131
Cdd:cd14085   1 LEDFFEIESELGRGATSVVYRCRQKgTQKPYAVK-----KLKKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN---IKIADFGLSNLYHKGK 208
Cdd:cd14085  76 VLELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSKIVDQQV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF-DGQDHKTLVKQISNGAYrEPPKP------SDAC 281
Cdd:cd14085 156 TMKTVCGTPGYCAPEILRGCAY-GPEVDMWSVGVITYILLCGFEPFyDERGDQYMFKRILNCDY-DFVSPwwddvsLNAK 233
                       250       260
                ....*....|....*....|....*.
gi 27229182 282 GLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14085 234 DLVKKLIVLDPKKRLTTQQALQHPWV 259
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
57-307 6.32e-51

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: 177.07  E-value: 6.32e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLL---HIRREIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd14196   7 YDIGEELGSGQFAIVKKCREkSTGLEYAAKFIKKRQSRASRRGVsreEIEREVSILRQVLHPNIITLHDVYENRTDVVLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENI-LLDANG---NIKIADFGLSNLYHKGK 208
Cdd:cd14196  87 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAHEIEDGV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTFCGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK----PSD-ACGL 283
Cdd:cd14196 167 EFKNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEffshTSElAKDF 245
                       250       260
                ....*....|....*....|....
gi 27229182 284 IRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14196 246 IRKLLVKETRKRLTIQEALRHPWI 269
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
57-307 8.52e-51

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: 176.69  E-value: 8.52e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARESSGRLV-AIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14116   7 FEIGRPLGKGKFGNVYLAREKQSKFIlALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEY 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSnLYHKGKFLQTFCG 215
Cdd:cd14116  87 APLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWS-VHAPSSRRTTLCG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 216 SPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSD-ACGLIRWLLMVNPTR 294
Cdd:cd14116 166 TLDYLPPEMIEGRMH-DEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEgARDLISRLLKHNPSQ 244
                       250
                ....*....|...
gi 27229182 295 RATLEDVASHWWV 307
Cdd:cd14116 245 RPMLREVLEHPWI 257
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
52-307 1.03e-50

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: 176.73  E-value: 1.03e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  52 NLRHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLL---HIRREIEIMSSLNHPHIIAIHEVFENSS 127
Cdd:cd14195   2 MVEDHYEMGEELGSGQFAIVRKCREkGTGKEYAAKFIKKRRLSSSRRGVsreEIEREVNILREIQHPNIITLHDIFENKT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 128 KIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENI-LLDANG---NIKIADFGLSNL 203
Cdd:cd14195  82 DVVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENImLLDKNVpnpRIKLIDFGIAHK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 204 YHKGKFLQTFCGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQIS--NGAYREP--PKPSD 279
Cdd:cd14195 162 IEAGNEFKNIFGTPEFVAPEIVNYEP-LGLEADMWSIGVITYILLSGASPFLGETKQETLTNISavNYDFDEEyfSNTSE 240
                       250       260
                ....*....|....*....|....*....
gi 27229182 280 -ACGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14195 241 lAKDFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
60-309 1.08e-50

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: 178.37  E-value: 1.08e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  60 LETLGKGTYGKV----KKARESSGRLVAIKSIRKDKI-KDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd05584   1 LKVLGKGGYGKVfqvrKTTGSDKGKIFAMKVLKKASIvRNQKDTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLILE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN-LYHKGKFLQTF 213
Cdd:cd05584  81 YLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKeSIHDGTVTHTF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-DACGLIRWLLMVNP 292
Cdd:cd05584 161 CGTIEYMAPEILTRSGH-GKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTnEARDLLKKLLKRNV 239
                       250       260
                ....*....|....*....|....*
gi 27229182 293 TRR--ATLED---VASHWW---VNW 309
Cdd:cd05584 240 SSRlgSGPGDaeeIKAHPFfrhINW 264
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
57-304 1.13e-50

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: 176.20  E-value: 1.13e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14186   3 FKVLNLLGKGSFACVYRARSlHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN---LYHKGKFlq 211
Cdd:cd14186  83 CHNGEMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATqlkMPHEKHF-- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-DACGLIRWLLMV 290
Cdd:cd14186 161 TMCGTPNYISPEIATRSAH-GLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSrEAQDLIHQLLRK 239
                       250
                ....*....|....
gi 27229182 291 NPTRRATLEDVASH 304
Cdd:cd14186 240 NPADRLSLSSVLDH 253
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
55-307 1.93e-50

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: 176.86  E-value: 1.93e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  55 HRYEFLETLGKGTYGKVKKA--RESSGRLVAIKSIRKDKIKDEQDL----LHIRREIEIMSSLNHPHIIAIHEVFENSSK 128
Cdd:cd14096   1 ENYRLINKIGEGAFSNVYKAvpLRNTGKPVAIKVVRKADLSSDNLKgssrANILKEVQIMKRLSHPNIVKLLDFQESDEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLD-------------------- 188
Cdd:cd14096  81 YYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEpipfipsivklrkadddetk 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 189 -------------ANGNIKIADFGLSNLYhKGKFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFD 255
Cdd:cd14096 161 vdegefipgvgggGIGIVKLADFGLSKQV-WDSNTKTPCGTVGYTAPEVVKDERY-SKKVDMWALGCVLYTLLCGFPPFY 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27229182 256 GQDHKTLVKQISNGAYrEPPKP------SDACGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14096 239 DESIETLTEKISRGDY-TFLSPwwdeisKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
52-307 2.35e-50

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: 176.78  E-value: 2.35e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  52 NLRHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIV 130
Cdd:cd14168   7 DIKKIFEFKEVLGTGAFSEVVLAEErATGKLFAVKCIPKKALKGKES--SIENEIAVLRKIKHENIVALEDIYESPNHLY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 IVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL---DANGNIKIADFGLSNLYHKG 207
Cdd:cd14168  85 LVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSKMEGKG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 208 KFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYR-EPPKPSD----ACG 282
Cdd:cd14168 165 DVMSTACGTPGYVAPEVLAQKPY-SKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEfDSPYWDDisdsAKD 243
                       250       260
                ....*....|....*....|....*
gi 27229182 283 LIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14168 244 FIRNLMEKDPNKRYTCEQALRHPWI 268
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
63-295 1.17e-49

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: 175.27  E-value: 1.17e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDL--LHIRREIEIMSSlNHPHIIAIHEVFENSSKIVIVMEYASRG 139
Cdd:cd05592   3 LGKGSFGKVMLAElKGTNQYFAIKALKKDVVLEDDDVecTMIERRVLALAS-QHPFLTHLFCTFQTESHLFFVMEYLNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL--SNLYHKGKfLQTFCGSP 217
Cdd:cd05592  82 DLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMckENIYGENK-ASTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 218 LYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNgayREP--PK--PSDACGLIRWLLMVNPT 293
Cdd:cd05592 161 DYIAPEILKGQKY-NQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICN---DTPhyPRwlTKEAASCLSLLLERNPE 236

                ..
gi 27229182 294 RR 295
Cdd:cd05592 237 KR 238
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
56-305 1.58e-49

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: 173.31  E-value: 1.58e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKD----KIKDEQDLLHIRREIEIMSSL-NHPHIIAIHEVFENSSKI 129
Cdd:cd13993   1 RYQLISPIGEGAYGVVYLAVDLrTGRKYAIKCLYKSgpnsKDGNDFQKLPQLREIDLHRRVsRHPNIITLHDVFETEVAI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 130 VIVMEYASRGDLYDYISERPR--LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDAN-GNIKIADFGLSNlyhK 206
Cdd:cd13993  81 YIVLEYCPNGDLFEAITENRIyvGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGLAT---T 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 207 GKFLQTF-CGSPLYASPEIVNGKPYVGPE-----VDSWSLGVLLYILVHGTMPF------------DGQDHKTLVKQIsn 268
Cdd:cd13993 158 EKISMDFgVGSEFYMAPECFDEVGRSLKGypcaaGDIWSLGIILLNLTFGRNPWkiasesdpifydYYLNSPNLFDVI-- 235
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 27229182 269 gayrePPKPSDACGLIRWLLMVNPTRRATLEDVASHW 305
Cdd:cd13993 236 -----LPMSDDFYNLLRQIFTVNPNNRILLPELQLLV 267
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
48-295 3.30e-49

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: 175.27  E-value: 3.30e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  48 HHKHNLRHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENS 126
Cdd:cd05593   8 HHKRKTMNDFDYLKLLGKGTFGKVILVREkASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 127 SKIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL-YH 205
Cdd:cd05593  88 DRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgIT 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 206 KGKFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK-PSDACGLI 284
Cdd:cd05593 168 DAATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTlSADAKSLL 246
                       250
                ....*....|.
gi 27229182 285 RWLLMVNPTRR 295
Cdd:cd05593 247 SGLLIKDPNKR 257
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
63-295 4.71e-49

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: 173.94  E-value: 4.71e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMS-SLNHPHIIAIHEVFENSSKIVIVMEYASRGD 140
Cdd:cd05590   3 LGKGSFGKVMLARlKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSlARNHPFLTQLYCCFQTPDRLFFVMEFVNGGD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 141 LYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL-SNLYHKGKFLQTFCGSPLY 219
Cdd:cd05590  83 LMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMcKEGIFNGKTTSTFCGTPDY 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27229182 220 ASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-DACGLIRWLLMVNPTRR 295
Cdd:cd05590 163 IAPEILQEMLY-GPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSqDAVDILKAFMTKNPTMR 238
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
55-304 6.89e-49

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: 172.08  E-value: 6.89e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  55 HRYEFLETLGKGTYGKVKKA-RESSGRLVAIK--SIRKDKIKDEQdLLHIR----REIEIMSSL-NHPHIIAIHEVFENS 126
Cdd:cd14181  10 QKYDPKEVIGRGVSSVVRRCvHRHTGQEFAVKiiEVTAERLSPEQ-LEEVRsstlKEIHILRQVsGHPSIITLIDSYESS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 127 SKIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHK 206
Cdd:cd14181  89 TFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEP 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 207 GKFLQTFCGSPLYASPEIVN-----GKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYR--EPP---K 276
Cdd:cd14181 169 GEKLRELCGTPGYLAPEILKcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQfsSPEwddR 248
                       250       260
                ....*....|....*....|....*...
gi 27229182 277 PSDACGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd14181 249 SSTVKDLISRLLVVDPEIRLTAEQALQH 276
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
57-309 9.54e-49

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: 173.62  E-value: 9.54e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd05573   3 FEVIKVIGRGAFGEVWLVRDKdTGQVYAMKILRKSDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGK------- 208
Cdd:cd05573  83 MPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNKSGdresyln 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 -----------------------FLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQ 265
Cdd:cd05573 163 dsvntlfqdnvlarrrphkqrrvRAYSAVGTPDYIAPEVLRGTGY-GPECDWWSLGVILYEMLYGFPPFYSDSLVETYSK 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 27229182 266 ISNgaYRE-------PPKPSDACGLIRWLLMVNPTRRATLEDVASHWW---VNW 309
Cdd:cd05573 242 IMN--WKEslvfpddPDVSPEAIDLIRRLLCDPEDRLGSAEEIKAHPFfkgIDW 293
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
58-301 1.24e-48

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 170.40  E-value: 1.24e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182     58 EFLETLGKGTYGKVKKAR-----ESSGRLVAIKSIRKDKikDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKlkgkgGKKKVEVAVKTLKEDA--SEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182    133 MEYASRGDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-NLYHKGKFL 210
Cdd:smart00219  80 MEYMEGGDLLSYLRKnRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSrDLYDDDYYR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182    211 QTFCGSPL-YASPEIVNGKPYvGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAYREPPK--PSDACGLIRW 286
Cdd:smart00219 160 KRGGKLPIrWMAPESLKEGKF-TSKSDVWSFGVLLWeIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPPncPPELYDLMLQ 238
                          250
                   ....*....|....*
gi 27229182    287 LLMVNPTRRATLEDV 301
Cdd:smart00219 239 CWAEDPEDRPTFSEL 253
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
57-309 1.43e-48

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: 171.43  E-value: 1.43e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14209   3 FDRIKTLGTGSFGRVMLVRHkETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYhKGKfLQTFCG 215
Cdd:cd14209  83 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRV-KGR-TWTLCG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 216 SPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK-PSDACGLIRWLLMVNPTR 294
Cdd:cd14209 161 TPEYLAPEIILSKGY-NKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHfSSDLKDLLRNLLQVDLTK 239
                       250       260
                ....*....|....*....|...
gi 27229182 295 R-----ATLEDVASHWW---VNW 309
Cdd:cd14209 240 RfgnlkNGVNDIKNHKWfatTDW 262
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
63-295 1.92e-48

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: 170.27  E-value: 1.92e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKV----KKARESSGRLVAIKSIRKDKIKDEQDLL-HIRREIEIMSSLNH-PHIIAIHEVFENSSKIVIVMEYA 136
Cdd:cd05583   2 LGTGAYGKVflvrKVGGHDAGKLYAMKVLKKATIVQKAKTAeHTMTERQVLEAVRQsPFLVTLHYAFQTDAKLHLILDYV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 137 SRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLY--HKGKFLQTFC 214
Cdd:cd05583  82 NGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFlpGENDRAYSFC 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 215 GSPLYASPEIVNGKPY-VGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGA-YREPPKPS----DACGLIRWLL 288
Cdd:cd05583 162 GTIEYMAPEVVRGGSDgHDKAVDWWSLGVLTYELLTGASPFTVDGERNSQSEISKRIlKSHPPIPKtfsaEAKDFILKLL 241

                ....*..
gi 27229182 289 MVNPTRR 295
Cdd:cd05583 242 EKDPKKR 248
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
60-295 4.06e-48

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: 171.04  E-value: 4.06e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  60 LETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPH-IIAIHEVFENSSKIVIVMEYAS 137
Cdd:cd05587   1 LMVLGKGSFGKVMLAeRKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLALSGKPPfLTQLHSCFQTMDRLYFVMEYVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 138 RGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL--SNLYhKGKFLQTFCG 215
Cdd:cd05587  81 GGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMckEGIF-GGKTTRTFCG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 216 SPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-DACGLIRWLLMVNPTR 294
Cdd:cd05587 160 TPDYIAPEIIAYQPY-GKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSkEAVSICKGLLTKHPAK 238

                .
gi 27229182 295 R 295
Cdd:cd05587 239 R 239
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
57-307 6.11e-48

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: 169.74  E-value: 6.11e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKiKDEQDllhirrEIEIMSSL-NHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14091   2 YEIKEEIGKGSYSVCKRCIhKATGKEYAVKIIDKSK-RDPSE------EIEILLRYgQHPNIITLRDVYDDGNSVYLVTE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL-DANGN---IKIADFGLS-NLYHKGKF 209
Cdd:cd14091  75 LLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYaDESGDpesLRICDFGFAkQLRAENGL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 210 LQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKT---LVKQISNGAYREPPK-----PSDAC 281
Cdd:cd14091 155 LMTPCYTANFVAPEVLKKQGY-DAACDIWSLGVLLYTMLAGYTPFASGPNDTpevILARIGSGKIDLSGGnwdhvSDSAK 233
                       250       260
                ....*....|....*....|....*.
gi 27229182 282 GLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14091 234 DLVRKMLHVDPSQRPTAAQVLQHPWI 259
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
61-306 1.34e-47

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: 167.85  E-value: 1.34e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKA-RESSGRLVAIKSIRkdkikdeqDLLHIRREIEI-MSSLNHPHIIAIHEVFENSSK----IVIVME 134
Cdd:cd14089   7 QVLGLGINGKVLECfHKKTGEKFALKVLR--------DNPKARREVELhWRASGCPHIVRIIDVYENTYQgrkcLLVVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPR--LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN---IKIADFGLSNLYHKGKF 209
Cdd:cd14089  79 CMEGGELFSRIQERADsaFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPnaiLKLTDFGFAKETTTKKS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 210 LQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDH----KTLVKQISNGAYrEPPKP------SD 279
Cdd:cd14089 159 LQTPCYTPYYVAPEVLGPEKY-DKSCDMWSLGVIMYILLCGYPPFYSNHGlaisPGMKKRIRNGQY-EFPNPewsnvsEE 236
                       250       260
                ....*....|....*....|....*..
gi 27229182 280 ACGLIRWLLMVNPTRRATLEDVASHWW 306
Cdd:cd14089 237 AKDLIRGLLKTDPSERLTIEEVMNHPW 263
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
58-297 2.60e-47

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: 166.96  E-value: 2.60e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182     58 EFLETLGKGTYGKVKKAR-----ESSGRLVAIKSIRKDKIKDEQDLLhiRREIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTlkgkgDGKEVEVAVKTLKEDASEQQIEEF--LREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182    133 MEYASRGDLYDYI--SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-NLYHKGKF 209
Cdd:smart00221  80 MEYMPGGDLLDYLrkNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSrDLYDDDYY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182    210 LQTFCGSPL-YASPEIVNGKPYvGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAYREPPK--PSDACGLIR 285
Cdd:smart00221 160 KVKGGKLPIrWMAPESLKEGKF-TSKSDVWSFGVLLWeIFTLGEEPYPGMSNAEVLEYLKKGYRLPKPPncPPELYKLML 238
                          250
                   ....*....|..
gi 27229182    286 WLLMVNPTRRAT 297
Cdd:smart00221 239 QCWAEDPEDRPT 250
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
61-308 2.73e-47

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: 168.63  E-value: 2.73e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARE-SSGRLVAIK--SIRKDkikdeqdllhIRREIEIMSSL-NHPHIIAIHEVFENSSKIVIVMEYA 136
Cdd:cd14092  12 EALGDGSFSVCRKCVHkKTGQEFAVKivSRRLD----------TSREVQLLRLCqGHPNIVKLHEVFQDELHTYLVMELL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 137 SRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL---DANGNIKIADFGLSNLYHKGKFLQTF 213
Cdd:cd14092  82 RGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGFARLKPENQPLKTP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CGSPLYASPEIVNGKPYVG---PEVDSWSLGVLLYILVHGTMPFDGQDHKT----LVKQISNGAYR---EPPKP--SDAC 281
Cdd:cd14092 162 CFTLPYAAPEVLKQALSTQgydESCDLWSLGVILYTMLSGQVPFQSPSRNEsaaeIMKRIKSGDFSfdgEEWKNvsSEAK 241
                       250       260
                ....*....|....*....|....*..
gi 27229182 282 GLIRWLLMVNPTRRATLEDVASHWWVN 308
Cdd:cd14092 242 SLIQGLLTVDPSKRLTMSELRNHPWLQ 268
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
63-304 3.01e-47

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: 166.78  E-value: 3.01e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR--ESSGRLVAIKSIRKDKIKDEQDLLhiRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGD 140
Cdd:cd14120   1 IGHGAFAVVFKGRhrKKPDLPVAIKCITKKNLSKSQNLL--GKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 141 LYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN---------IKIADFGLSNLYHKGKFLQ 211
Cdd:cd14120  79 LADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGrkpspndirLKIADFGFARFLQDGMMAA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKPYVGpEVDSWSLGVLLYILVHGTMPFDG---QDHKTLVKQISNGAYREPPKPSDAC-GLIRWL 287
Cdd:cd14120 159 TLCGSPMYMAPEVIMSLQYDA-KADLWSIGTIVYQCLTGKAPFQAqtpQELKAFYEKNANLRPNIPSGTSPALkDLLLGL 237
                       250
                ....*....|....*..
gi 27229182 288 LMVNPTRRATLEDVASH 304
Cdd:cd14120 238 LKRNPKDRIDFEDFFSH 254
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
61-306 3.31e-47

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: 166.82  E-value: 3.31e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKI--KDEQDLlhiRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEyAS 137
Cdd:cd14082   9 EVLGSGQFGIVYGGkHRKTGRDVAIKVIDKLRFptKQESQL---RNEVAILQQLSHPGVVNLECMFETPERVFVVME-KL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 138 RGDLYDYI--SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN---IKIADFGLSNLYHKGKFLQT 212
Cdd:cd14082  85 HGDMLEMIlsSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPfpqVKLCDFGFARIIGEKSFRRS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDgqDHKTLVKQISNGAYREPPKP-----SDACGLIRWL 287
Cdd:cd14082 165 VVGTPAYLAPEVLRNKGY-NRSLDMWSVGVIIYVSLSGTFPFN--EDEDINDQIQNAAFMYPPNPwkeisPDAIDLINNL 241
                       250
                ....*....|....*....
gi 27229182 288 LMVNPTRRATLEDVASHWW 306
Cdd:cd14082 242 LQVKMRKRYSVDKSLSHPW 260
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
57-304 5.07e-47

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: 166.23  E-value: 5.07e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKikdeQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd06614   2 YKNLEKIGEGASGEVYKATDRaTGKEVAIKKMRLRK----QNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERP-RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQ-TF 213
Cdd:cd06614  78 MDGGSLTDIITQNPvRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRnSV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAyrePPKPSDA-------CGLIRW 286
Cdd:cd06614 158 VGTPYWMAPEVIKRKDY-GPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKG---IPPLKNPekwspefKDFLNK 233
                       250
                ....*....|....*...
gi 27229182 287 LLMVNPTRRATLEDVASH 304
Cdd:cd06614 234 CLVKDPEKRPSAEELLQH 251
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
63-295 6.99e-47

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: 168.05  E-value: 6.99e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMS-SLNHPHIIAIHEVFENSSKIVIVMEYASRGD 140
Cdd:cd05591   3 LGKGSFGKVMLAeRKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILAlAAKHPFLTALHSCFQTKDRLFFVMEYVNGGD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 141 LYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL-YHKGKFLQTFCGSPLY 219
Cdd:cd05591  83 LMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgILNGKTTTTFCGTPDY 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27229182 220 ASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-DACGLIRWLLMVNPTRR 295
Cdd:cd05591 163 IAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSkEAVSILKAFMTKNPAKR 238
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
57-307 7.01e-47

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: 166.19  E-value: 7.01e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARESSGR-LVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14117   8 FDIGRPLGKGKFGNVYLAREKQSKfIVALKVLFKSQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSnLYHKGKFLQTFCG 215
Cdd:cd14117  88 APRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWS-VHAPSLRRRTMCG 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 216 SPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK-PSDACGLIRWLLMVNPTR 294
Cdd:cd14117 167 TLDYLPPEMIEGRTH-DEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFlSDGSRDLISKLLRYHPSE 245
                       250
                ....*....|...
gi 27229182 295 RATLEDVASHWWV 307
Cdd:cd14117 246 RLPLKGVMEHPWV 258
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
55-295 1.05e-46

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: 168.67  E-value: 1.05e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  55 HRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd05594  25 NDFEYLKLLGKGTFGKVILVKEkATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVM 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCH-QNGIVHRDLKLENILLDANGNIKIADFGLSNLYHK-GKFLQ 211
Cdd:cd05594 105 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKdGATMK 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-DACGLIRWLLMV 290
Cdd:cd05594 185 TFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSpEAKSLLSGLLKK 263

                ....*
gi 27229182 291 NPTRR 295
Cdd:cd05594 264 DPKQR 268
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
58-304 1.48e-46

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: 164.98  E-value: 1.48e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182    58 EFLETLGKGTYGKVKKAR-----ESSGRLVAIKSIRKDKikDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGTlkgegENTKIKVAVKTLKEGA--DEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   133 MEYASRGDLYDYI-SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-NLYHKGKFL 210
Cdd:pfam07714  80 TEYMPGGDLLDFLrKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSrDIYDDDYYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   211 QTfCGSPL---YASPE-IVNGKPYVgpEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGaYRePPKPSDAC---- 281
Cdd:pfam07714 160 KR-GGGKLpikWMAPEsLKDGKFTS--KSDVWSFGVLLWeIFTLGEQPYPGMSNEEVLEFLEDG-YR-LPQPENCPdely 234
                         250       260
                  ....*....|....*....|...
gi 27229182   282 GLIRWLLMVNPTRRATLEDVASH 304
Cdd:pfam07714 235 DLMKQCWAYDPEDRPTFSELVED 257
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
57-295 1.92e-46

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: 166.71  E-value: 1.92e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMS-SLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd05616   2 FNFLMVLGKGSFGKVMLAeRKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLAlSGKPPFLTQLHSCFQTMDRLYFVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL--SNLYhKGKFLQT 212
Cdd:cd05616  82 YVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMckENIW-DGVTTKT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQI--SNGAYrepPK--PSDACGLIRWLL 288
Cdd:cd05616 161 FCGTPDYIAPEIIAYQPY-GKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSImeHNVAY---PKsmSKEAVAICKGLM 236

                ....*..
gi 27229182 289 MVNPTRR 295
Cdd:cd05616 237 TKHPGKR 243
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
63-307 1.98e-46

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: 165.23  E-value: 1.98e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLL--------------------HIRREIEIMSSLNHPHIIAIHE 121
Cdd:cd14118   2 IGKGSYGIVKLAyNEEDNTLYAMKILSKKKLLKQAGFFrrppprrkpgalgkpldpldRVYREIAILKKLDHPNVVKLVE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 122 VFE--NSSKIVIVMEYASRGDLYDYISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFG 199
Cdd:cd14118  82 VLDdpNEDNLYMVFELVDKGAVMEVPTDNP-LSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 200 LSNLYHKGK-FLQTFCGSPLYASPEIV--NGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK 276
Cdd:cd14118 161 VSNEFEGDDaLLSSTAGTPAFMAPEALseSRKKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFPDD 240
                       250       260       270
                ....*....|....*....|....*....|....
gi 27229182 277 PSDACGL---IRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14118 241 PVVSEQLkdlILRMLDKNPSERITLPEIKEHPWV 274
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
56-304 2.03e-46

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: 164.52  E-value: 2.03e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARESSGR-LVAIKSIRKDKIKDEQDLlHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd08220   1 KYEKIRVVGRGAYGTVYLCRRKDDNkLVIIKQIPVEQMTKEERQ-AALNEVKVLSMLHHPNIIEYYESFLEDKALMIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPR--LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNI-KIADFGLSNLYHKGKFLQ 211
Cdd:cd08220  80 YAPGGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISKILSSKSKAY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKPYVgPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYrEPPKPS---DACGLIRWLL 288
Cdd:cd08220 160 TVVGTPCYISPELCEGKPYN-QKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTF-APISDRyseELRHLILSML 237
                       250
                ....*....|....*.
gi 27229182 289 MVNPTRRATLEDVASH 304
Cdd:cd08220 238 HLDPNKRPTLSEIMAQ 253
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
56-307 2.13e-46

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


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 164.68  E-value: 2.13e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIrkdKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14114   3 HYDILEELGTGAFGVVHRCTErATGNNFAAKFI---MTPHESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYIS-ERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDA--NGNIKIADFGLSNLYHKGKFLQ 211
Cdd:cd14114  80 FLSGGELFERIAaEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTkrSNEVKLIDFGLATHLDPKESVK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQ-DHKTL--VK----QISNGAYREPPKpsDACGLI 284
Cdd:cd14114 160 VTTGTAEFAAPEIVEREP-VGFYTDMWAVGVLSYVLLSGLSPFAGEnDDETLrnVKscdwNFDDSAFSGISE--EAKDFI 236
                       250       260
                ....*....|....*....|...
gi 27229182 285 RWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14114 237 RKLLLADPNKRMTIHQALEHPWL 259
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
57-306 2.69e-46

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: 163.94  E-value: 2.69e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDLlhirREIEIMSSLN----HPHIIAIHEVFE--NSSKI 129
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKvTGEKVAIKKIKNDFRHPKAAL----REIKLLKHLNdvegHPNIVKLLDVFEhrGGNHL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 130 VIVMEYASRgDLYDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLD-ANGNIKIADFGLSNLYHkG 207
Cdd:cd05118  77 CLVFELMGM-NLYELIKDYPRgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLADFGLARSFT-S 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 208 KFLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQIsngayREPPKPSDACGLIRWL 287
Cdd:cd05118 155 PPYTPYVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKI-----VRLLGTPEALDLLSKM 229
                       250
                ....*....|....*....
gi 27229182 288 LMVNPTRRATLEDVASHWW 306
Cdd:cd05118 230 LKYDPAKRITASQALAHPY 248
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
56-308 3.26e-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: 165.44  E-value: 3.26e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIR--REIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd07841   1 RYEKGKKLGEGTYAVVYKARDkETGRIVAIKKIKLGERKEAKDGINFTalREIKLLQELKHPNIIGLLDVFGHKSNINLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASrGDLYDYISER-PRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSnlyhkgkflq 211
Cdd:cd07841  81 FEFME-TDLEKVIKDKsIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLA---------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSP-----------LYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISN-----------G 269
Cdd:cd07841 150 RSFGSPnrkmthqvvtrWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEalgtpteenwpG 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27229182 270 AYREP---------PKP---------SDACGLIRWLLMVNPTRRATLEDVASH-WWVN 308
Cdd:cd07841 230 VTSLPdyvefkpfpPTPlkqifpaasDDALDLLQRLLTLNPNKRITARQALEHpYFSN 287
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
57-304 4.17e-46

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: 164.66  E-value: 4.17e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRrEIEIMSSLNHPHIIAIHEV------FENSSKI 129
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNkKTGELVALKKIRMENEKEGFPITAIR-EIKLLQKLDHPNVVRLKEIvtskgsAKYKGSI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 130 VIVMEYASRgDLYDYISERP-RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGK 208
Cdd:cd07840  80 YMVFEYMDH-DLTGLLDNPEvKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYTKEN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 flqtfcGSPL--------YASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQI-------------- 266
Cdd:cd07840 159 ------NADYtnrvitlwYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIfelcgspteenwpg 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 27229182 267 -SNGAYREPPKP-----------------SDACGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd07840 233 vSDLPWFENLKPkkpykrrlrevfknvidPSALDLLDKLLTLDPKKRISADQALQH 288
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
56-304 4.20e-46

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: 164.32  E-value: 4.20e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARESSGR---LVAIKSIRKDKIKDEQDLLHIR----REIEIMSSLN-HPHIIAIHEVFENSS 127
Cdd:cd14182   4 KYEPKEILGRGVSSVVRRCIHKPTRqeyAVKIIDITGGGSFSPEEVQELReatlKEIDILRKVSgHPNIIQLKDTYETNT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 128 KIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKG 207
Cdd:cd14182  84 FFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 208 KFLQTFCGSPLYASPEIV-----NGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYR----EPPKPS 278
Cdd:cd14182 164 EKLREVCGTPGYLAPEIIecsmdDNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQfgspEWDDRS 243
                       250       260
                ....*....|....*....|....*..
gi 27229182 279 DAC-GLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd14182 244 DTVkDLISRFLVVQPQKRYTAEEALAH 270
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
57-307 8.55e-46

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


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 163.10  E-value: 8.55e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14097   3 YTFGRKLGQGSFGVVIEATHkETQTKWAIKKINREKAGSSAVKL-LEREVDILKHVNHAHIIHLEEVFETPKRMYLVMEL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANG-------NIKIADFGLSNLYHKG- 207
Cdd:cd14097  82 CEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLSVQKYGLg 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 208 -KFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREP----PKPSDAC- 281
Cdd:cd14097 162 eDMLQETCGTPIYMAPEVISAHGY-SQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTqsvwQSVSDAAk 240
                       250       260
                ....*....|....*....|....*.
gi 27229182 282 GLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14097 241 NVLQQLLKVDPAHRMTASELLDNPWI 266
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
61-304 1.01e-45

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: 162.71  E-value: 1.01e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKAR----ESSGRLVAIKSIRKDKIKDEQ-DLLhirREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd00192   1 KKLGEGAFGEVYKGKlkggDGKTVDVAVKTLKEDASESERkDFL---KEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYI---------SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHK 206
Cdd:cd00192  78 MEGGDLLDFLrksrpvfpsPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 207 GKFLQTFCGSPL---YASPEIVNGKPYvGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGaYRePPKPSDACG 282
Cdd:cd00192 158 DDYYRKKTGGKLpirWMAPESLKDGIF-TSKSDVWSFGVLLWeIFTLGATPYPGLSNEEVLEYLRKG-YR-LPKPENCPD 234
                       250       260
                ....*....|....*....|....*..
gi 27229182 283 LIrWLLMV-----NPTRRATLEDVASH 304
Cdd:cd00192 235 EL-YELMLscwqlDPEDRPTFSELVER 260
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
63-307 1.59e-45

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: 162.80  E-value: 1.59e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKA-RESSGRLVAIKSIRKDKiKDEQDLLHIRREIEIMS-SLNHPHIIAIHEVFENSSKIVIVMEYASRGD 140
Cdd:cd14197  17 LGRGKFAVVRKCvEKDSGKEFAAKFMRKRR-KGQDCRMEIIHEIAVLElAQANPWVINLHEVYETASEMILVLEYAAGGE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 141 LYDY-ISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDAN---GNIKIADFGLSNLYHKGKFLQTFCG 215
Cdd:cd14197  96 IFNQcVADREEaFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRILKNSEELREIMG 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 216 SPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQIS--NGAYREPP---KPSDACGLIRWLLMV 290
Cdd:cd14197 176 TPEYVAPEILSYEP-ISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISqmNVSYSEEEfehLSESAIDFIKTLLIK 254
                       250
                ....*....|....*..
gi 27229182 291 NPTRRATLEDVASHWWV 307
Cdd:cd14197 255 KPENRATAEDCLKHPWL 271
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
63-308 2.67e-45

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


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 161.61  E-value: 2.67e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKSIrkdKIKDEQDLLH-IRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGD 140
Cdd:cd06623   9 LGQGSSGVVYKVRhKPTGKIYALKKI---HVDGDEEFRKqLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 141 LYDYISERPRLSERDARHFFRQIVSALHYCHQN-GIVHRDLKLENILLDANGNIKIADFGLS-NLYHKGKFLQTFCGSPL 218
Cdd:cd06623  86 LADLLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKIADFGISkVLENTLDQCNTFVGTVT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 219 YASPEIVNGKPYVGPEvDSWSLGVLLYILVHGTMPFDGQDHK---TLVKQISNGAyrEPPKPSDACG-----LIRWLLMV 290
Cdd:cd06623 166 YMSPERIQGESYSYAA-DIWSLGLTLLECALGKFPFLPPGQPsffELMQAICDGP--PPSLPAEEFSpefrdFISACLQK 242
                       250
                ....*....|....*...
gi 27229182 291 NPTRRATLEDVASHWWVN 308
Cdd:cd06623 243 DPKKRPSAAELLQHPFIK 260
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
57-295 3.31e-45

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: 163.24  E-value: 3.31e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKI--KDEQD-LLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd05589   1 FRCIAVLGRGHFGKVLLAEyKPTGELFAIKALKKGDIiaRDEVEsLMCEKRIFETVNSARHPFLVNLFACFQTPEHVCFV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL--SNLYHKGKfL 210
Cdd:cd05589  81 MEYAAGGDLMMHIHEDV-FSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLckEGMGFGDR-T 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 QTFCGSPLYASPEIVNGKPYVgPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-DACGLIRWLLM 289
Cdd:cd05589 159 STFCGTPEFLAPEVLTDTSYT-RAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLStEAISIMRRLLR 237

                ....*.
gi 27229182 290 VNPTRR 295
Cdd:cd05589 238 KNPERR 243
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
63-307 4.78e-45

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: 161.24  E-value: 4.78e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDE--QDLLHirrEIEIMS-SLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd14198  16 LGRGKFAVVRQCISkSTGQEYAAKFLKKRRRGQDcrAEILH---EIAVLElAKSNPRVVNLHEVYETTSEIILILEYAAG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYI--SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDAN---GNIKIADFGLSNLYHKGKFLQTF 213
Cdd:cd14198  93 GEIFNLCvpDLAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIyplGDIKIVDFGMSRKIGHACELREI 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQIS--NGAYREPPKPS---DACGLIRWLL 288
Cdd:cd14198 173 MGTPEYLAPEILNYDP-ITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISqvNVDYSEETFSSvsqLATDFIQKLL 251
                       250
                ....*....|....*....
gi 27229182 289 MVNPTRRATLEDVASHWWV 307
Cdd:cd14198 252 VKNPEKRPTAEICLSHSWL 270
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
57-295 7.12e-45

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: 162.86  E-value: 7.12e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIA-IHEVFENSSKIVIVME 134
Cdd:cd05615  12 FNFLMVLGKGSFGKVMLAeRKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALQDKPPFLTqLHSCFQTVDRLYFVME 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYH-KGKFLQTF 213
Cdd:cd05615  92 YVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMvEGVTTRTF 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-DACGLIRWLLMVNP 292
Cdd:cd05615 172 CGTPDYIAPEIIAYQPY-GRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSkEAVSICKGLMTKHP 250

                ...
gi 27229182 293 TRR 295
Cdd:cd05615 251 AKR 253
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
57-295 9.02e-45

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: 162.40  E-value: 9.02e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARESSG----RLVAIKSIRKDKI-KDEQDLLHIRREIEIMSSLNH-PHIIAIHEVFENSSKIV 130
Cdd:cd05614   2 FELLKVLGTGAYGKVFLVRKVSGhdanKLYAMKVLRKAALvQKAKTVEHTRTERNVLEHVRQsPFLVTLHYAFQTDAKLH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 IVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN--LYHKGK 208
Cdd:cd05614  82 LILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKefLTEEKE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYR-EPPKPS----DACGL 283
Cdd:cd05614 162 RTYSFCGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRRILKcDPPFPSfigpVARDL 241
                       250
                ....*....|..
gi 27229182 284 IRWLLMVNPTRR 295
Cdd:cd05614 242 LQKLLCKDPKKR 253
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
55-310 1.05e-44

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: 161.64  E-value: 1.05e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  55 HRYEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd05574   1 DHFKKIKLLGKGDVGRVYLVRLKgTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYISERP--RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL-------- 203
Cdd:cd05574  81 DYCPGGELFRLLQKQPgkRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQssvtpppv 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 204 -YHKGKFLQT---------------------FCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKT 261
Cdd:cd05574 161 rKSLRKGSRRssvksieketfvaepsarsnsFVGTEEYIAPEVIKGDGH-GSAVDWWTLGILLYEMLYGTTPFKGSNRDE 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27229182 262 LVKQISNGAYREPPKP--SDAC-GLIRWLLMVNPTRR----ATLEDVASHWW---VNWG 310
Cdd:cd05574 240 TFSNILKKELTFPESPpvSSEAkDLIRKLLVKDPSKRlgskRGASEIKRHPFfrgVNWA 298
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
56-307 1.43e-44

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: 159.31  E-value: 1.43e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIkDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd06627   1 NYQLGDLIGRGAFGSVYKGLNlNTGEFVAIKQISLEKI-PKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS---NLYHKGKFlq 211
Cdd:cd06627  80 YVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVAtklNEVEKDEN-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMP-FDGQDHKTLVKQISNgayREPPKPSDACGLIRWLLMV 290
Cdd:cd06627 158 SVVGTPYWMAPEVIEMSG-VTTASDIWSVGCTVIELLTGNPPyYDLQPMAALFRIVQD---DHPPLPENISPELRDFLLQ 233
                       250       260
                ....*....|....*....|.
gi 27229182 291 ----NPTRRATLEDVASHWWV 307
Cdd:cd06627 234 cfqkDPTLRPSAKELLKHPWL 254
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
57-295 1.45e-44

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: 160.55  E-value: 1.45e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARESSG----RLVAIKSIRKDKI-KDEQDLLHIRREIEIMSSLNH-PHIIAIHEVFENSSKIV 130
Cdd:cd05613   2 FELLKVLGTGAYGKVFLVRKVSGhdagKLYAMKVLKKATIvQKAKTAEHTRTERQVLEHIRQsPFLVTLHYAFQTDTKLH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 IVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN--LYHKGK 208
Cdd:cd05613  82 LILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKefLLDENE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTFCGSPLYASPEIVNGKPyVGPE--VDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYR-EPPKPSD----AC 281
Cdd:cd05613 162 RAYSFCGTIEYMAPEIVRGGD-SGHDkaVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKsEPPYPQEmsalAK 240
                       250
                ....*....|....
gi 27229182 282 GLIRWLLMVNPTRR 295
Cdd:cd05613 241 DIIQRLLMKDPKKR 254
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
63-295 1.55e-44

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: 161.41  E-value: 1.55e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKV----KKARESSGRLVAIKSIRKDKIKdEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd05582   3 LGQGSFGKVflvrKITGPDAGTLYAMKVLKKATLK-VRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLRG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN--LYHKGKfLQTFCGS 216
Cdd:cd05582  82 GDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKesIDHEKK-AYSFCGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 217 PLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-DACGLIRWLLMVNPTRR 295
Cdd:cd05582 161 VEYMAPEVVNRRGH-TQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSpEAQSLLRALFKRNPANR 239
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
62-309 2.66e-44

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: 160.95  E-value: 2.66e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  62 TLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEI-MSSLNHPHIIAIHEVFENSSKIVIVMEYASRG 139
Cdd:cd05575   2 VIGKGSFGKVLLARhKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVlLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL--SNLYHKGKfLQTFCGSP 217
Cdd:cd05575  82 ELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLckEGIEPSDT-TSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 218 LYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK-PSDACGLIRWLLMVNPTRR- 295
Cdd:cd05575 161 EYLAPEVLRKQPY-DRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNvSPSARDLLEGLLQKDRTKRl 239
                       250       260
                ....*....|....*....|
gi 27229182 296 ---ATLEDVASHWW---VNW 309
Cdd:cd05575 240 gsgNDFLEIKNHSFfrpINW 259
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
56-304 3.00e-44

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: 159.00  E-value: 3.00e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKiKDEqdllhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14010   1 NYVLYDEIGRGKHSVVYKGRrKGTIEFVAIKCVDKSK-RPE-----VLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL----------- 203
Cdd:cd14010  75 YCTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARRegeilkelfgq 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 204 ------YHKGKFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNgayREPPKP 277
Cdd:cd14010 155 fsdegnVNKVSKKQAKRGTPYYMAPELFQGGVH-SFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILN---EDPPPP 230
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 27229182 278 ---------SDACGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd14010 231 ppkvsskpsPDFKSLLKGLLEKDPAKRLSWDELVKH 266
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
55-309 7.54e-44

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 159.98  E-value: 7.54e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   55 HRYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:PTZ00263  18 SDFEMGETLGTGSFGRVRIAKhKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  134 EYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFlqTF 213
Cdd:PTZ00263  98 EFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTF--TL 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  214 CGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF-DGQDHKTLVKqISNGAYREPP-KPSDACGLIRWLLMVN 291
Cdd:PTZ00263 176 CGTPEYLAPEVIQSKGH-GKAVDWWTMGVLLYEFIAGYPPFfDDTPFRIYEK-ILAGRLKFPNwFDGRARDLVKGLLQTD 253
                        250       260
                 ....*....|....*....|....*.
gi 27229182  292 PTRR-ATL----EDVASHWW---VNW 309
Cdd:PTZ00263 254 HTKRlGTLkggvADVKNHPYfhgANW 279
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
63-307 1.70e-43

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: 156.55  E-value: 1.70e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDL---LHIRREIEIMSSL----NHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14101   8 LGKGGFGTVYAGhRISDGLQVAIKQISRNRVQQWSKLpgvNPVPNEVALLQSVgggpGHRGVIRLLDWFEIPEGFLLVLE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRG-DLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDA-NGNIKIADFGLSNLYHKGKFLQt 212
Cdd:cd14101  88 RPQHCqDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLrTGDIKLIDFGSGATLKDSMYTD- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDgQDHKTLVKQISngaYREPPKPsDACGLIRWLLMVNP 292
Cdd:cd14101 167 FDGTRVYSPPEWILYHQYHALPATVWSLGILLYDMVCGDIPFE-RDTDILKAKPS---FNKRVSN-DCRSLIRSCLAYNP 241
                       250
                ....*....|....*
gi 27229182 293 TRRATLEDVASHWWV 307
Cdd:cd14101 242 SDRPSLEQILLHPWM 256
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
56-303 1.99e-43

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: 156.66  E-value: 1.99e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDE---QDLLHirrEIEIMSSLNHPHIIAIHEVFENSSKIVI 131
Cdd:cd08224   1 NYEIEKKIGKGQFSVVYRARCLlDGRLVALKKVQIFEMMDAkarQDCLK---EIDLLQQLNHPNIIKYLASFIENNELNI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDYISERPR----LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNlYHKG 207
Cdd:cd08224  78 VLELADAGDLSRLIKHFKKqkrlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGR-FFSS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 208 KFLQTF--CGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF--DGQDHKTLVKQISNGAYrePPKPSDAC-- 281
Cdd:cd08224 157 KTTAAHslVGTPYYMSPERIREQGY-DFKSDIWSLGCLLYEMAALQSPFygEKMNLYSLCKKIEKCEY--PPLPADLYsq 233
                       250       260
                ....*....|....*....|....*
gi 27229182 282 ---GLIRWLLMVNPTRRATLEDVAS 303
Cdd:cd08224 234 elrDLVAACIQPDPEKRPDISYVLD 258
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
56-306 2.97e-43

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: 155.96  E-value: 2.97e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLlhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14184   2 KYKIGKVIGDGNFAVVKECVErSTGKEFALKIIDKAKCCGKEHL--IENEVSILRRVKHPNIIMLIEEMDTPAELYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL----DANGNIKIADFGLSNLYHKGkfL 210
Cdd:cd14184  80 LVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVVEGP--L 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 QTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDH--KTLVKQISNGAYrEPPKP------SDACG 282
Cdd:cd14184 158 YTVCGTPTYVAPEIIAETGY-GLKVDIWAAGVITYILLCGFPPFRSENNlqEDLFDQILLGKL-EFPSPywdnitDSAKE 235
                       250       260
                ....*....|....*....|....
gi 27229182 283 LIRWLLMVNPTRRATLEDVASHWW 306
Cdd:cd14184 236 LISHMLQVNVEARYTAEQILSHPW 259
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
63-309 7.10e-43

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: 157.05  E-value: 7.10e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKA-RESSGRLVAIKSIRKDKI--KDEQDLLHIRREIeIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRG 139
Cdd:cd05603   3 IGKGSFGKVLLAkRKCDGKFYAVKVLQKKTIlkKKEQNHIMAERNV-LLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL-YHKGKFLQTFCGSPL 218
Cdd:cd05603  82 ELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEgMEPEETTSTFCGTPE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 219 YASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPP-KPSDACGLIRWLLMVNPTRR-- 295
Cdd:cd05603 162 YLAPEVLRKEPY-DRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGgKTVAACDLLQGLLHKDQRRRlg 240
                       250
                ....*....|....*....
gi 27229182 296 --ATLEDVASHWW---VNW 309
Cdd:cd05603 241 akADFLEIKNHVFfspINW 259
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
63-304 1.16e-42

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: 154.31  E-value: 1.16e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd14189   9 LGKGGFARCYEMTDlATNKTYAVKVIPHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKSL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL-SNLYHKGKFLQTFCGSPLYA 220
Cdd:cd14189  89 AHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLaARLEPPEQRKKTICGTPNYL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 221 SPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-DACGLIRWLLMVNPTRRATLE 299
Cdd:cd14189 169 APEVLLRQGH-GPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSlPARHLLAGILKRNPGDRLTLD 247

                ....*
gi 27229182 300 DVASH 304
Cdd:cd14189 248 QILEH 252
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
56-301 1.38e-42

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: 154.20  E-value: 1.38e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIK-DEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd08218   1 KYVRIKKIGEGSFGKALLVKsKEDGKQYVIKEINISKMSpKERE--ESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYISERPRL--SERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHK-GKFL 210
Cdd:cd08218  79 DYCDGGDLYKRINAQRGVlfPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNStVELA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 QTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYrePPKPS----DACGLIRW 286
Cdd:cd08218 159 RTCIGTPYYLSPEICENKPY-NNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSY--PPVPSrysyDLRSLVSQ 235
                       250
                ....*....|....*
gi 27229182 287 LLMVNPTRRATLEDV 301
Cdd:cd08218 236 LFKRNPRDRPSINSI 250
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
52-301 1.98e-42

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: 153.99  E-value: 1.98e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  52 NLRHRYEF--LETLGKGTYGKVKKARES-SGRLVAIKSIRkdkIKDEQDLLH-IRREIEIMSSLNHPHIIAIHEVFENSS 127
Cdd:cd13996   1 NSRYLNDFeeIELLGSGGFGSVYKVRNKvDGVTYAIKKIR---LTEKSSASEkVLREVKALAKLNHPNIVRYYTAWVEEP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 128 KIVIVMEYASRGDLYDYISERPRLSERD---ARHFFRQIVSALHYCHQNGIVHRDLKLENILLD-ANGNIKIADFGLSNL 203
Cdd:cd13996  78 PLYIQMELCEGGTLRDWIDRRNSSSKNDrklALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDnDDLQVKIGDFGLATS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 204 YHKGKFLQTF---------------CGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHgtmPFDGQ-DHKTLVKQIS 267
Cdd:cd13996 158 IGNQKRELNNlnnnnngntsnnsvgIGTPLYASPEQLDGENY-NEKADIYSLGIILFEMLH---PFKTAmERSTILTDLR 233
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 27229182 268 NGAY-----REPPKPSDacgLIRWLLMVNPTRRATLEDV 301
Cdd:cd13996 234 NGILpesfkAKHPKEAD---LIQSLLSKNPEERPSAEQL 269
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
57-309 2.25e-42

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: 154.52  E-value: 2.25e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd05612   3 FERIKTIGTGTFGRVHLVRDRiSEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFlqTFCG 215
Cdd:cd05612  83 VPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDRTW--TLCG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 216 SPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYrEPPKPSD--ACGLIRWLLMVNPT 293
Cdd:cd05612 161 TPEYLAPEVIQSKGH-NKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKL-EFPRHLDlyAKDLIKKLLVVDRT 238
                       250       260
                ....*....|....*....|....
gi 27229182 294 RRA-----TLEDVASHWW---VNW 309
Cdd:cd05612 239 RRLgnmknGADDVKNHRWfksVDW 262
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
57-307 2.35e-42

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: 153.59  E-value: 2.35e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLLHIRR---EIEIMSSLNHPH--IIAIHEVFENSSKIV 130
Cdd:cd14100   2 YQVGPLLGSGGFGSVYSGiRVADGAPVAIKHVEKDRVSEWGELPNGTRvpmEIVLLKKVGSGFrgVIRLLDWFERPDSFV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 IVMEYASR-GDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDAN-GNIKIADFGLSNLYhKGK 208
Cdd:cd14100  82 LVLERPEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNtGELKLIDFGSGALL-KDT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDgQDHKTLVKQIsngAYREppKPSDACG-LIRWL 287
Cdd:cd14100 161 VYTDFDGTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDIPFE-HDEEIIRGQV---FFRQ--RVSSECQhLIKWC 234
                       250       260
                ....*....|....*....|
gi 27229182 288 LMVNPTRRATLEDVASHWWV 307
Cdd:cd14100 235 LALRPSDRPSFEDIQNHPWM 254
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
63-255 2.66e-42

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: 155.66  E-value: 2.66e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRRE---IEIMSslNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd05588   3 IGRGSYAKVLMVElKKTKRIYAMKVIKKELVNDDEDIDWVQTEkhvFETAS--NHPFLVGLHSCFQTESRLFFVIEFVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL-YHKGKFLQTFCGSP 217
Cdd:cd05588  81 GDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEgLRPGDTTSTFCGTP 160
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 27229182 218 LYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFD 255
Cdd:cd05588 161 NYIAPEILRGEDY-GFSVDWWALGVLMFEMLAGRSPFD 197
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
56-259 9.58e-42

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


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 152.86  E-value: 9.58e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKsirkdKIKDEQDLLHIR----REIEIMSSLNHPHIIAIHEVFENSSKIV 130
Cdd:cd07833   2 KYEVLGVVGEGAYGVVLKCRNkATGEIVAIK-----KFKESEDDEDVKktalREVKVLRQLRHENIVNLKEAFRRKGRLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 IVMEYASRgDLYDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGK- 208
Cdd:cd07833  77 LVFEYVER-TLLELLEASPGgLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPa 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 27229182 209 -FLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDH 259
Cdd:cd07833 156 sPLTDYVATRWYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSD 207
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
54-301 1.28e-41

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: 152.14  E-value: 1.28e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEF--LETLGKGTYGKVKKARES-SGRLVAIKSIRkdkIKDEQDLLH-IRREIEIMSSLNHPHIIAIHEVFENSSKI 129
Cdd:cd14046   3 RYLTDFeeLQVLGKGAFGQVVKVRNKlDGRYYAIKKIK---LRSESKNNSrILREVMLLSRLNHQHVVRYYQAWIERANL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 130 VIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-------- 201
Cdd:cd14046  80 YIQMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLAtsnklnve 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 202 ----NLYHKGKFLQTF-------CGSPLYASPEIV-NGKPYVGPEVDSWSLGVLLYILVHgtmPFDG--QDHKTLvkqis 267
Cdd:cd14046 160 latqDINKSTSAALGSsgdltgnVGTALYVAPEVQsGTKSTYNEKVDMYSLGIIFFEMCY---PFSTgmERVQIL----- 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 27229182 268 nGAYREPPK--PSDACG--------LIRWLLMVNPTRRATLEDV 301
Cdd:cd14046 232 -TALRSVSIefPPDFDDnkhskqakLIRWLLNHDPAKRPSAQEL 274
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
57-304 1.44e-41

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: 151.74  E-value: 1.44e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd06610   3 YELIEVIGSGATAVVYAAYcLPKKEKVAIKRIDLEKCQTSMD--ELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISER-PR--LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-NLYHKG---- 207
Cdd:cd06610  81 LSGGSLLDIMKSSyPRggLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSaSLATGGdrtr 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 208 KFLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQ-DHKTLVKQISNgayrEPPK-PSDA----C 281
Cdd:cd06610 161 KVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYSKYpPMKVLMLTLQN----DPPSlETGAdykkY 236
                       250       260
                ....*....|....*....|....*...
gi 27229182 282 G-----LIRWLLMVNPTRRATLEDVASH 304
Cdd:cd06610 237 SksfrkMISLCLQKDPSKRPTAEELLKH 264
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
61-271 2.12e-41

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: 150.88  E-value: 2.12e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDllhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRG 139
Cdd:cd14192  10 EVLGGGRFGQVHKCTElSTGLTLAAKIIKVKGAKEREE---VKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYIS-ERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENIL-LDANGN-IKIADFGLSNLYHKGKFLQTFCGS 216
Cdd:cd14192  87 ELFDRITdESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGNqIKIIDFGLARRYKPREKLKVNFGT 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27229182 217 PLYASPEIVNgKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAY 271
Cdd:cd14192 167 PEFLAPEVVN-YDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKW 220
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
56-304 3.15e-41

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: 150.16  E-value: 3.15e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14188   2 RYCRGKVLGKGGFAKCYEMTDlTTNKVYAAKIIPHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL-SNLYHKGKFLQTF 213
Cdd:cd14188  82 YCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLaARLEPLEHRRRTI 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK-PSDACGLIRWLLMVNP 292
Cdd:cd14188 162 CGTPNYLSPEVLNKQGH-GCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSlLAPAKHLIASMLSKNP 240
                       250
                ....*....|..
gi 27229182 293 TRRATLEDVASH 304
Cdd:cd14188 241 EDRPSLDEIIRH 252
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
57-301 5.51e-41

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: 149.50  E-value: 5.51e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKV---KKARESSgrLVAIKSIRKDKI--KDEQDLLHirrEIEIMSSLNHPHIIAIHEVFENSSKIVI 131
Cdd:cd08221   2 YIPVRVLGRGAFGEAvlyRKTEDNS--LVVWKEVNLSRLseKERRDALN---EIDILSLLNHDNIITYYNHFLDGESLFI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDYISERPR--LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN-LYHKGK 208
Cdd:cd08221  77 EMEYCNGGNLHDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKvLDSESS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYRE--PPKPSDACGLIRW 286
Cdd:cd08221 157 MAESIVGTPYYMSPELVQGVKY-NFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDidEQYSEEIIQLVHD 235
                       250
                ....*....|....*
gi 27229182 287 LLMVNPTRRATLEDV 301
Cdd:cd08221 236 CLHQDPEDRPTAEEL 250
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
56-308 7.69e-41

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: 149.76  E-value: 7.69e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLlhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14183   7 RYKVGRTIGDGNFAVVKECVErSTGREYALKIINKSKCRGKEHM--IQNEVSILRRVKHPNIVLLIEEMDMPTELYLVME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL----DANGNIKIADFGLSNLYHKGkfL 210
Cdd:cd14183  85 LVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLATVVDGP--L 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 QTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDG--QDHKTLVKQISNGAYrEPPKP-----SDACG- 282
Cdd:cd14183 163 YTVCGTPTYVAPEIIAETGY-GLKVDIWAAGVITYILLCGFPPFRGsgDDQEVLFDQILMGQV-DFPSPywdnvSDSAKe 240
                       250       260
                ....*....|....*....|....*.
gi 27229182 283 LIRWLLMVNPTRRATLEDVASHWWVN 308
Cdd:cd14183 241 LITMMLQVDVDQRYSALQVLEHPWVN 266
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
63-310 7.72e-41

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: 151.61  E-value: 7.72e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMS-SLNHPHIIAIHEVFENSSKIVIVMEYASRGD 140
Cdd:cd05619  13 LGKGSFGKVFLAElKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSlAWEHPFLTHLFCTFQTKENLFFVMEYLNGGD 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 141 LYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL--SNLYHKGKfLQTFCGSPL 218
Cdd:cd05619  93 LMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMckENMLGDAK-TSTFCGTPD 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 219 YASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQI--SNGAYrepPK--PSDACGLIRWLLMVNPTR 294
Cdd:cd05619 172 YIAPEILLGQKY-NTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIrmDNPFY---PRwlEKEAKDILVKLFVREPER 247
                       250       260
                ....*....|....*....|
gi 27229182 295 RATLE-DVASHWW---VNWG 310
Cdd:cd05619 248 RLGVRgDIRQHPFfreINWE 267
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
56-279 7.79e-41

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 156.49  E-value: 7.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   56 RYEFLETLGKGTYGKVKKARESS-GRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:NF033483   8 RYEIGERIGRGGMAEVYLAKDTRlDRDVAVKVLRPDLARDPEFVARFRREAQSAASLSHPNIVSVYDVGEDGGIPYIVME 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL------SNLYHKGK 208
Cdd:NF033483  88 YVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIaralssTTMTQTNS 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27229182  209 FLqtfcGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQdhkTLVkQIsngAYR----EPPKPSD 279
Cdd:NF033483 168 VL----GTVHYLSPEQARGGT-VDARSDIYSLGIVLYEMLTGRPPFDGD---SPV-SV---AYKhvqeDPPPPSE 230
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
61-266 9.50e-41

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: 149.29  E-value: 9.50e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDllhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRG 139
Cdd:cd14193  10 EILGGGRFGQVHKCEEkSSGLKLAAKIIKARSQKEKEE---VKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYD-YISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL---DANgNIKIADFGLSNLYHKGKFLQTFCG 215
Cdd:cd14193  87 ELFDrIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCvsrEAN-QVKIIDFGLARRYKPREKLRVNFG 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 27229182 216 SPLYASPEIVNGKpYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQI 266
Cdd:cd14193 166 TPEFLAPEVVNYE-FVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNI 215
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
57-309 1.10e-40

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: 151.32  E-value: 1.10e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIM-SSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd05602   9 FHFLKVIGKGSFGKVLLARhKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLlKNVKHPFLVGLHFSFQTTDKLYFVLD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL--SNLYHKGKfLQT 212
Cdd:cd05602  89 YINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLckENIEPNGT-TST 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDAC-GLIRWLLMVN 291
Cdd:cd05602 168 FCGTPEYLAPEVLHKQPY-DRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSArHLLEGLLQKD 246
                       250       260
                ....*....|....*....|....*
gi 27229182 292 PTRRATLED----VASHWW---VNW 309
Cdd:cd05602 247 RTKRLGAKDdfteIKNHIFfspINW 271
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
54-311 1.65e-40

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: 148.54  E-value: 1.65e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKARESSGRLV-AIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd14187   6 RRRYVRGRFLGKGGFAKCYEITDADTKEVfAGKIVPKSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL-SNLYHKGKFLQ 211
Cdd:cd14187  86 LELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLaTKVEYDGERKK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSD-ACGLIRWLLMV 290
Cdd:cd14187 166 TLCGTPNYIAPEVLSKKGH-SFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPvAASLIQKMLQT 244
                       250       260
                ....*....|....*....|.
gi 27229182 291 NPTRRATLEDVASHWWVNWGY 311
Cdd:cd14187 245 DPTARPTINELLNDEFFTSGY 265
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
57-304 2.88e-40

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: 147.84  E-value: 2.88e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIrkdKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd06613   2 YELIQRIGSGTYGDVYKARNiATGELAAVKVI---KLEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRG---DLYDYIseRPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-NLYHKGKFLQ 211
Cdd:cd06613  79 CGGGslqDIYQVT--GP-LSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSaQLTATIAKRK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEI--VNGKPYVGPEVDSWSLGVLLYILVHGTMP-FDGQDHKTLVkQISNGAYrEPPKPSDAC------- 281
Cdd:cd06613 156 SFIGTPYWMAPEVaaVERKGGYDGKCDIWALGITAIELAELQPPmFDLHPMRALF-LIPKSNF-DPPKLKDKEkwspdfh 233
                       250       260
                ....*....|....*....|...
gi 27229182 282 GLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd06613 234 DFIKKCLTKNPKKRPTATKLLQH 256
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
57-307 5.11e-40

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: 147.02  E-value: 5.11e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKV-KKARESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIM----SSLNHPHIIAIHEVFENSSKIVI 131
Cdd:cd14102   2 YQVGSVLGSGGFGTVyAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVPLEIVllkkVGSGFRGVIKLLDWYERPDGFLI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASR-GDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDA-NGNIKIADFGlSNLYHKGKF 209
Cdd:cd14102  82 VMERPEPvKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLrTGELKLIDFG-SGALLKDTV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 210 LQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDgQDHKTLVKQIsngAYREppKPSDAC-GLIRWLL 288
Cdd:cd14102 161 YTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFE-QDEEILRGRL---YFRR--RVSPECqQLIKWCL 234
                       250
                ....*....|....*....
gi 27229182 289 MVNPTRRATLEDVASHWWV 307
Cdd:cd14102 235 SLRPSDRPTLEQIFDHPWM 253
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
57-255 5.90e-40

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: 150.18  E-value: 5.90e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIM-SSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd05618  22 FDLLRVIGRGSYAKVLLVRlKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFeQASNHPFLVGLHSCFQTESRLFFVIE 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL-YHKGKFLQTF 213
Cdd:cd05618 102 YVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEgLRPGDTTSTF 181
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27229182 214 CGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFD 255
Cdd:cd05618 182 CGTPNYIAPEILRGEDY-GFSVDWWALGVLMFEMMAGRSPFD 222
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
50-254 6.58e-40

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: 147.04  E-value: 6.58e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  50 KHNLRHRYEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQdllhIRREIEIMSSLNHPHIIAIHEVFENSSK 128
Cdd:cd14113   2 KDNFDSFYSEVAELGRGRFSVVKKCdQRGTKRAVATKFVNKKLMKRDQ----VTHELGVLQSLQHPQLVGLLDTFETPTS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLD---ANGNIKIADFGLSNLYH 205
Cdd:cd14113  78 YILVLEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDqslSKPTIKLADFGDAVQLN 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 27229182 206 KGKFLQTFCGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPF 254
Cdd:cd14113 158 TTYYIHQLLGSPEFAAPEIILGNP-VSLTSDLWSIGVLTYVLLSGVSPF 205
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
56-289 9.44e-40

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: 146.69  E-value: 9.44e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEF--LETLGKGTYGKVKKAR--ESSGRLVAIKSIRKDKIKDEQDLLHirREIEIMSSLNHPHIIAIHEVFENSSKIVI 131
Cdd:cd14202   1 KFEFsrKDLIGHGAFAVVFKGRhkEKHDLEVAVKCINKKNLAKSQTLLG--KEIKILKELKHENIVALYDFQEIANSVYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLD------ANGN---IKIADFGLSN 202
Cdd:cd14202  79 VMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrkSNPNnirIKIADFGFAR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 203 LYHKGKFLQTFCGSPLYASPEIVNGKPYVGpEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDACG 282
Cdd:cd14202 159 YLQNNMMAATLCGSPMYMAPEVIMSQHYDA-KADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPNIPRETSS 237

                ....*..
gi 27229182 283 LIRWLLM 289
Cdd:cd14202 238 HLRQLLL 244
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
57-307 1.13e-39

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: 146.30  E-value: 1.13e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDllhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14191   4 YDIEERLGSGKFGQVFRLVEkKTKKVWAGKFFKAYSAKEKEN---IRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYD-YISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENIL-LDANGN-IKIADFGLSNLYHKGKFLQT 212
Cdd:cd14191  81 VSGGELFErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTkIKLIDFGLARRLENAGSLKV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDG-QDHKTLVKQIS------NGAYREPPKpsDACGLIR 285
Cdd:cd14191 161 LFGTPEFVAPEVINYEP-IGYATDMWSIGVICYILVSGLSPFMGdNDNETLANVTSatwdfdDEAFDEISD--DAKDFIS 237
                       250       260
                ....*....|....*....|..
gi 27229182 286 WLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14191 238 NLLKKDMKARLTCTQCLQHPWL 259
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
60-309 1.68e-39

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: 147.80  E-value: 1.68e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  60 LETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIM-SSLNHPHIIAIHEVFENSSKIVIVMEYAS 137
Cdd:cd05604   1 LKVIGKGSFGKVLLAkRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 138 RGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL-YHKGKFLQTFCGS 216
Cdd:cd05604  81 GGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEgISNSDTTTTFCGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 217 PLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPS-DACGLIRWLLMVNPTRR 295
Cdd:cd05604 161 PEYLAPEVIRKQPY-DNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISlTAWSILEELLEKDRQLR 239
                       250       260
                ....*....|....*....|.
gi 27229182 296 ----ATLEDVASHWW---VNW 309
Cdd:cd05604 240 lgakEDFLEIKNHPFfesINW 260
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
61-266 1.93e-39

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: 147.40  E-value: 1.93e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMS-SLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd05620   1 KVLGKGSFGKVLLAElKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLAlAWENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL--SNLYHKGKfLQTFCGS 216
Cdd:cd05620  81 GDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMckENVFGDNR-ASTFCGT 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 27229182 217 PLYASPEIVNGKPYVGpEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQI 266
Cdd:cd05620 160 PDYIAPEILQGLKYTF-SVDWWSFGVLLYEMLIGQSPFHGDDEDELFESI 208
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
56-301 2.63e-39

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: 145.55  E-value: 2.63e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKsirKDKIKDEQDLLHIRREIEIMSSL-NHPHIIAI--HEVF--ENSSKI 129
Cdd:cd13985   1 RYQVTKQLGEGGFSYVYLAHDvNTGRRYALK---RMYFNDEEQLRVAIKEIEIMKRLcGHPNIVQYydSAILssEGRKEV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 130 VIVMEYAsRGDLYDYISERP--RLSERDARHFFRQIVSALHYCHQNG--IVHRDLKLENILLDANGNIKIADFGLSNLYH 205
Cdd:cd13985  78 LLLMEYC-PGSLVDILEKSPpsPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSATTEH 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 206 KGKFLQTFCG----------SPLYASPEIVN---GKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDhktlVKQISNGAYR 272
Cdd:cd13985 157 YPLERAEEVNiieeeiqkntTPMYRAPEMIDlysKKP-IGEKADIWALGCLLYKLCFFKLPFDESS----KLAIVAGKYS 231
                       250       260       270
                ....*....|....*....|....*....|....
gi 27229182 273 EPPKPSdaCG-----LIRWLLMVNPTRRATLEDV 301
Cdd:cd13985 232 IPEQPR--YSpelhdLIRHMLTPDPAERPDIFQV 263
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
56-258 2.85e-39

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: 145.93  E-value: 2.85e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKD---EQDLlhirREIEIMSSLN-HPHIIAIHEVFENSSKIV 130
Cdd:cd07832   1 RYKILGRIGEGAHGIVFKAKDrETGETVALKKVALRKLEGgipNQAL----REIKALQACQgHPYVVKLRDVFPHGTGFV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 IVMEYASRgDLYDYI--SERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGK 208
Cdd:cd07832  77 LVFEYMLS-SLSEVLrdEERP-LTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEED 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 27229182 209 FLQTF--CGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQD 258
Cdd:cd07832 155 PRLYShqVATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELLNGSPLFPGEN 206
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
57-255 3.26e-39

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: 147.86  E-value: 3.26e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLN-HPHIIAIHEVFENSSKIVIVME 134
Cdd:cd05617  17 FDLIRVIGRGSYAKVLLVRlKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASsNPFLVGLHSCFQTTSRLFLVIE 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL-YHKGKFLQTF 213
Cdd:cd05617  97 YVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEgLGPGDTTSTF 176
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27229182 214 CGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFD 255
Cdd:cd05617 177 CGTPNYIAPEILRGEEY-GFSVDWWALGVLMFEMMAGRSPFD 217
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
61-258 4.43e-39

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: 144.68  E-value: 4.43e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDLLHirrEIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRG 139
Cdd:cd14190  10 EVLGGGKFGKVHTCTEKrTGLKLAAKVINKQNSKDKEMVLL---EIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYI-SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL-DANGN-IKIADFGLSNLYHKGKFLQTFCGS 216
Cdd:cd14190  87 ELFERIvDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvNRTGHqVKIIDFGLARRYNPREKLKVNFGT 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27229182 217 PLYASPEIVNGKpYVGPEVDSWSLGVLLYILVHGTMPFDGQD 258
Cdd:cd14190 167 PEFLSPEVVNYD-QVSFPTDMWSMGVITYMLLSGLSPFLGDD 207
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
60-309 4.72e-39

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: 144.55  E-value: 4.72e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  60 LETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEI-MSSLNHPHIIAIHEVFENSSKIVIVMEYAS 137
Cdd:cd05611   1 LKPISKGAFGSVYLAKKrSTGDYFAIKVLKKSDMIAKNQVTNVKAERAImMIQGESPYVAKLYYSFQSKDYLYLVMEYLN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 138 RGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCGSP 217
Cdd:cd05611  81 GGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEKRHNKKFVGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 218 LYASPEIVNGKPYVgPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDACG-----LIRWLLMVNP 292
Cdd:cd05611 161 DYLAPETILGVGDD-KMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKEFCSpeavdLINRLLCMDP 239
                       250       260
                ....*....|....*....|...
gi 27229182 293 TRR---ATLEDVASHWW---VNW 309
Cdd:cd05611 240 AKRlgaNGYQEIKSHPFfksINW 262
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
63-295 5.28e-39

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: 145.79  E-value: 5.28e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd05585   2 IGKGSFGKVMQVRKkDTSRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGEL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL-YHKGKFLQTFCGSPLYA 220
Cdd:cd05585  82 FHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLnMKDDDKTNTFCGTPEYL 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27229182 221 SPEIVNGKPYVgPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREP-PKPSDACGLIRWLLMVNPTRR 295
Cdd:cd05585 162 APELLLGHGYT-KAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPdGFDRDAKDLLIGLLNRDPTKR 236
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
56-304 6.47e-39

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: 144.77  E-value: 6.47e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIK--SIRKDKIKDEQD--LLHIRREIEIMSSLNHPHIIAIHEVFE-NSSKI 129
Cdd:cd13990   1 RYLLLNLLGKGGFSEVYKAFDlVEQRYVACKihQLNKDWSEEKKQnyIKHALREYEIHKSLDHPRIVKLYDVFEiDTDSF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 130 VIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYC--HQNGIVHRDLKLENILLD---ANGNIKIADFGLSNLY 204
Cdd:cd13990  81 CTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHsgnVSGEIKITDFGLSKIM 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 205 HKGKFLQT-------FCGSPLYASPEI-VNGK--PYVGPEVDSWSLGVLLYILVHGTMPF-DGQDHKTLVKQ--ISNGAY 271
Cdd:cd13990 161 DDESYNSDgmeltsqGAGTYWYLPPECfVVGKtpPKISSKVDVWSVGVIFYQMLYGRKPFgHNQSQEAILEEntILKATE 240
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 27229182 272 RE-PPKP---SDACGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd13990 241 VEfPSKPvvsSEAKDFIRRCLTYRKEDRPDVLQLAND 277
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
57-304 7.89e-39

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: 144.38  E-value: 7.89e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR--ESSGRLVAIKSIRKDKIKDEQDLLHirREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14201   8 YSRKDLVGHGAFAVVFKGRhrKKTDWEVAIKSINKKNLSKSQILLG--KEIKILKELQHENIVALYDVQEMPNSVFLVME 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANG---------NIKIADFGLSNLYH 205
Cdd:cd14201  86 YCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGFARYLQ 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 206 KGKFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDACGLIR 285
Cdd:cd14201 166 SNMMAATLCGSPMYMAPEVIMSQHY-DAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNKNLQPSIPRETSPYLA 244
                       250       260
                ....*....|....*....|...
gi 27229182 286 WLLMV----NPTRRATLEDVASH 304
Cdd:cd14201 245 DLLLGllqrNQKDRMDFEAFFSH 267
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
63-295 9.23e-39

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: 145.79  E-value: 9.23e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDLLHIRREIEIM---SSLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd05586   1 IGKGTFGQVYQVRKKdTRRIYAMKVLSKKVIVAKKEVAHTIGERNILvrtALDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS--NLyHKGKFLQTFCGS 216
Cdd:cd05586  81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSkaDL-TDNKTTNTFCGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 217 PLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK--PSDACGLIRWLLMVNPTR 294
Cdd:cd05586 160 TEYLAPEVLLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDvlSDEGRSFVKGLLNRNPKH 239

                .
gi 27229182 295 R 295
Cdd:cd05586 240 R 240
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
55-307 2.78e-38

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: 142.77  E-value: 2.78e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  55 HRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLlhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd06609   1 ELFTLLERIGKGSFGEVYKGIDkRTNQVVAIKVIDLEEAEDEIED--IQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-NLYHKGKFLQT 212
Cdd:cd06609  79 EYCGGGSVLDLLKPGP-LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSgQLTSTMSKRNT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNgayREPPK------PSDACGLIRW 286
Cdd:cd06609 158 FVGTPFWMAPEVIKQSGY-DEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPK---NNPPSlegnkfSKPFKDFVEL 233
                       250       260
                ....*....|....*....|.
gi 27229182 287 LLMVNPTRRATLEDVASHWWV 307
Cdd:cd06609 234 CLNKDPKERPSAKELLKHKFI 254
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
56-297 3.76e-38

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: 141.65  E-value: 3.76e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGK-VKKARESSGRLVAIKSIRKDKikDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd08219   1 QYNVLRVVGEGSFGRaLLVQHVNSDQKYAMKEIRLPK--SSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYIS-ERPRL-SERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN-LYHKGKFLQ 211
Cdd:cd08219  79 YCDGGDLMQKIKlQRGKLfPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARlLTSPGAYAC 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYRepPKPS----DACGLIRWL 287
Cdd:cd08219 159 TYVGTPYYVPPEIWENMPY-NNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYK--PLPShysyELRSLIKQM 235
                       250
                ....*....|
gi 27229182 288 LMVNPTRRAT 297
Cdd:cd08219 236 FKRNPRSRPS 245
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
63-307 5.82e-38

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: 141.34  E-value: 5.82e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDE--QDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRG 139
Cdd:cd06625   8 LGQGAFGQVYLCYDaDTGRELAVKQVEIDPINTEasKEVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSnlyhkgKFLQTFC----- 214
Cdd:cd06625  88 SVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGAS------KRLQTICsstgm 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 215 ----GSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMP-FDGQDHKTLVK-QISNGAYREPPKPSDAC-GLIRWL 287
Cdd:cd06625 162 ksvtGTPYWMSPEVINGEGY-GRKADIWSVGCTVVEMLTTKPPwAEFEPMAAIFKiATQPTNPQLPPHVSEDArDFLSLI 240
                       250       260
                ....*....|....*....|
gi 27229182 288 LMVNPTRRATLEDVASHWWV 307
Cdd:cd06625 241 FVRNKKQRPSAEELLSHSFV 260
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
57-242 6.41e-38

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


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 141.25  E-value: 6.41e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDkikdeQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd06612   5 FDILEKLGEGSYGSVYKAIhKETGQVVAIKVVPVE-----EDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-NLYHKGKFLQTF 213
Cdd:cd06612  80 CGAGSVSDIMKITNKtLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSgQLTDTMAKRNTV 159
                       170       180
                ....*....|....*....|....*....
gi 27229182 214 CGSPLYASPEIVNGKPYvGPEVDSWSLGV 242
Cdd:cd06612 160 IGTPFWMAPEVIQEIGY-NNKADIWSLGI 187
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
56-304 7.74e-38

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: 143.05  E-value: 7.74e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRkDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVF-----ENSSKI 129
Cdd:cd07834   1 RYELLKPIGSGAYGVVCSAYdKRTGRKVAIKKIS-NVFDDLIDAKRILREIKILRHLKHENIIGLLDILrppspEEFNDV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 130 VIVMEYAsRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS---NLYHK 206
Cdd:cd07834  80 YIVTELM-ETDLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLArgvDPDED 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 207 GKFLQTFCGSPLYASPEIV-NGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDH--------KTL-------VKQISNGA 270
Cdd:cd07834 159 KGFLTEYVVTRWYRAPELLlSSKKY-TKAIDIWSVGCIFAELLTRKPLFPGRDYidqlnlivEVLgtpseedLKFISSEK 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 27229182 271 YRE-----PPKP------------SDACGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd07834 238 ARNylkslPKKPkkplsevfpgasPEAIDLLEKMLVFNPKKRITADEALAH 288
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
56-307 8.29e-38

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: 141.63  E-value: 8.29e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKI-----------------------KDEQDLLHIRREIEIMSSL 111
Cdd:cd14200   1 QYKLQSEIGKGSYGVVKLAyNESDDKYYAMKVLSKKKLlkqygfprrppprgskaaqgeqaKPLAPLERVYQEIAILKKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 112 NHPHIIAIHEVFENSSK--IVIVMEYASRGDLYDYISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDA 189
Cdd:cd14200  81 DHVNIVKLIEVLDDPAEdnLYMVFDLLRKGPVMEVPSDKP-FSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 190 NGNIKIADFGLSNLYH-KGKFLQTFCGSPLYASPEIV--NGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQI 266
Cdd:cd14200 160 DGHVKIADFGVSNQFEgNDALLSSTAGTPAFMAPETLsdSGQSFSGKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKI 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 27229182 267 SNGAYREPPKPS---DACGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14200 240 KNKPVEFPEEPEiseELKDLILKMLDKNPETRITVPEIKVHPWV 283
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
55-304 1.16e-37

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: 140.81  E-value: 1.16e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  55 HRYEFLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIkDEQDLLHIRREIEIMSSLNH-PHIIAI--HEVFENSSKIVI 131
Cdd:cd14131   1 KPYEILKQLGKGGSSKVYKVLNPKKKIYALKRVDLEGA-DEQTLQSYKNEIELLKKLKGsDRIIQLydYEVTDEDDYLYM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASrGDLYDYISER--PRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLdANGNIKIADFGLSNLYHKG-- 207
Cdd:cd14131  80 VMECGE-IDLATILKKKrpKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-VKGRLKLIDFGIAKAIQNDtt 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 208 ---KFLQtfCGSPLYASPEIVN--------GKPY-VGPEVDSWSLGVLLYILVHGTMPFD---GQDHKtlVKQISNGAYR 272
Cdd:cd14131 158 sivRDSQ--VGTLNYMSPEAIKdtsasgegKPKSkIGRPSDVWSLGCILYQMVYGKTPFQhitNPIAK--LQAIIDPNHE 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 27229182 273 --EPPKPSDacglirWLLMV-------NPTRRATLEDVASH 304
Cdd:cd14131 234 ieFPDIPNP------DLIDVmkrclqrDPKKRPSIPELLNH 268
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
56-307 1.23e-37

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: 140.55  E-value: 1.23e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKS-IRKDKIKDEQdllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd14088   2 RYDLGQVIKTEEFCEIFRAKDkTTGKLYTCKKfLKRDGRKVRK---AAKNEINILKMVKHPNILQLVDVFETRKEYFIFL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLD---ANGNIKIADFGLSNLyhKGKFL 210
Cdd:cd14088  79 ELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYnrlKNSKIVISDFHLAKL--ENGLI 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 QTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF-------DGQDH-KTLVKQISNGAYR-EPPKPSD-- 279
Cdd:cd14088 157 KEPCGTPEYLAPEVVGRQRY-GRPVDCWAIGVIMYILLSGNPPFydeaeedDYENHdKNLFRKILAGDYEfDSPYWDDis 235
                       250       260       270
                ....*....|....*....|....*....|
gi 27229182 280 --ACGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14088 236 qaAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
54-295 1.42e-37

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: 140.88  E-value: 1.42e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIrkdKIKDEQDLLHIRREIEIMSSL-NHPHII-----AIHEVFENS 126
Cdd:cd14037   2 SHHVTIEKYLAEGGFAHVYLVKtSNGGNRAALKRV---YVNDEHDLNVCKREIEIMKRLsGHKNIVgyidsSANRSGNGV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 127 SKIVIVMEYASRGDLYDYISER--PRLSERDARHFFRQI---VSALHYChQNGIVHRDLKLENILLDANGNIKIADFGLS 201
Cdd:cd14037  79 YEVLLLMEYCKGGGVIDLMNQRlqTGLTESEILKIFCDVceaVAAMHYL-KPPLIHRDLKVENVLISDSGNYKLCDFGSA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 202 NlyhkGKFL--QTFCG------------SPLYASPEIVN---GKPyVGPEVDSWSLGVLLYILVHGTMPFdgQDHKTLVk 264
Cdd:cd14037 158 T----TKILppQTKQGvtyveedikkytTLQYRAPEMIDlyrGKP-ITEKSDIWALGCLLYKLCFYTTPF--EESGQLA- 229
                       250       260       270
                ....*....|....*....|....*....|....
gi 27229182 265 qISNGAYREPPKP---SDACGLIRWLLMVNPTRR 295
Cdd:cd14037 230 -ILNGNFTFPDNSrysKRLHKLIRYMLEEDPEKR 262
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
64-307 1.84e-37

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: 140.13  E-value: 1.84e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  64 GKGTYGKVKKARE-SSGRLVAIKSIRKDKiKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDLY 142
Cdd:cd06626   9 GEGTFGKVYTAVNlDTGELMAMKEIRFQD-NDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEGTLE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 143 DYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKF------LQTFCGS 216
Cdd:cd06626  88 ELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNTTtmapgeVNSLVGT 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 217 PLYASPEIVNGKPYVGPE--VDSWSLGVLLYILVHGTMPFDGQDHK-TLVKQIsnGAYREPPKP-----SDAC-GLIRWL 287
Cdd:cd06626 168 PAYMAPEVITGNKGEGHGraADIWSLGCVVLEMATGKRPWSELDNEwAIMYHV--GMGHKPPIPdslqlSPEGkDFLSRC 245
                       250       260
                ....*....|....*....|
gi 27229182 288 LMVNPTRRATLEDVASHWWV 307
Cdd:cd06626 246 LESDPKKRPTASELLDHPFI 265
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
63-304 5.02e-37

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: 138.61  E-value: 5.02e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKdEQDLLhirREIEIMSSLN-HPHIIAIHEV-FENSSKIVIVMEYASRG 139
Cdd:cd13987   1 LGEGTYGKVLLAVHkGSGTKMALKFVPKPSTK-LKDFL---REYNISLELSvHPHIIKTYDVaFETEDYYVFAQEYAPYG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL-DAN-GNIKIADFGLSNlyHKGKFLQTFCGSP 217
Cdd:cd13987  77 DLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfDKDcRRVKLCDFGLTR--RVGSTVKRVSGTI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 218 LYASPE----IVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHktlvkqiSNGAYRE------------PPK----P 277
Cdd:cd13987 155 PYTAPEvceaKKNEGFVVDPSIDVWAFGVLLFCCLTGNFPWEKADS-------DDQFYEEfvrwqkrkntavPSQwrrfT 227
                       250       260
                ....*....|....*....|....*..
gi 27229182 278 SDACGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd13987 228 PKALRMFKKLLAPEPERRCSIKEVFKY 254
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
61-307 8.29e-37

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: 138.03  E-value: 8.29e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIkdeqdllhIRREIEIMSSLNHPHIIAIHEVFENSSK-IVIVMEYASR 138
Cdd:cd14109  10 EDEKRAAQGAPFHVTErSTGRNFLAQLRYGDPF--------LMREVDIHNSLDHPNIVQMHDAYDDEKLaVTVIDNLAST 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLY--DYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLdANGNIKIADFGLSNLYHKGKFLQTFCGS 216
Cdd:cd14109  82 IELVrdNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILL-QDDKLKLADFGQSRRLLRGKLTTLIYGS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 217 PLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYR---EPPKP--SDACGLIRWLLMVN 291
Cdd:cd14109 161 PEFVSPEIVNSYP-VTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSfdsSPLGNisDDARDFIKKLLVYI 239
                       250
                ....*....|....*.
gi 27229182 292 PTRRATLEDVASHWWV 307
Cdd:cd14109 240 PESRLTVDEALNHPWF 255
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
57-241 8.96e-37

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: 138.96  E-value: 8.96e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKiKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd07835   1 YQKLEKIGEGTYGVVYKARDkLTGEIVALKKIRLET-EDEGVPSTAIREISLLKELNHPNIVRLLDVVHSENKLYLVFEF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRgDLYDYISERPR--LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYhkgkflqtf 213
Cdd:cd07835  80 LDL-DLKKYMDSSPLtgLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAF--------- 149
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 27229182 214 cGSPL-----------YASPEIVNGKPYVGPEVDSWSLG 241
Cdd:cd07835 150 -GVPVrtythevvtlwYRAPEILLGSKHYSTPVDIWSVG 187
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
49-258 9.14e-37

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: 139.60  E-value: 9.14e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  49 HKHnLRHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKikdeQDLLHIRREIEIMSSLNH------PHIIAIHE 121
Cdd:cd14210   8 GDH-IAYRYEVLSVLGKGSFGQVVKCLDhKTGQLVAIKIIRNKK----RFHQQALVEVKILKHLNDndpddkHNIVRYKD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 122 VFENSSKIVIVMEYASRgDLYDYISERP--RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANG--NIKIAD 197
Cdd:cd14210  83 SFIFRGHLCIVFELLSI-NLYELLKSNNfqGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSksSIKVID 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27229182 198 FGLSNLYHKGKFlqTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQD 258
Cdd:cd14210 162 FGSSCFEGEKVY--TYIQSRFYRAPEVILGLPY-DTAIDMWSLGCILAELYTGYPLFPGEN 219
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
57-309 1.05e-36

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: 139.67  E-value: 1.05e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRK-DKIKDEQdLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd05599   3 FEPLKVIGRGAFGEVRLVRKkDTGHVYAMKKLRKsEMLEKEQ-VAHVRAERDILAEADNPWVVKLYYSFQDEENLYLIME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFC 214
Cdd:cd05599  82 FLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKKSHLAYSTV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 215 GSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNgaYRE----PPKPS---DACGLIRWL 287
Cdd:cd05599 162 GTPDYIAPEVFLQKGY-GKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMN--WREtlvfPPEVPispEAKDLIERL 238
                       250       260
                ....*....|....*....|....*..
gi 27229182 288 LMVNPTRRAT--LEDVASHWW---VNW 309
Cdd:cd05599 239 LCDAEHRLGAngVEEIKSHPFfkgVDW 265
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
57-307 1.18e-36

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: 138.83  E-value: 1.18e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA--RESsGRLVAIKSIRKDKIKDEQDLL--HIRREIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd14094   5 YELCEVIGKGPFSVVRRCihRET-GQQFAVKIVDVAKFTSSPGLSteDLKREASICHMLKHPHIVELLETYSSDGMLYMV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISERPR----LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL---DANGNIKIADFGLS-NLY 204
Cdd:cd14094  84 FEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAiQLG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 205 HKGKFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKtLVKQISNGAYREPPK-----PSD 279
Cdd:cd14094 164 ESGLVAGGRVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNPRqwshiSES 241
                       250       260
                ....*....|....*....|....*...
gi 27229182 280 ACGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14094 242 AKDLVRRMLMLDPAERITVYEALNHPWI 269
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
56-301 1.33e-36

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: 137.40  E-value: 1.33e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHiRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd08225   1 RYEIIKKIGEGSFGKIYLAKaKSDSEHCVIKEIDLTKMPVKEKEAS-KKEVILLAKMKHPNIVTFFASFQENGRLFIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYIsERPR---LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNI-KIADFGLSN-LYHKGKF 209
Cdd:cd08225  80 YCDGGDLMKRI-NRQRgvlFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARqLNDSMEL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 210 LQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGaYREPPKPS---DACGLIRW 286
Cdd:cd08225 159 AYTCVGTPYYLSPEICQNRPY-NNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQG-YFAPISPNfsrDLRSLISQ 236
                       250
                ....*....|....*
gi 27229182 287 LLMVNPTRRATLEDV 301
Cdd:cd08225 237 LFKVSPRDRPSITSI 251
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
57-304 1.35e-36

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: 139.75  E-value: 1.35e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd05601   3 FEVKNVIGRGHFGEVQVVKEkATGDIYAMKVLKKSETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENLYLVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERP-RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-NLYHKGKFLQTF 213
Cdd:cd05601  83 HPGGDLLSLLSRYDdIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAaKLSSDKTVTSKM 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 -CGSPLYASPEIV-----NGKPYVGPEVDSWSLGVLLYILVHGTMPF-DGQDHKTLVKQIS---NGAYREPPK-PSDACG 282
Cdd:cd05601 163 pVGTPDYIAPEVLtsmngGSKGTYGVECDWWSLGIVAYEMLYGKTPFtEDTVIKTYSNIMNfkkFLKFPEDPKvSESAVD 242
                       250       260
                ....*....|....*....|..
gi 27229182 283 LIRWLLmVNPTRRATLEDVASH 304
Cdd:cd05601 243 LIKGLL-TDAKERLGYEGLCCH 263
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
57-304 1.56e-36

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


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 138.05  E-value: 1.56e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKdKIKDEQDLLHIRrEIEIMSSLN-HPHIIAIHEVFENSSKIVIVME 134
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNkETGELVAIKKMKK-KFYSWEECMNLR-EVKSLRKLNeHPNIVKLKEVFRENDELYFVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASrGDLYDYISER--PRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQT 212
Cdd:cd07830  79 YME-GNLYQLMKDRkgKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREIRSRPPYTD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPYVGPEVDSWSLGVL---LYIL------------------VHGT-MPFDGQDHKTLVKQISnga 270
Cdd:cd07830 158 YVSTRWYRAPEILLRSTSYSSPVDIWALGCImaeLYTLrplfpgsseidqlykicsVLGTpTKQDWPEGYKLASKLG--- 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 27229182 271 YREPPK------------PSDACGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd07830 235 FRFPQFaptslhqlipnaSPEAIDLIKDMLRWDPKKRPTASQALQH 280
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
57-304 2.81e-36

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: 137.15  E-value: 2.81e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVK--KARESSGRLvAIKSIRKdkikdeQDLLHiRREIE-------IMSSLNHPHIIAIHEVFENSS 127
Cdd:cd05609   2 FETIKLISNGAYGAVYlvRHRETRQRF-AMKKINK------QNLIL-RNQIQqvfverdILTFAENPFVVSMYCSFETKR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 128 KIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS------ 201
Cdd:cd05609  74 HLCMVMEYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSkiglms 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 202 ---NLY--HKGKFLQTF-----CGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAY 271
Cdd:cd05609 154 lttNLYegHIEKDTREFldkqvCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEI 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 27229182 272 REPPK----PSDACGLIRWLLMVNPTRR---ATLEDVASH 304
Cdd:cd05609 233 EWPEGddalPDDAQDLITRLLQQNPLERlgtGGAEEVKQH 272
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
57-241 3.62e-36

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: 137.36  E-value: 3.62e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIrkdKIKDEQDLLHIR--REIEIMSSLNHPHIIAIHEVF--ENSSKIVI 131
Cdd:cd07843   7 YEKLNRIEEGTYGVVYRARDkKTGEIVALKKL---KMEKEKEGFPITslREINILLKLQHPNIVTVKEVVvgSNLDKIYM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRgDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYhkgkfl 210
Cdd:cd07843  84 VMEYVEH-DLKSLMETmKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREY------ 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27229182 211 qtfcGSPL-----------YASPEIVNGKPYVGPEVDSWSLG 241
Cdd:cd07843 157 ----GSPLkpytqlvvtlwYRAPELLLGAKEYSTAIDMWSVG 194
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
56-304 6.66e-36

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: 135.59  E-value: 6.66e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKdKIKDEQDLLHIRREIEIMSSL-NHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd13997   1 HFHELEQIGSGSFSEVFKVRSKvDGCLYAVKKSKK-PFRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYISERP---RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLsnLYHKGKFL 210
Cdd:cd13997  80 ELCENGSLQDALEELSpisKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGL--ATRLETSG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 QTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGT-MPFDGQdhktLVKQISNGAYREPPKPSDACGL---IRW 286
Cdd:cd13997 158 DVEEGDSRYLAPELLNENYTHLPKADIFSLGVTVYEAATGEpLPRNGQ----QWQQLRQGKLPLPPGLVLSQELtrlLKV 233
                       250
                ....*....|....*...
gi 27229182 287 LLMVNPTRRATLEDVASH 304
Cdd:cd13997 234 MLDPDPTRRPTADQLLAH 251
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
57-303 1.12e-35

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: 135.32  E-value: 1.12e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE--SSGRLVAIKSI-------RKDKIKDEQDLLHIRREIEIM-SSLNHPHIIAIHEVFENS 126
Cdd:cd08528   2 YAVLELLGSGAFGCVYKVRKksNGQTLLALKEInmtnpafGRTEQERDKSVGDIISEVNIIkEQLRHPNIVRYYKTFLEN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 127 SKIVIVMEY---ASRGDLYDYISER-PRLSERDARHFFRQIVSALHYCH-QNGIVHRDLKLENILLDANGNIKIADFGLS 201
Cdd:cd08528  82 DRLYIVMELiegAPLGEHFSSLKEKnEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDFGLA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 202 NlyHKG---KFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYRepPKPS 278
Cdd:cd08528 162 K--QKGpesSKMTSVVGTILYSCPEIVQNEPY-GEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYE--PLPE 236
                       250       260       270
                ....*....|....*....|....*....|
gi 27229182 279 DA-----CGLIRWLLMVNPTRRATLEDVAS 303
Cdd:cd08528 237 GMysddiTFVIRSCLTPDPEARPDIVEVSS 266
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
57-304 1.19e-35

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: 135.87  E-value: 1.19e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKdkIKDEQDL-LHIRREIEIMSSL---NHPHIIAIHEVF-----ENS 126
Cdd:cd07838   1 YEEVAEIGEGAYGTVYKARDlQDGRFVALKKVRV--PLSEEGIpLSTIREIALLKQLesfEHPNVVRLLDVChgprtDRE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 127 SKIVIVMEYASRgDLYDYISERPR--LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLY 204
Cdd:cd07838  79 LKLTLVFEHVDQ-DLATYLDKCPKpgLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARIY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 205 HKGKFLQTFCGSPLYASPEIVNGKPYVGPeVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQI------------------ 266
Cdd:cd07838 158 SFEMALTSVVVTLWYRAPEVLLQSSYATP-VDMWSVGCIFAELFNRRPLFRGSSEADQLGKIfdviglpseeewprnsal 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 27229182 267 --SNGAYREPPKPSDAC--------GLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd07838 237 prSSFPSYTPRPFKSFVpeideeglDLLKKMLTFNPHKRISAFEALQH 284
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
61-307 1.26e-35

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: 134.84  E-value: 1.26e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKA-RESSGRLVAIKSIR--KDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYAS 137
Cdd:cd06632   6 QLLGSGSFGSVYEGfNGDTGDFFAVKEVSlvDDDKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVP 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 138 RGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCGSP 217
Cdd:cd06632  86 GGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAKSFKGSP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 218 LYASPEIVNGK-PYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAyREPPKPS----DACGLIRWLLMVNP 292
Cdd:cd06632 166 YWMAPEVIMQKnSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSG-ELPPIPDhlspDAKDFIRLCLQRDP 244
                       250
                ....*....|....*
gi 27229182 293 TRRATLEDVASHWWV 307
Cdd:cd06632 245 EDRPTASQLLEHPFV 259
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
55-307 1.29e-35

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: 135.86  E-value: 1.29e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  55 HRYEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDK-----------------------IKDEQDLLHIRREIEIMSS 110
Cdd:cd14199   2 NQYKLKDEIGKGSYGVVKLAyNEDDNTYYAMKVLSKKKlmrqagfprrppprgaraapegcTQPRGPIERVYQEIAILKK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 111 LNHPHIIAIHEVFENSSK--IVIVMEYASRGDLYDYISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLD 188
Cdd:cd14199  82 LDHPNVVKLVEVLDDPSEdhLYMVFELVKQGPVMEVPTLKP-LSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 189 ANGNIKIADFGLSNLYhKGK--FLQTFCGSPLYASPEIVNG--KPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVK 264
Cdd:cd14199 161 EDGHIKIADFGVSNEF-EGSdaLLTNTVGTPAFMAPETLSEtrKIFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLHS 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 27229182 265 QISNGAYREPPKP---SDACGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14199 240 KIKTQPLEFPDQPdisDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
57-307 1.35e-35

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: 134.57  E-value: 1.35e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVaiksIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14111   5 YTFLDEKARGRFGVIRRCREnATGKNF----PAKIVPYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQ--TF 213
Cdd:cd14111  81 CSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSLRQlgRR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNG---AYREPPKPSDACGL-IRWLLM 289
Cdd:cd14111 161 TGTLEYMAPEMVKGEP-VGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAkfdAFKLYPNVSQSASLfLKKVLS 239
                       250
                ....*....|....*...
gi 27229182 290 VNPTRRATLEDVASHWWV 307
Cdd:cd14111 240 SYPWSRPTTKDCFAHAWL 257
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
56-304 1.74e-35

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: 134.47  E-value: 1.74e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKV-----KKARESsGRLVAIKSIRKDKIKdEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIV 130
Cdd:cd08222   1 RYRVVRKLGSGNFGTVylvsdLKATAD-EELKVLKEISVGELQ-PDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 IVMEYASRGDLYDYISE----RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLdANGNIKIADFGLSN-LYH 205
Cdd:cd08222  79 IVTEYCEGGDLDDKISEykksGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISRiLMG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 206 KGKFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK--PSDACGL 283
Cdd:cd08222 158 TSDLATTFTGTPYYMSPEVLKHEGY-NSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETPSLPDkySKELNAI 236
                       250       260
                ....*....|....*....|.
gi 27229182 284 IRWLLMVNPTRRATLEDVASH 304
Cdd:cd08222 237 YSRMLNKDPALRPSAAEILKI 257
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
57-308 1.93e-35

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: 134.87  E-value: 1.93e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIrkdKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd06611   7 WEIIGELGDGAFGKVYKAQhKETGLFAAAKII---QIESEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-NLYHKGKFLQTF 213
Cdd:cd06611  84 CDGGALDSIMLELERgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSaKNKSTLQKRDTF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CGSPLYASPEIVN-----GKPYvGPEVDSWSLGVLLYILVHGTMPF-DGQDHKTLVKQISNgayrEPPK---PSdacgli 284
Cdd:cd06611 164 IGTPYWMAPEVVAcetfkDNPY-DYKADIWSLGITLIELAQMEPPHhELNPMRVLLKILKS----EPPTldqPS------ 232
                       250       260       270
                ....*....|....*....|....*....|....
gi 27229182 285 RW----------LLMVNPTRRATLEDVASHWWVN 308
Cdd:cd06611 233 KWsssfndflksCLVKDPDDRPTAAELLKHPFVS 266
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
61-307 2.84e-35

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: 134.85  E-value: 2.84e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIkdeqdllHIR----REIEIMSSL-NHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14090   8 ELLGEGAYASVQTCINlYTGKEYAVKIIEKHPG-------HSRsrvfREVETLHQCqGHPNILQLIEYFEDDERFYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNI---KIADFGLSNLYHKGKF-- 209
Cdd:cd14090  81 KMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVspvKICDFDLGSGIKLSSTsm 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 210 -------LQTFCGSPLYASPEIVNGkpYVG------PEVDSWSLGVLLYILVHGTMPFDG--------------QD-HKT 261
Cdd:cd14090 161 tpvttpeLLTPVGSAEYMAPEVVDA--FVGealsydKRCDLWSLGVILYIMLCGYPPFYGrcgedcgwdrgeacQDcQEL 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 27229182 262 LVKQISNGAYREPPK-----PSDACGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14090 239 LFHSIQEGEYEFPEKewshiSAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
38-327 3.47e-35

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: 137.09  E-value: 3.47e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  38 LMKKQAvkRHHHKHnlrhrYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHI 116
Cdd:cd05600   1 LRKRRT--RLKLSD-----FQILTQVGQGGYGSVFLARKkDTGEICALKIMKKKVLFKLNEVNHVLTERDILTTTNSPWL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 117 IAIHEVFENSSKIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIA 196
Cdd:cd05600  74 VKLLYAFQDPENVYLAMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 197 DFGLS---------------------------------NLYHK-----GKFLQTFCGSPLYASPEIVNGKPYvGPEVDSW 238
Cdd:cd05600 154 DFGLAsgtlspkkiesmkirleevkntafleltakerrNIYRAmrkedQNYANSVVGSPDYMAPEVLRGEGY-DLTVDYW 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 239 SLGVLLYILVHGTMPFDGQD-----------HKTLVKQISNGAYREPPKPSDACGLIRWLLMVNPTRRATLEDVASHWW- 306
Cdd:cd05600 233 SLGCILFECLVGFPPFSGSTpnetwanlyhwKKTLQRPVYTDPDLEFNLSDEAWDLITKLITDPQDRLQSPEQIKNHPFf 312
                       330       340
                ....*....|....*....|...
gi 27229182 307 --VNWgyttgvgeqEALREGGHP 327
Cdd:cd05600 313 knIDW---------DRLREGSKP 326
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
48-310 4.39e-35

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: 134.78  E-value: 4.39e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  48 HHKHNLRHRyefleTLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQdllhirREIEIMSSLN-HPHIIAIHEVFEN 125
Cdd:cd14179   5 HYELDLKDK-----PLGEGSFSICRKClHKKTNQEYAVKIVSKRMEANTQ------REIAALKLCEgHPNIVKLHEVYHD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 126 SSKIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL---DANGNIKIADFGLSN 202
Cdd:cd14179  74 QLHTFLVMELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFAR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 203 LY-HKGKFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDhKTL--------VKQISNG---- 269
Cdd:cd14179 154 LKpPDNQPLKTPCFTLHYAAPELLNYNGY-DESCDLWSLGVILYTMLSGQVPFQCHD-KSLtctsaeeiMKKIKQGdfsf 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 27229182 270 ---AYREPPKpsDACGLIRWLLMVNPTRRATLEDVASHWWVNWG 310
Cdd:cd14179 232 egeAWKNVSQ--EAKDLIQGLLTVDPNKRIKMSGLRYNEWLQDG 273
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
58-308 5.69e-35

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: 133.24  E-value: 5.69e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  58 EFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYA 136
Cdd:cd06605   4 EYLGELGEGNGGVVSKVRhRPSGQIMAVKVIRLEIDEALQK--QILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 137 SRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQN-GIVHRDLKLENILLDANGNIKIADFGLSnlyhkGKFL----Q 211
Cdd:cd06605  82 DGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVS-----GQLVdslaK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKT------LVKQISNGayrEPPK------PSD 279
Cdd:cd06605 157 TFVGTRSYMAPERISGGKY-TVKSDIWSLGLSLVELATGRFPYPPPNAKPsmmifeLLSYIVDE---PPPLlpsgkfSPD 232
                       250       260
                ....*....|....*....|....*....
gi 27229182 280 ACGLIRWLLMVNPTRRATLEDVASHWWVN 308
Cdd:cd06605 233 FQDFVSQCLQKDPTERPSYKELMEHPFIK 261
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
56-295 1.83e-34

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 137.31  E-value: 1.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   56 RYEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIkDEQDLLHIRREIEIMSSLNHPHIIAIHEVF--------ENS 126
Cdd:PTZ00283  33 KYWISRVLGSGATGTVLCAkRVSDGEPFAVKVVDMEGM-SEADKNRAQAEVCCLLNCDFFSIVKCHEDFakkdprnpENV 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  127 SKIVIVMEYASRGDLYDYISERPRLS----ERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN 202
Cdd:PTZ00283 112 LMIALVLDYANAGDLRQEIKSRAKTNrtfrEHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSK 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  203 LYH---KGKFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQD-----HKTLvkqisngAYREP 274
Cdd:PTZ00283 192 MYAatvSDDVGRTFCGTPYYVAPEIWRRKPY-SKKADMFSLGVLLYELLTLKRPFDGENmeevmHKTL-------AGRYD 263
                        250       260
                 ....*....|....*....|....*
gi 27229182  275 PKPS----DACGLIRWLLMVNPTRR 295
Cdd:PTZ00283 264 PLPPsispEMQEIVTALLSSDPKRR 288
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
63-304 2.03e-34

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: 130.69  E-value: 2.03e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAReSSGRLVAIKSIRKDKikdEQDLLHIRReieimssLNHPHIIAIHEVFENSSKIVIVMEYASRGDLY 142
Cdd:cd14059   1 LGSGAQGAVFLGK-FRGEEVAVKKVRDEK---ETDIKHLRK-------LNHPNIIKFKGVCTQAPCYCILMEYCPYGQLY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 143 DYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCGSPLYASP 222
Cdd:cd14059  70 EVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKMSFAGTVAWMAP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 223 EIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREpPKPSDACGLIRWLLMV----NPTRRATL 298
Cdd:cd14059 150 EVIRNEP-CSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLQL-PVPSTCPDGFKLLMKQcwnsKPRNRPSF 227

                ....*.
gi 27229182 299 EDVASH 304
Cdd:cd14059 228 RQILMH 233
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
57-307 2.91e-34

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: 131.44  E-value: 2.91e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKikDEQDLLHIRREIEIMSSLNH---PHIIAIHEVFENSSKIVIV 132
Cdd:cd06917   3 YRRLELVGRGSYGAVYRGYHvKTGRVVALKVLNLDT--DDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKF-LQ 211
Cdd:cd06917  81 MDYCEGGSIRTLMRAGP-IAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSkRS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQIsngAYREPPKPSD------------ 279
Cdd:cd06917 160 TFVGTPYWMAPEVITEGKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLI---PKSKPPRLEGngyspllkefva 236
                       250       260
                ....*....|....*....|....*...
gi 27229182 280 ACglirwlLMVNPTRRATLEDVASHWWV 307
Cdd:cd06917 237 AC------LDEEPKDRLSADELLKSKWI 258
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
61-307 3.20e-34

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: 131.26  E-value: 3.20e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKA-RESSGRLVAIKsIRKDKIKDEQDL-LHIRREieimsslNHPHIIAIHEVFENSSK----IVIVME 134
Cdd:cd14172  10 QVLGLGVNGKVLECfHRRTGQKCALK-LLYDSPKARREVeHHWRAS-------GGPHIVHILDVYENMHHgkrcLLIIME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISER--PRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL---DANGNIKIADFGLSNLYHKGKF 209
Cdd:cd14172  82 CMEGGELFSRIQERgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKETTVQNA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 210 LQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF---DGQD-HKTLVKQISNGAYrEPPKP------SD 279
Cdd:cd14172 162 LQTPCYTPYYVAPEVLGPEKY-DKSCDMWSLGVIMYILLCGFPPFysnTGQAiSPGMKRRIRMGQY-GFPNPewaevsEE 239
                       250       260
                ....*....|....*....|....*...
gi 27229182 280 ACGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14172 240 AKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
56-268 4.37e-34

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: 131.90  E-value: 4.37e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIK---SIRKDKIKdeqdllhirREIEIMSSLN-HPHIIAIHEVF--ENSSK 128
Cdd:cd14132  19 DYEIIRKIGRGKYSEVFEGINiGNNEKVVIKvlkPVKKKKIK---------REIKILQNLRgGPNIVKLLDVVkdPQSKT 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IVIVMEYAsrgDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLD-ANGNIKIADFGLSNLYHKG 207
Cdd:cd14132  90 PSLIFEYV---NNTDFKTLYPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDhEKRKLRLIDWGLAEFYHPG 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27229182 208 KFLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMP-FDGQDHKTLVKQISN 268
Cdd:cd14132 167 QEYNVRVASRYYKGPELLVDYQYYDYSLDMWSLGCMLASMIFRKEPfFHGHDNYDQLVKIAK 228
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
57-306 4.60e-34

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: 131.06  E-value: 4.60e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKikDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd07836   2 FKQLEKLGEGTYATVYKGRnRTTGEIVALKEIHLDA--EEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASrGDLYDYI---SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYhkGKFLQT 212
Cdd:cd07836  80 MD-KDLKKYMdthGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAF--GIPVNT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPL---YASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISN--------------------- 268
Cdd:cd07836 157 FSNEVVtlwYRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRimgtptestwpgisqlpeykp 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 27229182 269 ---------GAYREPPKPSDACGLIRWLLMVNPTRRATLEDVASHWW 306
Cdd:cd07836 237 tfpryppqdLQQLFPHADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
63-265 6.89e-34

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: 130.72  E-value: 6.89e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd05577   1 LGRGGFGEVCACQvKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISE--RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCGSPLY 219
Cdd:cd05577  81 KYHIYNvgTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKIKGRVGTHGY 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 27229182 220 ASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFdgQDHKTLVKQ 265
Cdd:cd05577 161 MAPEVLQKEVAYDFSVDWFALGCMLYEMIAGRSPF--RQRKEKVDK 204
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
61-307 8.15e-34

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: 130.66  E-value: 8.15e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKA-RESSGRLVAIKsIRKDKIKDEQD-LLHIRreieimsSLNHPHIIAIHEVFENS----------SK 128
Cdd:cd14171  12 QKLGTGISGPVRVCvKKSTGERFALK-ILLDRPKARTEvRLHMM-------CSGHPNIVQIYDVYANSvqfpgessprAR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN---IKIADFGLSNLyH 205
Cdd:cd14171  84 LLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEdapIKLCDFGFAKV-D 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 206 KGKfLQTFCGSPLYASPEIVN---------------GKPYV-GPEVDSWSLGVLLYILVHGTMPFDGQDH-----KTLVK 264
Cdd:cd14171 163 QGD-LMTPQFTPYYVAPQVLEaqrrhrkersgiptsPTPYTyDKSCDMWSLGVIIYIMLCGYPPFYSEHPsrtitKDMKR 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 27229182 265 QISNGAYREPPKP----SD-ACGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14171 242 KIMTGSYEFPEEEwsqiSEmAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
56-271 1.11e-33

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: 129.98  E-value: 1.11e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQdllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14104   1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQV---LVKKEISILNIARHRNILRLHESFESHEELVMIFEF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDA--NGNIKIADFGLSNLYHKGKFLQT 212
Cdd:cd14104  78 ISGVDIFERITTaRFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTrrGSYIKIIEFGQSRQLKPGDKFRL 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27229182 213 FCGSPLYASPEIVNGKpYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAY 271
Cdd:cd14104 158 QYTSAEFYAPEVHQHE-SVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEY 215
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
57-305 1.50e-33

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: 129.76  E-value: 1.50e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIrkdKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd06643   7 WEIVGELGDGAFGKVYKAQnKETGILAAAKVI---DTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRG--DLYDYISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNlyHKGKFLQ-- 211
Cdd:cd06643  84 CAGGavDAVMLELERP-LTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSA--KNTRTLQrr 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 -TFCGSPLYASPEIV-----NGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQIsngAYREPP---KPSdacg 282
Cdd:cd06643 161 dSFIGTPYWMAPEVVmcetsKDRPY-DYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKI---AKSEPPtlaQPS---- 232
                       250       260
                ....*....|....*....|....
gi 27229182 283 liRWLLMVNPTRRATLE-DVASHW 305
Cdd:cd06643 233 --RWSPEFKDFLRKCLEkNVDARW 254
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
61-307 1.89e-33

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: 129.04  E-value: 1.89e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQD-------LLHIRREIEIMSSLNHPHIIAiHEVFENSSKIV-I 131
Cdd:cd06629   7 ELIGKGTYGRVYLAMNaTTGEMLAVKQVELPKTSSDRAdsrqktvVDALKSEIDTLKDLDHPNIVQ-YLGFEETEDYFsI 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS----NLY--H 205
Cdd:cd06629  86 FLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISkksdDIYgnN 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 206 KGKFLQtfcGSPLYASPEIV--NGKPYvGPEVDSWSLGVLLYILVHGTMPFdGQDHKTLVKQISNGAYREPPKPSD---- 279
Cdd:cd06629 166 GATSMQ---GSVFWMAPEVIhsQGQGY-SAKVDIWSLGCVVLEMLAGRRPW-SDDEAIAAMFKLGNKRSAPPVPEDvnls 240
                       250       260       270
                ....*....|....*....|....*....|
gi 27229182 280 --ACGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd06629 241 peALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
57-309 3.23e-33

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: 130.16  E-value: 3.23e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd05597   3 FEILKVIGRGAFGEVAVVKLkSTEKVYAMKILNKWEMLKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLVMDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQ--T 212
Cdd:cd05597  83 YCGGDLLTLLSKfEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLKLREDGTVQssV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIV----NGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQdhkTLVK---QISNGAYR------EPPKPSD 279
Cdd:cd05597 163 AVGTPDYISPEILqameDGKGRYGPECDWWSLGVCMYEMLYGETPFYAE---SLVEtygKIMNHKEHfsfpddEDDVSEE 239
                       250       260       270
                ....*....|....*....|....*....|....*
gi 27229182 280 ACGLIRWLLMVNPTR--RATLEDVASHWW---VNW 309
Cdd:cd05597 240 AKDLIRRLICSRERRlgQNGIDDFKKHPFfegIDW 274
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
56-304 4.21e-33

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: 127.55  E-value: 4.21e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARESSGR-------LVAIKSIRKDKIKDEQdllhirrEIEIMSSLNHPHIIAIHEVFENSSK 128
Cdd:cd08223   1 EYQFLRVIGKGSYGEVWLVRHKRDRkqyvikkLNLKNASKRERKAAEQ-------EAKLLSKLKHPNIVSYKESFEGEDG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IV-IVMEYASRGDLYDYISERP--RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN-LY 204
Cdd:cd08223  74 FLyIVMGFCEGGDLYTRLKEQKgvLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARvLE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 205 HKGKFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGayREPPKPSD----A 280
Cdd:cd08223 154 SSSDMATTLIGTPYYMSPELFSNKPY-NHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEG--KLPPMPKQyspeL 230
                       250       260
                ....*....|....*....|....
gi 27229182 281 CGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd08223 231 GELIKAMLHQDPEKRPSVKRILRQ 254
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
63-310 4.69e-33

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: 129.22  E-value: 4.69e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQdllhirREIEIMSSL-NHPHIIAIHEVFENSSKIVIVMEYASRGD 140
Cdd:cd14180  14 LGEGSFSVCRKCRHrQSGQEYAVKIISRRMEANTQ------REVAALRLCqSHPNIVALHEVLHDQYHTYLVMELLRGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 141 LYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN---IKIADFGLSNLYHKG-KFLQTFCGS 216
Cdd:cd14180  88 LLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFARLRPQGsRPLQTPCFT 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 217 PLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKT-------LVKQISNGAYREPPK-----PSDACGLI 284
Cdd:cd14180 168 LQYAAPELFSNQGY-DESCDLWSLGVILYTMLSGQVPFQSKRGKMfhnhaadIMHKIKEGDFSLEGEawkgvSEEAKDLV 246
                       250       260
                ....*....|....*....|....*.
gi 27229182 285 RWLLMVNPTRRATLEDVASHWWVNWG 310
Cdd:cd14180 247 RGLLTVDPAKRLKLSELRESDWLQGG 272
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
54-254 6.73e-33

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: 129.80  E-value: 6.73e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd05596  25 AEDFDVIKVIGRGAFGEVQLVRhKSTKKVYAMKLLSKFEMIKRSDSAFFWEERDIMAHANSEWIVQLHYAFQDDKYLYMV 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISeRPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQ- 211
Cdd:cd05596 105 MDYMPGGDLVNLMS-NYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMKMDKDGLVRs 183
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 27229182 212 -TFCGSPLYASPEIV---NGKPYVGPEVDSWSLGVLLYILVHGTMPF 254
Cdd:cd05596 184 dTAVGTPDYISPEVLksqGGDGVYGRECDWWSVGVFLYEMLVGDTPF 230
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
57-241 1.58e-32

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: 126.85  E-value: 1.58e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRrEIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd07860   2 FQKVEKIGEGTYGVVYKARNkLTGEVVALKKIRLDTETEGVPSTAIR-EISLLKELNHPNIVKLLDVIHTENKLYLVFEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRgDLYDYISERPR--LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYhkGKFLQTF 213
Cdd:cd07860  81 LHQ-DLKKFMDASALtgIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAF--GVPVRTY 157
                       170       180       190
                ....*....|....*....|....*....|.
gi 27229182 214 CGSPL---YASPEIVNGKPYVGPEVDSWSLG 241
Cdd:cd07860 158 THEVVtlwYRAPEILLGCKYYSTAVDIWSLG 188
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
56-244 1.75e-32

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: 127.43  E-value: 1.75e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIrkdKIKDEQDLLHIR--REIEIMSSLNHPHIIAIHE-VFENSSK--- 128
Cdd:cd07866   9 DYEILGKLGEGTFGEVYKARQiKTGRVVALKKI---LMHNEKDGFPITalREIKILKKLKHPNVVPLIDmAVERPDKskr 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 ----IVIVMEYASRgDLYDYIS-ERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL 203
Cdd:cd07866  86 krgsVYMVTPYMDH-DLSGLLEnPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLARP 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 27229182 204 YHKGKFLQTFCGSPL------------YASPEIVNGKPYVGPEVDSWSLGVLL 244
Cdd:cd07866 165 YDGPPPNPKGGGGGGtrkytnlvvtrwYRPPELLLGERRYTTAVDIWGIGCVF 217
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
54-254 1.90e-32

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: 129.74  E-value: 1.90e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd05624  71 RDDFEIIKVIGRGAFGEVAVVKmKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQWITTLHYAFQDENYLYLV 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQ 211
Cdd:cd05624 151 MDYYVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMNDDGTVQ 230
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 27229182 212 T--FCGSPLYASPEIV----NGKPYVGPEVDSWSLGVLLYILVHGTMPF 254
Cdd:cd05624 231 SsvAVGTPDYISPEILqameDGMGKYGPECDWWSLGVCMYEMLYGETPF 279
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
92-297 2.33e-32

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 130.91  E-value: 2.33e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   92 IKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDLYDYISERPR----LSERDARHFFRQIVSAL 167
Cdd:PTZ00267 103 LNDERQAAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRLKehlpFQEYEVGLLFYQIVLAL 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  168 HYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFL---QTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLL 244
Cdd:PTZ00267 183 DEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLdvaSSFCGTPYYLAPELWERKRY-SKKADMWSLGVIL 261
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 27229182  245 YILVHGTMPFDGQDHKTLVKQISNGAYREPPKP--SDACGLIRWLLMVNPTRRAT 297
Cdd:PTZ00267 262 YELLTLHRPFKGPSQREIMQQVLYGKYDPFPCPvsSGMKALLDPLLSKNPALRPT 316
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
57-307 2.41e-32

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: 126.84  E-value: 2.41e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDLLHIRrEIEIMSSLNHPHIIAIHEVFENSSKIV----- 130
Cdd:cd07864   9 FDIIGIIGEGTYGQVYKAKDKdTGELVALKKVRLDNEKEGFPITAIR-EIKILRQLNHRSVVNLKEIVTDKQDALdfkkd 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 -----IVMEYASRgDLYDYI-SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLY 204
Cdd:cd07864  88 kgafyLVFEYMDH-DLMGLLeSGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARLY 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 205 HK-------GKFLQTFcgsplYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISN--------- 268
Cdd:cd07864 167 NSeesrpytNKVITLW-----YRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRlcgspcpav 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27229182 269 --GAYREP------PK--------------PSDACGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd07864 242 wpDVIKLPyfntmkPKkqyrrrlreefsfiPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
57-306 2.43e-32

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 125.40  E-value: 2.43e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDllhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYA 136
Cdd:cd14108   4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTS---ARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 137 SRgDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN--IKIADFGLSNLYHKGKFLQTFC 214
Cdd:cd14108  81 HE-ELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTdqVRICDFGNAQELTPNEPQYCKY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 215 GSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNG--AYREPPKPS---DACGLIRWLLm 289
Cdd:cd14108 160 GTPEFVAPEIVNQSP-VSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYnvAFEESMFKDlcrEAKGFIIKVL- 237
                       250
                ....*....|....*..
gi 27229182 290 VNPTRRATLEDVASHWW 306
Cdd:cd14108 238 VSDRLRPDAEETLEHPW 254
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
40-309 5.51e-32

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 127.02  E-value: 5.51e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   40 KKQAVKRHHHKHNLRHRYE---FLETLGKGTYGKVKKARESSGRL--VAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHP 114
Cdd:PTZ00426  12 KKDSDSTKEPKRKNKMKYEdfnFIRTLGTGSFGRVILATYKNEDFppVAIKRFEKSKIIKQKQVDHVFSERKILNYINHP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  115 HIIAIHEVFENSSKIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIK 194
Cdd:PTZ00426  92 FCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIK 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  195 IADFGLSNLYHKGKFlqTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREP 274
Cdd:PTZ00426 172 MTDFGFAKVVDTRTY--TLCGTPEYIAPEILLNVGH-GKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFP 248
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 27229182  275 PKPSDACG-LIRWLLMVNPTRR-----ATLEDVASHWW---VNW 309
Cdd:PTZ00426 249 KFLDNNCKhLMKKLLSHDLTKRygnlkKGAQNVKEHPWfgnIDW 292
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
113-306 7.53e-32

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: 123.69  E-value: 7.53e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 113 HPHIIAIHEVFENSSKIVIVMEYASrGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN 192
Cdd:cd13976  44 HPNISGVHEVIAGETKAYVFFERDH-GDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEER 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 193 IKIADFGLSNLY-HKGK--FLQTFCGSPLYASPEIVN-GKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISN 268
Cdd:cd13976 123 TKLRLESLEDAViLEGEddSLSDKHGCPAYVSPEILNsGATYSGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRR 202
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 27229182 269 GAYREPP--KPSDACgLIRWLLMVNPTRRATLEDVASHWW 306
Cdd:cd13976 203 GQFAIPEtlSPRARC-LIRSLLRREPSERLTAEDILLHPW 241
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
57-323 8.44e-32

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: 125.14  E-value: 8.44e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIrkdKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd06644  14 WEIIGELGDGAFGKVYKAKnKETGALAAAKVI---ETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEF 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS--NLyhkgKFLQ- 211
Cdd:cd06644  91 CPGGAVDAIMLELDRgLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSakNV----KTLQr 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 --TFCGSPLYASPEIV-----NGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQIsngAYREPP---KPS--- 278
Cdd:cd06644 167 rdSFIGTPYWMAPEVVmcetmKDTPY-DYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKI---AKSEPPtlsQPSkws 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 27229182 279 -DACGLIRWLLMVNPTRRATLEDVASHWWVnwgytTGVGEQEALRE 323
Cdd:cd06644 243 mEFRDFLKTALDKHPETRPSAAQLLEHPFV-----SSVTSNRPLRE 283
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
57-306 9.84e-32

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: 125.17  E-value: 9.84e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDLLHIRrEIEIMSSLNHPHIIAIHEVFENSS--KIVIVM 133
Cdd:cd07845   9 FEKLNRIGEGTYGIVYRARDTtSGEIVALKKVRMDNERDGIPISSLR-EITLLLNLRHPNIVELKEVVVGKHldSIFLVM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRgDLYDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQT 212
Cdd:cd07845  88 EYCEQ-DLASLLDNMPTpFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLPAKPMT 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPL-YASPEIVNGKPYVGPEVDSWSLGVLL-YILVH--------------------GT-----------MPFDGQdh 259
Cdd:cd07845 167 PKVVTLwYRAPELLLGCTTYTTAIDMWAVGCILaELLAHkpllpgkseieqldliiqllGTpnesiwpgfsdLPLVGK-- 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 27229182 260 KTLVKQISNGAYREPPKPSDA-CGLIRWLLMVNPTRRATLEDVASHWW 306
Cdd:cd07845 245 FTLPKQPYNNLKHKFPWLSEAgLRLLNFLLMYDPKKRATAEEALESSY 292
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
56-250 1.06e-31

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


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 124.41  E-value: 1.06e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKsirkdKIKDEQDLLHIR----REIEIMSSLNHPHIIAIHEVFENSSKIV 130
Cdd:cd07847   2 KYEKLSKIGEGSYGVVFKCRNrETGQIVAIK-----KFVESEDDPVIKkialREIRMLKQLKHPNLVNLIEVFRRKRKLH 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 IVMEYASRGDLYDyISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKF 209
Cdd:cd07847  77 LVFEYCDHTVLNE-LEKNPRgVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGD 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27229182 210 LQT-FCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHG 250
Cdd:cd07847 156 DYTdYVATRWYRAPELLVGDTQYGPPVDVWAIGCVFAELLTG 197
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
57-307 1.48e-31

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: 124.36  E-value: 1.48e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKK-ARESSGRLVAIKSIRKDKiKDEQDllhirrEIEIMSSL-NHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14178   5 YEIKEDIGIGSYSVCKRcVHKATSTEYAVKIIDKSK-RDPSE------EIEILLRYgQHPNIITLKDVYDDGKFVYLVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENIL-LDANGN---IKIADFGLS-NLYHKGKF 209
Cdd:cd14178  78 LMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAkQLRAENGL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 210 LQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF-DGQDH--KTLVKQISNGAYREP----PKPSDAC- 281
Cdd:cd14178 158 LMTPCYTANFVAPEVLKRQGY-DAACDIWSLGILLYTMLAGFTPFaNGPDDtpEEILARIGSGKYALSggnwDSISDAAk 236
                       250       260
                ....*....|....*....|....*.
gi 27229182 282 GLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14178 237 DIVSKMLHVDPHQRLTAPQVLRHPWI 262
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
56-307 2.40e-31

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: 123.18  E-value: 2.40e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARES-SGRLVAIKSIrkDKIKDEQDllHIRREIEIMSSL-NHPHIIAIHEVFENSS------ 127
Cdd:cd06608   7 IFELVEVIGEGTYGKVYKARHKkTGQLAAIKIM--DIIEDEEE--EIKLEINILRKFsNHPNIATFYGAFIKKDppggdd 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 128 KIVIVMEYASRG---DLYDYISERP-RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-N 202
Cdd:cd06608  83 QLWLVMEYCGGGsvtDLVKGLRKKGkRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSaQ 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 203 LYHKGKFLQTFCGSPLYASPEIVNGKPYVGPEVDS----WSLGVLLYILVHGTMPF-DGQDHKTLVKQISNgayrEPPK- 276
Cdd:cd06608 163 LDSTLGRRNTFIGTPYWMAPEVIACDQQPDASYDArcdvWSLGITAIELADGKPPLcDMHPMRALFKIPRN----PPPTl 238
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 27229182 277 --PSDAC----GLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd06608 239 ksPEKWSkefnDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
63-304 2.50e-31

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: 122.94  E-value: 2.50e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIK--SIRKDKikdEQDLLHirREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRG 139
Cdd:cd06648  15 IGEGSTGIVCIATDkSTGRQVAVKkmDLRKQQ---RRELLF--NEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYISERpRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFG----LSNLYHKGKFLqtfCG 215
Cdd:cd06648  90 ALTDIVTHT-RMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGfcaqVSKEVPRRKSL---VG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 216 SPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNgayREPPKPSDAC-------GLIRWLL 288
Cdd:cd06648 166 TPYWMAPEVISRLPY-GTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRD---NEPPKLKNLHkvsprlrSFLDRML 241
                       250
                ....*....|....*.
gi 27229182 289 MVNPTRRATLEDVASH 304
Cdd:cd06648 242 VRDPAQRATAAELLNH 257
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
57-307 2.84e-31

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: 123.60  E-value: 2.84e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKiKDEQDllhirrEIEIMSSL-NHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14175   3 YVVKETIGVGSYSVCKRCvHKATNMEYAVKVIDKSK-RDPSE------EIEILLRYgQHPNIITLKDVYDDGKHVYLVTE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENIL-LDANGN---IKIADFGLS-NLYHKGKF 209
Cdd:cd14175  76 LMRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAkQLRAENGL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 210 LQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKT---LVKQISNGAYREPPKPSDACG---- 282
Cdd:cd14175 156 LMTPCYTANFVAPEVLKRQGY-DEGCDIWSLGILLYTMLAGYTPFANGPSDTpeeILTRIGSGKFTLSGGNWNTVSdaak 234
                       250       260
                ....*....|....*....|....*.
gi 27229182 283 -LIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14175 235 dLVSKMLHVDPHQRLTAKQVLQHPWI 260
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
56-304 3.61e-31

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: 122.79  E-value: 3.61e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRkdkIKDEQDLLHIRREIEIMSSLNHPHII-----AIHEVFENSSKI 129
Cdd:cd13986   1 RYRIQRLLGEGGFSFVYLVEDlSTGRLYALKKIL---CHSKEDVKEAMREIENYRLFNHPNILrlldsQIVKEAGGKKEV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 130 VIVMEYASRGDLYDYIS----ERPRLSERDARHFFRQIVSALHYCHQNGIV---HRDLKLENILLDANGNIKIADFGLSN 202
Cdd:cd13986  78 YLLLPYYKRGSLQDEIErrlvKGTFFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPILMDLGSMN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 203 L-------YHKGKFLQTFC---GSPLYASPEIVNGKPY--VGPEVDSWSLGVLLYILVHGTMPFD--GQDHKTLVKQISN 268
Cdd:cd13986 158 ParieiegRREALALQDWAaehCTMPYRAPELFDVKSHctIDEKTDIWSLGCTLYALMYGESPFEriFQKGDSLALAVLS 237
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 27229182 269 GAYREPPKPS---DACGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd13986 238 GNYSFPDNSRyseELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
63-304 3.65e-31

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: 122.64  E-value: 3.65e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDLLH------IRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd06628   8 IGSGSFGSVYLGMNAsSGELMAVKQVELPSVSAENKDRKksmldaLQREIALLRELQHENIVQYLGSSSDANHLNIFLEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN-------LYHKGK 208
Cdd:cd06628  88 VPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKkleanslSTKNNG 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTFCGSPLYASPEIVNGKPYVgPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK--PSDACGLIRW 286
Cdd:cd06628 168 ARPSLQGSVFWMAPEVVKQTSYT-RKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIGENASPTIPSniSSEARDFLEK 246
                       250
                ....*....|....*...
gi 27229182 287 LLMVNPTRRATLEDVASH 304
Cdd:cd06628 247 TFEIDHNKRPTADELLKH 264
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
36-304 5.62e-31

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: 125.51  E-value: 5.62e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  36 KPLMKKQAVKRHHhkhnlRHRYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHP 114
Cdd:cd05623  58 KPFTSKVKQMRLH-----KEDFEILKVIGRGAFGEVAVVKlKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSQ 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 115 HIIAIHEVFENSSKIVIVMEYASRGDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNI 193
Cdd:cd05623 133 WITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHI 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 194 KIADFGLS-NLYHKGKFLQTFC-GSPLYASPEIV----NGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQIS 267
Cdd:cd05623 213 RLADFGSClKLMEDGTVQSSVAvGTPDYISPEILqameDGKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIM 292
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 27229182 268 NGA--YREPPKPSD----ACGLIRWLLMVNPTR--RATLEDVASH 304
Cdd:cd05623 293 NHKerFQFPTQVTDvsenAKDLIRRLICSREHRlgQNGIEDFKNH 337
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
60-307 1.03e-30

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: 121.76  E-value: 1.03e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  60 LETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVF--ENSSKIVIVMEYA 136
Cdd:cd06621   6 LSSLGEGAGGSVTKCRlRNTKTIFALKTITTDPNPDVQK--QILRELEINKSCASPYIVKYYGAFldEQDSSIGIAMEYC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 137 SRGDLyDYI-----SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSnlyhkGKFLQ 211
Cdd:cd06621  84 EGGSL-DSIykkvkKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVS-----GELVN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 ----TFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF--DGQDHKTLVKQISNGAYREPPKPSDACGL-I 284
Cdd:cd06621 158 slagTFTGTSYYMAPERIQGGPY-SITSDVWSLGLTLLEVAQNRFPFppEGEPPLGPIELLSYIVNMPNPELKDEPENgI 236
                       250       260       270
                ....*....|....*....|....*....|...
gi 27229182 285 RW----------LLMVNPTRRATLEDVASHWWV 307
Cdd:cd06621 237 KWsesfkdfiekCLEKDGTRRPGPWQMLAHPWI 269
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
61-307 1.08e-30

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: 121.68  E-value: 1.08e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLhirREIEIMSSLN-HPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd14174   8 ELLGEGAYAKVQGCVSlQNGKEYAVKIIEKNAGHSRSRVF---REVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLRG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL---DANGNIKIADFGLSNLYHKGKF------ 209
Cdd:cd14174  85 GSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCespDKVSPVKICDFDLGSGVKLNSActpitt 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 210 --LQTFCGSPLYASPEIV----NGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQ---------------DHKTLVKQISN 268
Cdd:cd14174 165 peLTTPCGSAEYMAPEVVevftDEATFYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwdrgevcrvCQNKLFESIQE 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 27229182 269 GAYREPPK-----PSDACGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14174 245 GKYEFPDKdwshiSSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
57-306 1.22e-30

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: 120.76  E-value: 1.22e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIR-KDKIKDEQdllhiRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14107   4 YEVKEEIGRGTFGFVKRVtHKGNGECCAAKFIPlRSSTRARA-----FQERDILARLSHRRLTCLLDQFETRKTLILILE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL--DANGNIKIADFGLSNLYHKGKFLQT 212
Cdd:cd14107  79 LCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFAQEITPSEHQFS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQ-DHKTLVKQISNGAYREPP----KPSDACGLIRWL 287
Cdd:cd14107 159 KYGSPEFVAPEIVHQEP-VSAATDIWALGVIAYLSLTCHSPFAGEnDRATLLNVAEGVVSWDTPeithLSEDAKDFIKRV 237
                       250
                ....*....|....*....
gi 27229182 288 LMVNPTRRATLEDVASHWW 306
Cdd:cd14107 238 LQPDPEKRPSASECLSHEW 256
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
57-254 1.54e-30

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: 123.96  E-value: 1.54e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARESSGRLV-AIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd05622  75 YEVVKVIGRGAFGEVQLVRHKSTRKVyAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQ--TF 213
Cdd:cd05622 155 MPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRcdTA 233
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 27229182 214 CGSPLYASPEIVN---GKPYVGPEVDSWSLGVLLYILVHGTMPF 254
Cdd:cd05622 234 VGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPF 277
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
63-300 1.59e-30

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: 121.14  E-value: 1.59e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd05608   9 LGKGGFGEVSACqMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNGGDL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 ----YDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-NLYHKGKFLQTFCGS 216
Cdd:cd05608  89 ryhiYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAvELKDGQTKTKGYAGT 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 217 PLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQ----DHKTLVKQISNGAYREPPKPSDAC-GLIRWLLMVN 291
Cdd:cd05608 169 PGFMAPELLLGEEY-DYSVDYFTLGVTLYEMIAARGPFRARgekvENKELKQRILNDSVTYSEKFSPASkSICEALLAKD 247

                ....*....
gi 27229182 292 PTRRATLED 300
Cdd:cd05608 248 PEKRLGFRD 256
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
61-308 1.60e-30

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: 121.68  E-value: 1.60e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKA-RESSGRLVAIKSIrkdkikdeQDLLHIRREIEIMSSLNH-PHIIAIHEVFENSSK----IVIVME 134
Cdd:cd14170   8 QVLGLGINGKVLQIfNKRTQEKFALKML--------QDCPKARREVELHWRASQcPHIVRIVDVYENLYAgrkcLLIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISER--PRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDA---NGNIKIADFGLSNLYHKGKF 209
Cdd:cd14170  80 CLDGGELFSRIQDRgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETTSHNS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 210 LQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFdGQDHKTLV-----KQISNGAYrEPPKPS------ 278
Cdd:cd14170 160 LTTPCYTPYYVAPEVLGPEKY-DKSCDMWSLGVIMYILLCGYPPF-YSNHGLAIspgmkTRIRMGQY-EFPNPEwsevse 236
                       250       260       270
                ....*....|....*....|....*....|
gi 27229182 279 DACGLIRWLLMVNPTRRATLEDVASHWWVN 308
Cdd:cd14170 237 EVKMLIRNLLKTEPTQRMTITEFMNHPWIM 266
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
63-307 1.81e-30

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: 120.52  E-value: 1.81e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDE--QDLLHIRREIEIMSSLNHPHIIAIHEVFEN--SSKIVIVMEYAS 137
Cdd:cd06653  10 LGRGAFGEVYLCYDAdTGRELAVKQVPFDPDSQEtsKEVNALECEIQLLKNLRHDRIVQYYGCLRDpeEKKLSIFVEYMP 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 138 RGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS----NLYHKGKFLQTF 213
Cdd:cd06653  90 GGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkriqTICMSGTGIKSV 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAY--REPPKPSDACGLIRWLLMVN 291
Cdd:cd06653 170 TGTPYWMSPEVISGEGY-GRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTkpQLPDGVSDACRDFLRQIFVE 248
                       250
                ....*....|....*.
gi 27229182 292 PTRRATLEDVASHWWV 307
Cdd:cd06653 249 EKRRPTAEFLLRHPFV 264
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
55-257 2.67e-30

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


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 120.49  E-value: 2.67e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  55 HRYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIrKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd07848   1 NKFEVLGVVGEGAYGVVLKCRhKETKEIVAIKKF-KDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRgDLYDYISERPRLSERD-ARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGK--FL 210
Cdd:cd07848  80 EYVEK-NMLELLEEMPNGVPPEkVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSnaNY 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 27229182 211 QTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQ 257
Cdd:cd07848 159 TEYVATRWYRSPELLLGAPY-GKAVDMWSVGCILGELSDGQPLFPGE 204
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
54-304 2.75e-30

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: 120.03  E-value: 2.75e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIR-KDKIKDEQdllhIRREIEIMSSLNHPHIIAIHEVFENSSKIVI 131
Cdd:cd06647   6 KKKYTRFEKIGQGASGTVYTAIDvATGQEVAIKQMNlQQQPKKEL----IINEILVMRENKNPNIVNYLDSYLVGDELWV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDYISErPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL-SNLYHKGKFL 210
Cdd:cd06647  82 VMEYLAGGSLTDVVTE-TCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSKR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 QTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDACGLIRWL--- 287
Cdd:cd06647 161 STMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFlnr 239
                       250
                ....*....|....*...
gi 27229182 288 -LMVNPTRRATLEDVASH 304
Cdd:cd06647 240 cLEMDVEKRGSAKELLQH 257
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
42-307 3.27e-30

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: 121.67  E-value: 3.27e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  42 QAVKRHHHKHNLRHR--YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKiKDEQDllhirrEIEIMSSL-NHPHII 117
Cdd:cd14176   4 HSIVQQLHRNSIQFTdgYEVKEDIGVGSYSVCKRCiHKATNMEFAVKIIDKSK-RDPTE------EIEILLRYgQHPNII 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 118 AIHEVFENSSKIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENIL-LDANGN---I 193
Cdd:cd14176  77 TLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesI 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 194 KIADFGLS-NLYHKGKFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF-DGQDH--KTLVKQISNG 269
Cdd:cd14176 157 RICDFGFAkQLRAENGLLMTPCYTANFVAPEVLERQGY-DAACDIWSLGVLLYTMLTGYTPFaNGPDDtpEEILARIGSG 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 27229182 270 AYREP-----PKPSDACGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14176 236 KFSLSggywnSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 278
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
92-306 3.62e-30

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


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 119.00  E-value: 3.62e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  92 IKDEQDllHIRREIEIMSslnHPHIIAIHEVFENSSKIVIVMEyASRGDLYDYISERPRLSERDARHFFRQIVSALHYCH 171
Cdd:cd14023  28 LKHYQD--KIRPYIQLPS---HRNITGIVEVILGDTKAYVFFE-KDFGDMHSYVRSCKRLREEEAARLFKQIVSAVAHCH 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 172 QNGIVHRDLKLENILLDANGNIKIADFGLSNLY-HKGK--FLQTFCGSPLYASPEIVNGK-PYVGPEVDSWSLGVLLYIL 247
Cdd:cd14023 102 QSAIVLGDLKLRKFVFSDEERTQLRLESLEDTHiMKGEddALSDKHGCPAYVSPEILNTTgTYSGKSADVWSLGVMLYTL 181
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27229182 248 VHGTMPFDGQDHKTLVKQISNGAYREPP--KPSDACgLIRWLLMVNPTRRATLEDVASHWW 306
Cdd:cd14023 182 LVGRYPFHDSDPSALFSKIRRGQFCIPDhvSPKARC-LIRSLLRREPSERLTAPEILLHPW 241
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
57-307 5.04e-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: 118.91  E-value: 5.04e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARES-SGRLVAIKSIR--KDKIKDEQDllhirrEIEIMSSLN------HPHIIAIHEVFENSS 127
Cdd:cd14133   1 YEVLEVLGKGTFGQVVKCYDLlTGEEVALKIIKnnKDYLDQSLD------EIRLLELLNkkdkadKYHIVRLKDVFYFKN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 128 KIVIVMEYASRgDLYDYISE--RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANG--NIKIADFGLSNL 203
Cdd:cd14133  75 HLCIVFELLSQ-NLYEFLKQnkFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSrcQIKIIDFGSSCF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 204 YHKGkfLQTFCGSPLYASPEIVNGKPYVGPeVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDACG- 282
Cdd:cd14133 154 LTQR--LYSYIQSRYYRAPEVILGLPYDEK-IDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMLDQGKa 230
                       250       260       270
                ....*....|....*....|....*....|..
gi 27229182 283 -------LIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14133 231 ddelfvdFLKKLLEIDPKERPTASQALSHPWL 262
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
56-304 5.18e-30

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: 119.91  E-value: 5.18e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKikdeqdllHIR-REIEIMSSLNHPHIIAIHEVF----ENSSKI 129
Cdd:cd14137   5 SYTIEKVIGSGSFGVVYQAKlLETGEVVAIKKVLQDK--------RYKnRELQIMRRLKHPNIVKLKYFFyssgEKKDEV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 130 V--IVMEYASrGDLYDYISE----RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLD-ANGNIKIADFGLSn 202
Cdd:cd14137  77 YlnLVMEYMP-ETLYRVIRHysknKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDpETGVLKLCDFGSA- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 203 lyhkgKFLQT-------FCgSPLYASPEIVNGKPYVGPEVDSWSLG------VLLYILVHGTmpfDGQDHktLVKQI--- 266
Cdd:cd14137 155 -----KRLVPgepnvsyIC-SRYYRAPELIFGATDYTTAIDIWSAGcvlaelLLGQPLFPGE---SSVDQ--LVEIIkvl 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27229182 267 ----------SNGAYREPP----------------KPSDACGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd14137 224 gtptreqikaMNPNYTEFKfpqikphpwekvfpkrTPPDAIDLLSKILVYNPSKRLTALEALAH 287
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
50-307 7.33e-30

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: 120.74  E-value: 7.33e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  50 KHNLRhRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRkDKIKDEQDLLHIRREIEIMSSLN-HPHIIAIHEVF--EN 125
Cdd:cd07852   3 KHILR-RYEILKKLGKGAYGIVWKAIDkKTGEVVALKKIF-DAFRNATDAQRTFREIMFLQELNdHPNIIKLLNVIraEN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 126 SSKIVIVMEYASRgDLYDYIseRPRLSERDARHF-FRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS--- 201
Cdd:cd07852  81 DKDIYLVFEYMET-DLHAVI--RANILEDIHKQYiMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLArsl 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 202 ---NLYHKGKFLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDG-------------------QDH 259
Cdd:cd07852 158 sqlEEDDENPVLTDYVATRWYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGKPLFPGtstlnqlekiievigrpsaEDI 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27229182 260 KTLV-----KQISNGAYREPPK--------PSDACGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd07852 238 ESIQspfaaTMLESLPPSRPKSldelfpkaSPDALDLLKKLLVFNPNKRLTAEEALRHPYV 298
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
63-306 7.68e-30

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: 118.14  E-value: 7.68e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQdllhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd14115   1 IGRGRFSIVKKClHKATRKDVAVKFVSKKMKKKEQ----AAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDAN---GNIKIADFG----LSNLYHKGKFLqtfc 214
Cdd:cd14115  77 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRipvPRVKLIDLEdavqISGHRHVHHLL---- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 215 GSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK-----PSDACGLIRWLLM 289
Cdd:cd14115 153 GNPEFAAPEVIQGTP-VSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEyfgdvSQAARDFINVILQ 231
                       250
                ....*....|....*..
gi 27229182 290 VNPTRRATLEDVASHWW 306
Cdd:cd14115 232 EDPRRRPTAATCLQHPW 248
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
56-254 9.06e-30

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: 118.10  E-value: 9.06e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RY-EFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKdEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSK--IVI 131
Cdd:cd13983   1 RYlKFNEVLGRGSFKTVYRAfDTEEGIEVAWNEIKLRKLP-KAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKkeVIF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCH--QNGIVHRDLKLENILLDAN-GNIKIADFGLSNLYhKGK 208
Cdd:cd13983  80 ITELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHtrDPPIIHRDLKCDNIFINGNtGEVKIGDLGLATLL-RQS 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 27229182 209 FLQTFCGSPLYASPEIVNGKpYvGPEVDSWSLGVLLYILVHGTMPF 254
Cdd:cd13983 159 FAKSVIGTPEFMAPEMYEEH-Y-DEKVDIYAFGMCLLEMATGEYPY 202
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
57-307 9.82e-30

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: 119.35  E-value: 9.82e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARESSGRL-VAIKSIRKDKiKDEQDllhirrEIEI-MSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14177   6 YELKEDIGVGSYSVCKRCIHRATNMeFAVKIIDKSK-RDPSE------EIEIlMRYGQHPNIITLKDVYDDGRYVYLVTE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENIL-LDANGN---IKIADFGLS-NLYHKGKF 209
Cdd:cd14177  79 LMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAkQLRGENGL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 210 LQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKT---LVKQISNGAYREPPKPSD-----AC 281
Cdd:cd14177 159 LLTPCYTANFVAPEVLMRQGY-DAACDIWSLGVLLYTMLAGYTPFANGPNDTpeeILLRIGSGKFSLSGGNWDtvsdaAK 237
                       250       260
                ....*....|....*....|....*.
gi 27229182 282 GLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14177 238 DLLSHMLHVDPHQRYTAEQVLKHSWI 263
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
50-306 1.06e-29

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 120.25  E-value: 1.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   50 KHNLRHRYEFLET-LGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDLLH-----------IRREIEIMSSLNHPHI 116
Cdd:PTZ00024   3 SFSISERYIQKGAhLGEGTYGKVEKAYDTlTGKIVAIKKVKIIEISNDVTKDRqlvgmcgihftTLRELKIMNEIKHENI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  117 IAIHEVFENSSKIVIVMEYASrGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIA 196
Cdd:PTZ00024  83 MGLVDVYVEGDFINLVMDIMA-SDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  197 DFGLSNLYHKGKFLQTFCGSPL---------------YASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKT 261
Cdd:PTZ00024 162 DFGLARRYGYPPYSDTLSKDETmqrreemtskvvtlwYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEID 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27229182  262 LVKQI-------SNGAYRE-----------PPKP-----------SDACGLIRWLLMVNPTRRATLEDVASHWW 306
Cdd:PTZ00024 242 QLGRIfellgtpNEDNWPQakklplyteftPRKPkdlktifpnasDDAIDLLQSLLKLNPLERISAKEALKHEY 315
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
56-266 1.13e-29

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: 118.69  E-value: 1.13e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKiKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd07839   1 KYEKLEKIGEGTYGTVFKAKNrETHEIVALKRVRLDD-DDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRgDLYDYI-SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYhkGKFLQTF 213
Cdd:cd07839  80 YCDQ-DLKKYFdSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAF--GIPVRCY 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 27229182 214 CGSPL---YASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMP-FDGQDHKTLVKQI 266
Cdd:cd07839 157 SAEVVtlwYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPlFPGNDVDDQLKRI 213
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
54-245 1.15e-29

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: 118.64  E-value: 1.15e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYeFLETLGKGTYGKVKKAR-----ESSGRLVAIKSIRKDKikDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSK 128
Cdd:cd05038   4 RHLK-FIKQLGEGHFGSVELCRydplgDNTGEQVAVKSLQPSG--EEQHMSDFKREIEILRTLDHEYIVKYKGVCESPGR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 --IVIVMEYASRGDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL-- 203
Cdd:cd05038  81 rsLRLIMEYLPSGSLRDYLQRhRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVlp 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 27229182 204 ----YHKGKFLQTfcgSPL--YASPEIVNGKPYVgpEVDSWSLGVLLY 245
Cdd:cd05038 161 edkeYYYVKEPGE---SPIfwYAPECLRESRFSS--ASDVWSFGVTLY 203
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
52-304 1.32e-29

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: 119.72  E-value: 1.32e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  52 NLRHRYEFLETLGKGTYGKVKKARES-SGRLVAIKsirkdKIKD-EQDLLHIR--REIEIMSSLNHPHIIAIHEV----- 122
Cdd:cd07849   2 DVGPRYQNLSYIGEGAYGMVCSAVHKpTGQKVAIK-----KISPfEHQTYCLRtlREIKILLRFKHENIIGILDIqrppt 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 123 FENSSKIVIVMEYASRgDLYDYISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN 202
Cdd:cd07849  77 FESFKDVYIVQELMET-DLYKLIKTQH-LSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLAR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 203 LY-----HKGkFLQTFCGSPLYASPEI-VNGKPYVgPEVDSWSLGVLLYILVHGTMPFDGQDHK---TLVKQ-------- 265
Cdd:cd07849 155 IAdpehdHTG-FLTEYVATRWYRAPEImLNSKGYT-KAIDIWSVGCILAEMLSNRPLFPGKDYLhqlNLILGilgtpsqe 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 266 ----ISNGAYRE-----PPKP------------SDACGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd07849 233 dlncIISLKARNyikslPFKPkvpwnklfpnadPKALDLLDKMLTFNPHKRITVEEALAH 292
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
59-262 1.81e-29

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: 117.48  E-value: 1.81e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  59 FLETLGKGTYGKVKKArESSGRLVAIKSIRKDKiKDEQDLLHIRREIEImSSLNHPHII---AIHEVFENSSKIVIVMEY 135
Cdd:cd13979   7 LQEPLGSGGFGSVYKA-TYKGETVAVKIVRRRR-KNRASRQSFWAELNA-ARLRHENIVrvlAAETGTDFASLGLIIMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQT-- 212
Cdd:cd13979  84 CGNGTLQQLIYEgSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEGNEVGTpr 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 27229182 213 --FCGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTL 262
Cdd:cd13979 164 shIGGTYTYRAPELLKGER-VTPKADIYSFGITLWQMLTRELPYAGLRQHVL 214
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
58-304 2.06e-29

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 117.86  E-value: 2.06e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  58 EFLETLGKGTYGKVKK------ARESSGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVI 131
Cdd:cd05048   8 RFLEELGEGAFGKVYKgellgpSSEESAISVAIKTLKENASPKTQQ--DFRREAELMSDLQHPNIVCLLGVCTKEQPQCM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDY-ISERPR---------------LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKI 195
Cdd:cd05048  86 LFEYMAHGDLHEFlVRHSPHsdvgvssdddgtassLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDGLTVKI 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 196 ADFGLSNLYHKGKFLQTFCGSPL---YASPE-IVNGKpyVGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNga 270
Cdd:cd05048 166 SDFGLSRDIYSSDYYRVQSKSLLpvrWMPPEaILYGK--FTTESDVWSFGVVLWeIFSYGLQPYYGYSNQEVIEMIRS-- 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 27229182 271 yREP-PKPSDaCGLIRWLLMVN-----PTRRATLEDVASH 304
Cdd:cd05048 242 -RQLlPCPED-CPARVYSLMVEcwheiPSRRPRFKEIHTR 279
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
50-307 2.09e-29

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: 117.44  E-value: 2.09e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  50 KHNLRHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIrkdKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSK 128
Cdd:cd06646   4 RRNPQHDYELIQRVGSGTYGDVYKARNlHTGELAAVKII---KLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL-SNLYHKG 207
Cdd:cd06646  81 LWICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVaAKITATI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 208 KFLQTFCGSPLYASPEIVNGKPYVGPE--VDSWSLGVLLYILVHGTMP-FDGQDHKTLVkqISNGAYREPPKPSDAC--- 281
Cdd:cd06646 161 AKRKSFIGTPYWMAPEVAAVEKNGGYNqlCDIWAVGITAIELAELQPPmFDLHPMRALF--LMSKSNFQPPKLKDKTkws 238
                       250       260       270
                ....*....|....*....|....*....|
gi 27229182 282 ----GLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd06646 239 stfhNFVKISLTKNPKKRPTAERLLTHLFV 268
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
57-245 2.58e-29

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: 117.76  E-value: 2.58e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIrKDKIKDEQDLLHIRrEIEIMSSLN-HPHIIAIHEV-FENSS-KIVIV 132
Cdd:cd07831   1 YKILGKIGEGTFSEVLKAQSrKTGKYYAIKCM-KKHFKSLEQVNNLR-EIQALRRLSpHPNILRLIEVlFDRKTgRLALV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASrGDLYDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANgNIKIADFG-LSNLYHKGKFL 210
Cdd:cd07831  79 FELMD-MNLYELIKGRKRpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFGsCRGIYSKPPYT 156
                       170       180       190
                ....*....|....*....|....*....|....*
gi 27229182 211 QtFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLY 245
Cdd:cd07831 157 E-YISTRWYRAPECLLTDGYYGPKMDIWAVGCVFF 190
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
56-244 2.98e-29

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: 117.76  E-value: 2.98e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRkdkIKDEQDLLHIR--REIEIMSSL---NHPHIIAIHEVFENS--- 126
Cdd:cd07863   1 QYEPVAEIGVGAYGTVYKARDpHSGHFVALKSVR---VQTNEDGLPLStvREVALLKRLeafDHPNIVRLMDVCATSrtd 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 127 --SKIVIVMEYASRgDLYDYISERPR--LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN 202
Cdd:cd07863  78 reTKVTLVFEHVDQ-DLRTYLDKVPPpgLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLAR 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27229182 203 LYHKGKFLQTFCGSPLYASPEIVNGKPYVGPeVDSWSLGVLL 244
Cdd:cd07863 157 IYSCQMALTPVVVTLWYRAPEVLLQSTYATP-VDMWSVGCIF 197
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
58-304 3.13e-29

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: 117.54  E-value: 3.13e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  58 EFLETLGKGTYGKVKKA-RESSGRLVAIKSI---RKDKIKDEqdllhIRREIEIMSSLNHPHIIAIHEVFEN-SSKIVIV 132
Cdd:cd06620   8 ETLKDLGAGNGGSVSKVlHIPTGTIMAKKVIhidAKSSVRKQ-----ILRELQILHECHSPYIVSFYGAFLNeNNNIIIC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCH-QNGIVHRDLKLENILLDANGNIKIADFGLSnlyhkGKFL- 210
Cdd:cd06620  83 MEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYnVHRIIHRDIKPSNILVNSKGQIKLCDFGVS-----GELIn 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 ---QTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF-------DGQDHKT----LVKQISNgayREPPK 276
Cdd:cd06620 158 siaDTFVGTSTYMSPERIQGGKY-SVKSDVWSLGLSIIELALGEFPFagsndddDGYNGPMgildLLQRIVN---EPPPR 233
                       250       260       270
                ....*....|....*....|....*....|....*
gi 27229182 277 -------PSDACGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd06620 234 lpkdrifPKDLRDFVDRCLLKDPRERPSPQLLLDH 268
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
63-297 3.52e-29

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: 117.55  E-value: 3.52e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVI------VMEY 135
Cdd:cd13989   1 LGSGGFGYVTLWKhQDTGEYVAIKKCRQELSPSDKNRERWCLEVQIMKKLNHPNVVSARDVPPELEKLSPndlpllAMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISeRPR----LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL-DANGNI--KIADFGLSNLYHKGK 208
Cdd:cd13989  81 CSGGDLRKVLN-QPEnccgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLqQGGGRViyKLIDLGYAKELDQGS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTFCGSPLYASPEIVNGKPYVGpEVDSWSLGVLLYILVHGTMPFDGQ----DHKTLVKQISN----------GAYR-- 272
Cdd:cd13989 160 LCTSFVGTLQYLAPELFESKKYTC-TVDYWSFGTLAFECITGYRPFLPNwqpvQWHGKVKQKKPehicayedltGEVKfs 238
                       250       260       270
                ....*....|....*....|....*....|....
gi 27229182 273 -EPPKPSDACGLI-----RWL---LMVNPTRRAT 297
Cdd:cd13989 239 sELPSPNHLSSILkeyleSWLqlmLRWDPRQRGG 272
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
57-304 3.74e-29

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: 116.25  E-value: 3.74e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRkDKIKDEQDLLHIRREIEIMSSLN-HPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14050   3 FTILSKLGEGSFGEVFKVRsREDGKLYAVKRSR-SRFRGEKDRKRKLEEVERHEKLGeHPNCVRFIKAWEEKGILYIQTE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YAsRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL-SNLYHKGKFLQTF 213
Cdd:cd14050  82 LC-DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLvVELDKEDIHDAQE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 cGSPLYASPEIVNGKPyvGPEVDSWSLGV-LLYILVHGTMPFDGqdhkTLVKQISNGAYREP---PKPSDACGLIRWLLM 289
Cdd:cd14050 161 -GDPRYMAPELLQGSF--TKAADIFSLGItILELACNLELPSGG----DGWHQLRQGYLPEEftaGLSPELRSIIKLMMD 233
                       250
                ....*....|....*
gi 27229182 290 VNPTRRATLEDVASH 304
Cdd:cd14050 234 PDPERRPTAEDLLAL 248
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
63-313 6.69e-29

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: 118.06  E-value: 6.69e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd05610  12 ISRGAFGKVYLGRKkNNSKLYAVKVVKKADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDV 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-------------------- 201
Cdd:cd05610  92 KSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSkvtlnrelnmmdilttpsma 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 202 ---NLYHK--GKFL-----------------------------QTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYIL 247
Cdd:cd05610 172 kpkNDYSRtpGQVLslisslgfntptpyrtpksvrrgaarvegERILGTPDYLAPELLLGKPH-GPAVDWWALGVCLFEF 250
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27229182 248 VHGTMPFDGQDHKTLVKQISNgayREPPKPS-------DACGLIRWLLMVNPTRRATLEDVASHW------WVNWGYTT 313
Cdd:cd05610 251 LTGIPPFNDETPQQVFQNILN---RDIPWPEgeeelsvNAQNAIEILLTMDPTKRAGLKELKQHPlfhgvdWENLQNQT 326
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
63-307 7.12e-29

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: 115.91  E-value: 7.12e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARES-SGRLVAIKSIR--KDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSK--IVIVMEYAS 137
Cdd:cd06652  10 LGQGAFGRVYLCYDAdTGRELAVKQVQfdPESPETSKEVNALECEIQLLKNLLHERIVQYYGCLRDPQErtLSIFMEYMP 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 138 RGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSnlyhkgKFLQTFC--- 214
Cdd:cd06652  90 GGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGAS------KRLQTIClsg 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 215 -------GSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYRE--PPKPSDACGLIR 285
Cdd:cd06652 164 tgmksvtGTPYWMSPEVISGEGY-GRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPqlPAHVSDHCRDFL 242
                       250       260
                ....*....|....*....|..
gi 27229182 286 WLLMVNPTRRATLEDVASHWWV 307
Cdd:cd06652 243 KRIFVEAKLRPSADELLRHTFV 264
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
57-304 8.23e-29

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: 116.37  E-value: 8.23e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKiKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd07861   2 YTKIEKIGEGTYGVVYKGRnKKTGQIVAMKKIRLES-EEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRgDLYDYISERPRLSERDA---RHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYhkgkflqt 212
Cdd:cd07861  81 LSM-DLKKYLDSLPKGKYMDAelvKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAF-------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 fcGSPL-----------YASPEIVNGKPYVGPEVDSWSLGVLLYILV------HGTMPFDG------------------- 256
Cdd:cd07861 152 --GIPVrvythevvtlwYRAPEVLLGSPRYSTPVDIWSIGTIFAEMAtkkplfHGDSEIDQlfrifrilgtptediwpgv 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 27229182 257 ---QDHKTLVKQISNGAYREPPKPSDACG--LIRWLLMVNPTRRATLEDVASH 304
Cdd:cd07861 230 tslPDYKNTFPKWKKGSLRTAVKNLDEDGldLLEKMLIYDPAKRISAKKALVH 282
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
113-306 1.00e-28

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: 114.75  E-value: 1.00e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 113 HPHIIAIHEVFENSSKIVIVMEyASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN 192
Cdd:cd14022  44 HSNINQITEIILGETKAYVFFE-RSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEER 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 193 IKIADFGLSNLY---HKGKFLQTFCGSPLYASPEIVNGK-PYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISN 268
Cdd:cd14022 123 TRVKLESLEDAYilrGHDDSLSDKHGCPAYVSPEILNTSgSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRR 202
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 27229182 269 GAYREPP--KPSDACgLIRWLLMVNPTRRATLEDVASHWW 306
Cdd:cd14022 203 GQFNIPEtlSPKAKC-LIRSILRREPSERLTSQEILDHPW 241
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
50-307 1.21e-28

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: 115.53  E-value: 1.21e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  50 KHNLRHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIrkdKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSK 128
Cdd:cd06645   6 RRNPQEDFELIQRIGSGTYGDVYKARNvNTGELAAIKVI---KLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-NLYHKG 207
Cdd:cd06645  83 LWICMEFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSaQITATI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 208 KFLQTFCGSPLYASPEI--VNGKPYVGPEVDSWSLGVLLYILVHGTMP-FDGQDHKTLVkqISNGAYREPPKPSDACG-- 282
Cdd:cd06645 163 AKRKSFIGTPYWMAPEVaaVERKGGYNQLCDIWAVGITAIELAELQPPmFDLHPMRALF--LMTKSNFQPPKLKDKMKws 240
                       250       260       270
                ....*....|....*....|....*....|
gi 27229182 283 -----LIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd06645 241 nsfhhFVKMALTKNPKKRPTAEKLLQHPFV 270
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
38-254 2.74e-28

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: 117.02  E-value: 2.74e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  38 LMKKQAVKRHHHKHNLR-HRYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPH 115
Cdd:cd05621  34 LNRYEKIVNKIRELQMKaEDYDVVKVIGRGAFGEVQLVRhKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPW 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 116 IIAIHEVFENSSKIVIVMEYASRGDLYDYISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKI 195
Cdd:cd05621 114 VVQLFCAFQDDKYLYMVMEYMPGGDLVNLMSNYD-VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKL 192
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27229182 196 ADFGLSNLYHKGKFLQ--TFCGSPLYASPEIVN---GKPYVGPEVDSWSLGVLLYILVHGTMPF 254
Cdd:cd05621 193 ADFGTCMKMDETGMVHcdTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLFEMLVGDTPF 256
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
35-279 3.18e-28

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: 114.74  E-value: 3.18e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  35 PKPLMKKQAVKRHHHKHNLRHRYEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNH 113
Cdd:cd08229   4 PVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRATCLlDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNH 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 114 PHIIAIHEVFENSSKIVIVMEYASRGDLYDYI----SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDA 189
Cdd:cd08229  84 PNVIKYYASFIEDNELNIVLELADAGDLSRMIkhfkKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITA 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 190 NGNIKIADFGLSNLY-HKGKFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF--DGQDHKTLVKQI 266
Cdd:cd08229 164 TGVVKLGDLGLGRFFsSKTTAAHSLVGTPYYMSPERIHENGY-NFKSDIWSLGCLLYEMAALQSPFygDKMNLYSLCKKI 242
                       250
                ....*....|...
gi 27229182 267 SNGAYrePPKPSD 279
Cdd:cd08229 243 EQCDY--PPLPSD 253
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
56-241 3.19e-28

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: 115.46  E-value: 3.19e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKAR---ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSS--KIV 130
Cdd:cd07842   1 KYEIEGCIGRGTYGRVYKAKrknGKDGKEYAIKKFKGDKEQYTGISQSACREIALLRELKHENVVSLVEVFLEHAdkSVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 IVMEYASRgDLYDYI-----SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL----DANGNIKIADFGLS 201
Cdd:cd07842  81 LLFDYAEH-DLWQIIkfhrqAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGDLGLA 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 27229182 202 NLYHKGkfLQTFC-GSPL-----YASPEIVNGKPYVGPEVDSWSLG 241
Cdd:cd07842 160 RLFNAP--LKPLAdLDPVvvtiwYRAPELLLGARHYTKAIDIWAIG 203
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
54-265 3.37e-28

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


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 114.62  E-value: 3.37e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFlETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd05607   2 KYFYEF-RVLGKGGFGEVCAVQvKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYI---SERPRLSERdARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKF 209
Cdd:cd05607  81 MSLMNGGDLKYHIynvGERGIEMER-VIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKP 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 27229182 210 LQTFCGSPLYASPEIVNGKPYVGPeVDSWSLGVLLYILVHGTMPFdgQDHKTLVKQ 265
Cdd:cd05607 160 ITQRAGTNGYMAPEILKEESYSYP-VDWFAMGCSIYEMVAGRTPF--RDHKEKVSK 212
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
56-307 4.59e-28

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: 113.40  E-value: 4.59e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14112   4 RFSFGSEIFRGRFSVIVKAVDSTTETDAHCAVKIFEVSDEAS--EAVREFESLRTLQHENVQRLIAAFKPSNFAYLVMEK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 AsRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDA--NGNIKIADFGLSNLYHKgKFLQTF 213
Cdd:cd14112  82 L-QEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSvrSWQVKLVDFGRAQKVSK-LGKVPV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQ-DHKTLVKQ-ISNGAYREPPKP----SDACGLIRWL 287
Cdd:cd14112 160 DGDTDWASPEFHNPETPITVQSDIWGLGVLTFCLLSGFHPFTSEyDDEEETKEnVIFVKCRPNLIFveatQEALRFATWA 239
                       250       260
                ....*....|....*....|
gi 27229182 288 LMVNPTRRATLEDVASHWWV 307
Cdd:cd14112 240 LKKSPTRRMRTDEALEHRWL 259
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
57-272 5.08e-28

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: 113.09  E-value: 5.08e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKdKIKDEQDLLhirREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14110   5 YAFQTEINRGRFSVVRQCEEKrSGQMLAAKIIPY-KPEDKQLVL---REYQVLRRLSHPRIAQLHSAYLSPRHLVLIEEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQT--F 213
Cdd:cd14110  81 CSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTdkK 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27229182 214 CGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYR 272
Cdd:cd14110 161 GDYVETMAPELLEGQG-AGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQ 218
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
63-295 5.59e-28

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: 113.86  E-value: 5.59e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKV--KKARESsGRLVAIKSIRKD-KIKDEQDLLHirrEIEIMSSLNHPHIIAIHEVFENSSKIV-----IVME 134
Cdd:cd14039   1 LGTGGFGNVclYQNQET-GEKIAIKSCRLElSVKNKDRWCH---EIQIMKKLNHPNVVKACDVPEEMNFLVndvplLAME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISeRPR----LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL-DANGNI--KIADFGLSNLYHKG 207
Cdd:cd14039  77 YCSGGDLRKLLN-KPEnccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLqEINGKIvhKIIDLGYAKDLDQG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 208 KFLQTFCGSPLYASPEIVNGKPYVgPEVDSWSLGVLLYILVHGTMPF-------------DGQDHKTLVK-QISNGAYR- 272
Cdd:cd14039 156 SLCTSFVGTLQYLAPELFENKSYT-VTVDYWSFGTMVFECIAGFRPFlhnlqpftwhekiKKKDPKHIFAvEEMNGEVRf 234
                       250       260       270
                ....*....|....*....|....*....|...
gi 27229182 273 --EPPKPSDACGLI-----RWL-LMVN--PTRR 295
Cdd:cd14039 235 stHLPQPNNLCSLIvepmeGWLqLMLNwdPVQR 267
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
63-295 7.94e-28

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


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 113.58  E-value: 7.94e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd05630   8 LGKGGFGEVCACQvRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERPRLSERDARHFF--RQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCGSPLY 219
Cdd:cd05630  88 KFHIYHMGQAGFPEARAVFyaAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGRVGTVGY 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 220 ASPEIVNGKPYV-GPevDSWSLGVLLYILVHGTMPFDGQDHKT-------LVKQISNgAYREPPKPsDACGLIRWLLMVN 291
Cdd:cd05630 168 MAPEVVKNERYTfSP--DWWALGCLLYEMIAGQSPFQQRKKKIkreeverLVKEVPE-EYSEKFSP-QARSLCSMLLCKD 243

                ....
gi 27229182 292 PTRR 295
Cdd:cd05630 244 PAER 247
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
58-307 1.19e-27

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: 113.24  E-value: 1.19e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  58 EFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDllHIRREIEIMS-SLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd06618  18 ENLGEIGSGTCGQVYKMRhKKTGHVMAVKQMRRSGNKEENK--RILMDLDVVLkSHDCPYIVKCYGYFITDSDVFICMEL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRgdLYDYISERPR--LSERDARHFFRQIVSALHYCHQN-GIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQT 212
Cdd:cd06618  96 MST--CLDKLLKRIQgpIPEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILLDESGNVKLCDFGISGRLVDSKAKTR 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPYVGPEV--DSWSLGVLLYILVHGTMPFDG--QDHKTLVKQISNgayrEPPKPS-------DAC 281
Cdd:cd06618 174 SAGCAAYMAPERIDPPDNPKYDIraDVWSLGISLVELATGQFPYRNckTEFEVLTKILNE----EPPSLPpnegfspDFC 249
                       250       260
                ....*....|....*....|....*.
gi 27229182 282 GLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd06618 250 SFVDLCLTKDHRYRPKYRELLQHPFI 275
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
61-304 1.24e-27

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


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 112.53  E-value: 1.24e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARESSGRLVAIKSIR---KDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYAS 137
Cdd:cd06631   7 NVLGKGAYGTVYCGLTSTGQLIAVKQVEldtSDKEKAEKEYEKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFVP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 138 RGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-----NLYH--KGKFL 210
Cdd:cd06631  87 GGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAkrlciNLSSgsQSQLL 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 QTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKP----SDACGLIRW 286
Cdd:cd06631 167 KSMRGTPYWMAPEVINETGH-GRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVPRLPdkfsPEARDFVHA 245
                       250
                ....*....|....*...
gi 27229182 287 LLMVNPTRRATLEDVASH 304
Cdd:cd06631 246 CLTRDQDERPSAEQLLKH 263
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
100-304 1.29e-27

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 112.26  E-value: 1.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  100 HIRREIEIM-SSL--NHPHIIAIHEVFENSSKIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIV 176
Cdd:PHA03390  52 KNFNAIEPMvHQLmkDNPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNII 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  177 HRDLKLENILLD-ANGNIKIADFGLSNlyHKGkflQTFC--GSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMP 253
Cdd:PHA03390 132 HNDIKLENVLYDrAKDRIYLCDYGLCK--IIG---TPSCydGTLDYFSPEKIKGHNY-DVSFDWWAVGVLTYELLTGKHP 205
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 27229182  254 FDGQDHKTL-VKQISNGAYREPPKPSD----ACGLIRWLLMVNPTRRA-TLEDVASH 304
Cdd:PHA03390 206 FKEDEDEELdLESLLKRQQKKLPFIKNvsknANDFVQSMLKYNINYRLtNYNEIIKH 262
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
54-254 1.34e-27

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


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 113.28  E-value: 1.34e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKARESS-GRLVAIKSIRKDKIKDEQDLLHirrEIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd06655  18 KKKYTRYEKIGQGASGTVFTAIDVAtGQEVAIKQINLQKQPKKELIIN---EILVMKELKNPNIVNFLDSFLVGDELFVV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL-SNLYHKGKFLQ 211
Cdd:cd06655  95 MEYLAGGSLTDVVTETC-MDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFcAQITPEQSKRS 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 27229182 212 TFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF 254
Cdd:cd06655 174 TMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPY 215
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
54-278 1.44e-27

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 112.14  E-value: 1.44e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEF--LETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLlhiRREIEIMSSLNHPHIIAIHEVFENSSKIVI 131
Cdd:cd05148   3 RPREEFtlERKLGSGYFGEVWEGLWKNRVRVAIKILKSDDLLKQQDF---QKEVQALKRLRHKHLISLFAVCSVGEPVYI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDYI--SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKF 209
Cdd:cd05148  80 ITELMEKGSLLAFLrsPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIKEDVY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27229182 210 LQTFCGSPL-YASPEIVNGKPYvGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGaYREPPKPS 278
Cdd:cd05148 160 LSSDKKIPYkWTAPEAASHGTF-STKSDVWSFGILLYeMFTYGQVPYPGMNNHEVYDQITAG-YRMPCPAK 228
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
63-304 1.49e-27

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: 113.16  E-value: 1.49e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARES-SGRLVAIK--SIRKDKikdEQDLLHirREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRG 139
Cdd:cd06659  29 IGEGSTGVVCIAREKhSGRQVAVKmmDLRKQQ---RRELLF--NEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGG 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYISErPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFG----LSNLYHKGKFLqtfCG 215
Cdd:cd06659 104 ALTDIVSQ-TRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGfcaqISKDVPKRKSL---VG 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 216 SPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAyrePPKPSDAC-------GLIRWLL 288
Cdd:cd06659 180 TPYWMAPEVISRCPY-GTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSP---PPKLKNSHkaspvlrDFLERML 255
                       250
                ....*....|....*.
gi 27229182 289 MVNPTRRATLEDVASH 304
Cdd:cd06659 256 VRDPQERATAQELLDH 271
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
57-309 1.63e-27

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: 114.56  E-value: 1.63e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd05629   3 FHTVKVIGKGAFGEVRLVQKkDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIMEF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHK-------GK 208
Cdd:cd05629  83 LPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTGFHKqhdsayyQK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQ-----------------------------------------TFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYIL 247
Cdd:cd05629 163 LLQgksnknridnrnsvavdsinltmsskdqiatwkknrrlmaySTVGTPDYIAPEIFLQQGY-GQECDWWSLGAIMFEC 241
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27229182 248 VHGTMPFDGQD-HKTLVKQIsngAYREPPK-PSD------ACGLIRWLLMVNPTR--RATLEDVASHWW---VNW 309
Cdd:cd05629 242 LIGWPPFCSENsHETYRKII---NWRETLYfPDDihlsveAEDLIRRLITNAENRlgRGGAHEIKSHPFfrgVDW 313
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
140-301 1.64e-27

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: 112.50  E-value: 1.64e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN-IKIADFGLS-NLYHKGKFLQTFCGSP 217
Cdd:cd13974 118 NLQHYVIREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTRkITITNFCLGkHLVSEDDLLKDQRGSP 197
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 218 LYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPP--KPSDAC-GLIRWLLMVNPTR 294
Cdd:cd13974 198 AYISPDVLSGKPYLGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEdgRVSENTvCLIRKLLVLNPQK 277

                ....*..
gi 27229182 295 RATLEDV 301
Cdd:cd13974 278 RLTASEV 284
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
63-304 1.93e-27

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 114.15  E-value: 1.93e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   63 LGKGTYGKVKKARE-SSGRLVAIKSIRKDKikDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:PLN00034  82 IGSGAGGTVYKVIHrPTGRLYALKVIYGNH--EDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSL 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  142 YD-YISERPRLSerdarHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLyhkgkFLQTF--CGSPL 218
Cdd:PLN00034 160 EGtHIADEQFLA-----DVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRI-----LAQTMdpCNSSV 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  219 ----YASPEIVN-----GKpYVGPEVDSWSLGVLLYILVHGTMPFD-GQ--DHKTLVKQISngaYREPPKPSDACG---- 282
Cdd:PLN00034 230 gtiaYMSPERINtdlnhGA-YDGYAGDIWSLGVSILEFYLGRFPFGvGRqgDWASLMCAIC---MSQPPEAPATASrefr 305
                        250       260
                 ....*....|....*....|...
gi 27229182  283 -LIRWLLMVNPTRRATLEDVASH 304
Cdd:PLN00034 306 hFISCCLQREPAKRWSAMQLLQH 328
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
58-307 2.15e-27

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


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 112.25  E-value: 2.15e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  58 EFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKikDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYA 136
Cdd:cd06622   4 EVLDELGKGNYGSVYKVLHRpTGVTMAMKEIRLEL--DESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 137 SRGD---LYDYISERPRLSERDARHFFRQIVSALHYC-HQNGIVHRDLKLENILLDANGNIKIADFGLS-NLyhKGKFLQ 211
Cdd:cd06622  82 DAGSldkLYAGGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSgNL--VASLAK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIV-----NGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK-PS----DAC 281
Cdd:cd06622 160 TNIGCQSYMAPERIksggpNQNPTYTVQSDVWSLGLSILEMALGRYPYPPETYANIFAQLSAIVDGDPPTlPSgysdDAQ 239
                       250       260
                ....*....|....*....|....*.
gi 27229182 282 GLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd06622 240 DFVAKCLNKIPNRRPTYAQLLEHPWL 265
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
57-241 2.39e-27

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: 113.11  E-value: 2.39e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARESS-GRLVAIKSIRKDKIKDEQDLLhirrEIEIMSSLN-------HPHIIAIHEVFENSSK 128
Cdd:cd14212   1 YLVLDLLGQGTFGQVVKCQDLKtNKLVAVKVLKNKPAYFRQAML----EIAILTLLNtkydpedKHHIVRLLDHFMHHGH 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IVIVMEYASRgDLYDYISERPR--LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDAN--GNIKIADFGLSnlY 204
Cdd:cd14212  77 LCIVFELLGV-NLYELLKQNQFrgLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLdsPEIKLIDFGSA--C 153
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 27229182 205 HKGKFLQTFCGSPLYASPEIVNGKPYVGPeVDSWSLG 241
Cdd:cd14212 154 FENYTLYTYIQSRFYRSPEVLLGLPYSTA-IDMWSLG 189
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
61-258 3.09e-27

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: 111.27  E-value: 3.09e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKArESSGRLVAIKSIRKDKIKD-EQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRG 139
Cdd:cd14147   9 EVIGIGGFGKVYRG-SWRGELVAVKAARQDPDEDiSVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYISERpRLSERDARHFFRQIVSALHYCHQNGIV---HRDLKLENILLDANG--------NIKIADFGLSNLYHKGK 208
Cdd:cd14147  88 PLSRALAGR-RVPPHVLVNWAVQIARGMHYLHCEALVpviHRDLKSNNILLLQPIenddmehkTLKITDFGLAREWHKTT 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTfCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQD 258
Cdd:cd14147 167 QMSA-AGTYAWMAPEVIKASTF-SKGSDVWSFGVLLWELLTGEVPYRGID 214
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
58-303 3.22e-27

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 110.90  E-value: 3.22e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  58 EFLETLGKGTYGKVKKArESSGRLVAIKSIrKDKIKDEQDLLhirREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYAS 137
Cdd:cd05039   9 KLGELIGKGEFGDVMLG-DYRGQKVAVKCL-KDDSTAAQAFL---AEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 138 RGDLYDYISERPR--LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL---SNLYHK-GKFlq 211
Cdd:cd05039  84 KGSLVDYLRSRGRavITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLakeASSNQDgGKL-- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 tfcgsPL-YASPEIVNGKPYVGpEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGaYR-EPPK--PSDACGLIRW 286
Cdd:cd05039 162 -----PIkWTAPEALREKKFST-KSDVWSFGILLWeIYSFGRVPYPRIPLKDVVPHVEKG-YRmEAPEgcPPEVYKVMKN 234
                       250
                ....*....|....*..
gi 27229182 287 LLMVNPTRRATLEDVAS 303
Cdd:cd05039 235 CWELDPAKRPTFKQLRE 251
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
63-304 4.22e-27

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: 110.98  E-value: 4.22e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIKSI---RKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd06630   8 LGTGAFSSCYQARDvKTGTLMAVKQVsfcRNSSSEQEEVVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN-IKIADFGL-----SNLYHKGKFLQT 212
Cdd:cd06630  88 GSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQrLRIADFGAaarlaSKGTGAGEFQGQ 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDG---QDHKTLVKQISNgAYREPPKPSDACGLIRWLLM 289
Cdd:cd06630 168 LLGTIAFMAPEVLRGEQY-GRSCDVWSVGCVIIEMATAKPPWNAekiSNHLALIFKIAS-ATTPPPIPEHLSPGLRDVTL 245
                       250
                ....*....|....*....
gi 27229182 290 ----VNPTRRATLEDVASH 304
Cdd:cd06630 246 rcleLQPEDRPPARELLKH 264
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
113-307 5.25e-27

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: 109.97  E-value: 5.25e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 113 HPHIIAIHEVFENSSKIVIVMEyASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN 192
Cdd:cd14024  44 HEGVCSVLEVVIGQDRAYAFFS-RHYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELR 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 193 IKIADFGLSN---LYHKGKFLQTFCGSPLYASPEIVN-GKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISN 268
Cdd:cd14024 123 TKLVLVNLEDscpLNGDDDSLTDKHGCPAYVGPEILSsRRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRR 202
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 27229182 269 GAYREPP--KPSDACgLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14024 203 GAFSLPAwlSPGARC-LVSCMLRRSPAERLKASEILLHPWL 242
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
63-279 6.88e-27

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


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 110.50  E-value: 6.88e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd08228  10 IGRGQFSEVYRATcLLDRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELADAGDL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YD---YISERPRL-SERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLY-HKGKFLQTFCGS 216
Cdd:cd08228  90 SQmikYFKKQKRLiPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFsSKTTAAHSLVGT 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27229182 217 PLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF--DGQDHKTLVKQISNGAYrePPKPSD 279
Cdd:cd08228 170 PYYMSPERIHENGY-NFKSDIWSLGCLLYEMAALQSPFygDKMNLFSLCQKIEQCDY--PPLPTE 231
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
57-256 8.77e-27

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: 110.48  E-value: 8.77e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKikDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd07871   7 YVKLDKLGEGTYATVFKGRSKlTENLVALKEIRLEH--EEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASrGDLYDYISERPRL-SERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLyhKGKFLQTFC 214
Cdd:cd07871  85 LD-SDLKQYLDNCGNLmSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARA--KSVPTKTYS 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 27229182 215 GSPL---YASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDG 256
Cdd:cd07871 162 NEVVtlwYRPPDVLLGSTEYSTPIDMWGVGCILYEMATGRPMFPG 206
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
57-257 9.94e-27

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: 111.25  E-value: 9.94e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRK-DKIKDEQdLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd05598   3 FEKIKTIGVGAFGEVSLVRKkDTNALYAMKTLRKkDVLKRNQ-VAHVKAERDILAEADNEWVVKLYYSFQDKENLYFVMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLY---HKGKFLQ 211
Cdd:cd05598  82 YIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwtHDSKYYL 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 27229182 212 --TFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQ 257
Cdd:cd05598 162 ahSLVGTPNYIAPEVLLRTGY-TQLCDWWSVGVILYEMLVGQPPFLAQ 208
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
56-268 1.37e-26

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


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 111.23  E-value: 1.37e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKikdeQDLLHIR---REIEIMSSLNHPHIIAIHEVF------EN 125
Cdd:cd07851  16 RYQNLSPVGSGAYGQVCSAFDTkTGRKVAIKKLSRPF----QSAIHAKrtyRELRLLKHMKHENVIGLLDVFtpasslED 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 126 SSKIVIVMEYASRgDLYDYISERpRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNlyH 205
Cdd:cd07851  92 FQDVYLVTHLMGA-DLNNIVKCQ-KLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLAR--H 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27229182 206 KGKFLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISN 268
Cdd:cd07851 168 TDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMN 230
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
61-307 1.40e-26

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: 110.12  E-value: 1.40e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKikdeqdlLHIR----REIEIMSSLN-HPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14173   8 EVLGEGAYARVQTCINlITNKEYAVKIIEKRP-------GHSRsrvfREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNI---KIADFGL-SNLYHKGKF- 209
Cdd:cd14173  81 KMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVspvKICDFDLgSGIKLNSDCs 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 210 ------LQTFCGSPLYASPEIVNG----KPYVGPEVDSWSLGVLLYILVHGTMPFDGQ---------------DHKTLVK 264
Cdd:cd14173 161 pistpeLLTPCGSAEYMAPEVVEAfneeASIYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdcgwdrgeacpaCQNMLFE 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 27229182 265 QISNGAYREPPK-----PSDACGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd14173 241 SIQEGKYEFPEKdwahiSCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
64-256 1.51e-26

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: 108.51  E-value: 1.51e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  64 GKGTYGKVKKAR-ESSGRLVAIKSirkdkikdeqdLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDLY 142
Cdd:cd14060   2 GGGSFGSVYRAIwVSQDKEVAVKK-----------LLKIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 143 DYISERpRLSERDARHFF---RQIVSALHYCHQNG---IVHRDLKLENILLDANGNIKIADFGLSNlYHKGKFLQTFCGS 216
Cdd:cd14060  71 DYLNSN-ESEEMDMDQIMtwaTDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFGASR-FHSHTTHMSLVGT 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 27229182 217 PLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDG 256
Cdd:cd14060 149 FPWMAPEVIQSLP-VSETCDTYSYGVVLWEMLTREVPFKG 187
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
54-304 2.30e-26

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


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 109.43  E-value: 2.30e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHirrEIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd06656  18 KKKYTRFEKIGQGASGTVYTAIDiATGQEVAIKQMNLQQQPKKELIIN---EILVMRENKNPNIVNYLDSYLVGDELWVV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL-SNLYHKGKFLQ 211
Cdd:cd06656  95 MEYLAGGSLTDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSKRS 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDACGLIRWL---- 287
Cdd:cd06656 174 TMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFlnrc 252
                       250
                ....*....|....*..
gi 27229182 288 LMVNPTRRATLEDVASH 304
Cdd:cd06656 253 LEMDVDRRGSAKELLQH 269
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
63-295 2.53e-26

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: 109.31  E-value: 2.53e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd05631   8 LGKGGFGEVCACQvRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISE--RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCGSPLY 219
Cdd:cd05631  88 KFHIYNmgNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETVRGRVGTVGY 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 220 ASPEIVNGKPYV-GPevDSWSLGVLLYILVHGTMPFdgQDHKTLVK------QISNGAYREPPKPS-DACGLIRWLLMVN 291
Cdd:cd05631 168 MAPEVINNEKYTfSP--DWWGLGCLIYEMIQGQSPF--RKRKERVKreevdrRVKEDQEEYSEKFSeDAKSICRMLLTKN 243

                ....
gi 27229182 292 PTRR 295
Cdd:cd05631 244 PKER 247
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
56-256 2.76e-26

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: 109.05  E-value: 2.76e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKAR-ESSGRLVAIKsirkdKIKDEQDLLHIR----REIEIMSSLNHPHIIAIHEVFENSSKIV 130
Cdd:cd07846   2 KYENLGLVGEGSYGMVMKCRhKETGQIVAIK-----KFLESEDDKMVKkiamREIKMLKQLRHENLVNLIEVFRRKKRWY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 IVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-NLYHKGKF 209
Cdd:cd07846  77 LVFEFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFArTLAAPGEV 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 27229182 210 LQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDG 256
Cdd:cd07846 157 YTDYVATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPG 203
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
63-260 3.21e-26

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


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 109.68  E-value: 3.21e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd05632  10 LGKGGFGEVCACQvRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGDL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISE--RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCGSPLY 219
Cdd:cd05632  90 KFHIYNmgNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGESIRGRVGTVGY 169
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 27229182 220 ASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHK 260
Cdd:cd05632 170 MAPEVLNNQRY-TLSPDYWGLGCLIYEMIEGQSPFRGRKEK 209
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
54-288 3.73e-26

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: 109.04  E-value: 3.73e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHirrEIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd06654  19 KKKYTRFEKIGQGASGTVYTAMDvATGQEVAIRQMNLQQQPKKELIIN---EILVMRENKNPNIVNYLDSYLVGDELWVV 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL-SNLYHKGKFLQ 211
Cdd:cd06654  96 MEYLAGGSLTDVVTETC-MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSKRS 174
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27229182 212 TFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDACGLIRWLL 288
Cdd:cd06654 175 TMVGTPYWMAPEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFL 250
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
56-241 3.76e-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: 109.38  E-value: 3.76e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRrEIEIMSSLNHPHIIAIHEVFENSSK------ 128
Cdd:cd07865  13 KYEKLAKIGQGTFGEVFKARHrKTGQIVALKKVLMENEKEGFPITALR-EIKILQLLKHENVVNLIEICRTKATpynryk 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 --IVIVMEYASRgDLYDYISERP-RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYH 205
Cdd:cd07865  92 gsIYLVFEFCEH-DLAGLLSNKNvKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARAFS 170
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 27229182 206 KGKFLQTFCGSP-----LYASPEIVNGKPYVGPEVDSWSLG 241
Cdd:cd07865 171 LAKNSQPNRYTNrvvtlWYRPPELLLGERDYGPPIDMWGAG 211
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
63-254 5.27e-26

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: 108.51  E-value: 5.27e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKK-ARESSGRLVAIKSIRKD---KIKDEQDLlhirrEIEIMSSLNHPHIIAIHEVFENSSKI------VIV 132
Cdd:cd14038   2 LGTGGFGNVLRwINQETGEQVAIKQCRQElspKNRERWCL-----EIQIMKRLNHPNVVAARDVPEGLQKLapndlpLLA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISERPR---LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNI---KIADFGLSNLYHK 206
Cdd:cd14038  77 MEYCQGGDLRKYLNQFENccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRlihKIIDLGYAKELDQ 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 27229182 207 GKFLQTFCGSPLYASPEIVNGKPYVgPEVDSWSLGVLLYILVHGTMPF 254
Cdd:cd14038 157 GSLCTSFVGTLQYLAPELLEQQKYT-VTVDYWSFGTLAFECITGFRPF 203
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
63-301 5.52e-26

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: 107.54  E-value: 5.52e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSGR-LVAIKSIRKDKIKDEQDLlHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFgMVAIKCLHSSPNCIEERK-ALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 ---YDYISERPRLSERdarhfFR---QIVSALHYCH--QNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGK----- 208
Cdd:cd13978  80 kslLEREIQDVPWSLR-----FRiihEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKLGMKSIsanrr 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 -FLQTFCGSPLYASPEI---VNGKPYVGPEVdsWSLGVLLYILVHGTMPFDGQDHKTLVKQISN----------GAYREP 274
Cdd:cd13978 155 rGTENLGGTPIYMAPEAfddFNKKPTSKSDV--YSFAIVIWAVLTRKEPFENAINPLLIMQIVSkgdrpslddiGRLKQI 232
                       250       260
                ....*....|....*....|....*..
gi 27229182 275 PKPSDACGLIRWLLMVNPTRRATLEDV 301
Cdd:cd13978 233 ENVQELISLMIRCWDGNPDARPTFLEC 259
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
57-304 1.17e-25

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: 106.15  E-value: 1.17e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKAR--------ESSGRLVAIKsirkdKIKDEQDLLHIRREIEIMSSLN-HPHIIAIHEVFENSS 127
Cdd:cd14019   3 YRIIEKIGEGTFSSVYKAEdklhdlydRNKGRLVALK-----HIYPTSSPSRILNELECLERLGgSNNVSGLITAFRNED 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 128 KIVIVMEYASRGDLYDYISErprLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDA-NGNIKIADFGLSNLYHK 206
Cdd:cd14019  78 QVVAVLPYIEHDDFRDFYRK---MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNReTGKGVLVDFGLAQREED 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 207 GKFLQTFC-GSPLYASPEIVNGKPYVGPEVDSWSLGV-LLYILVHGTMPFDGQDHKTLVKQISN--GAYreppkpsDACG 282
Cdd:cd14019 155 RPEQRAPRaGTRGFRAPEVLFKCPHQTTAIDIWSAGViLLSILSGRFPFFFSSDDIDALAEIATifGSD-------EAYD 227
                       250       260
                ....*....|....*....|..
gi 27229182 283 LIRWLLMVNPTRRATLEDVASH 304
Cdd:cd14019 228 LLDKLLELDPSKRITAEEALKH 249
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
59-276 1.23e-25

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


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 106.38  E-value: 1.23e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  59 FLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIkDEQDLLHirrEIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd05059   8 FLKELGSGQFGVVHLGKWRGKIDVAIKMIKEGSM-SEDDFIE---EAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMAN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISERP-RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFcGS- 216
Cdd:cd05059  84 GCLLNYLRERRgKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDDEYTSSV-GTk 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27229182 217 -PL-YASPEIVNGKPYvGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAYREPPK 276
Cdd:cd05059 163 fPVkWSPPEVFMYSKF-SSKSDVWSFGVLMWeVFSEGKMPYERFSNSEVVEHISQGYRLYRPH 224
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
57-256 1.27e-25

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: 107.40  E-value: 1.27e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKikDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd07873   4 YIKLDKLGEGTYATVYKGRSKlTDNLVALKEIRLEH--EEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRgDLYDYISERPRL-SERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLyhKGKFLQTFC 214
Cdd:cd07873  82 LDK-DLKQYLDDCGNSiNMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARA--KSIPTKTYS 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 27229182 215 GSPL---YASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDG 256
Cdd:cd07873 159 NEVVtlwYRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPG 203
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
52-306 1.35e-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: 108.04  E-value: 1.35e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  52 NLRHRYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRK-DKIKDEQdllhiRREIEIMSSLNH------PHIIAIHEVF 123
Cdd:cd14134   9 LLTNRYKILRLLGEGTFGKVLECWdRKRKRYVAVKIIRNvEKYREAA-----KIEIDVLETLAEkdpngkSHCVQLRDWF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 124 ENSSKIVIVMEY--ASrgdLYDYISE---RPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLD---------- 188
Cdd:cd14134  84 DYRGHMCIVFELlgPS---LYDFLKKnnyGP-FPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVdsdyvkvynp 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 189 ---------ANGNIKIADFG---LSNLYHkgkflqtfcgsplyasPEIVNGKPYVGPEV----------DSWSLGVLLYI 246
Cdd:cd14134 160 kkkrqirvpKSTDIKLIDFGsatFDDEYH----------------SSIVSTRHYRAPEVilglgwsypcDVWSIGCILVE 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 247 LVHGTMPFDGQDH----------------------KTLVKQI--SNGAYREPPKPSDA---------------------- 280
Cdd:cd14134 224 LYTGELLFQTHDNlehlammerilgplpkrmirraKKGAKYFyfYHGRLDWPEGSSSGrsikrvckplkrlmllvdpehr 303
                       330       340
                ....*....|....*....|....*...
gi 27229182 281 --CGLIRWLLMVNPTRRATLEDVASHWW 306
Cdd:cd14134 304 llFDLIRKMLEYDPSKRITAKEALKHPF 331
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
60-254 1.70e-25

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


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 106.68  E-value: 1.70e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  60 LETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd06642   9 LERIGKGSFGEVYKGIDNrTKEVVAIKIIDLEEAEDEIE--DIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQ-TFCGSP 217
Cdd:cd06642  87 GSALDLLKPGP-LEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRnTFVGTP 165
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 27229182 218 LYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF 254
Cdd:cd06642 166 FWMAPEVIKQSAY-DFKADIWSLGITAIELAKGEPPN 201
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
63-309 2.01e-25

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: 106.29  E-value: 2.01e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd05605   8 LGKGGFGEVCACQvRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISE--RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCGSPLY 219
Cdd:cd05605  88 KFHIYNmgNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETIRGRVGTVGY 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 220 ASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPK-----PSDACGLIRWLLMVNPT- 293
Cdd:cd05605 168 MAPEVVKNERY-TFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDRRVKEDQEEysekfSEEAKSICSQLLQKDPKt 246
                       250       260
                ....*....|....*....|...
gi 27229182 294 ----RRATLEDVASHWW---VNW 309
Cdd:cd05605 247 rlgcRGEGAEDVKSHPFfksINF 269
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
63-277 2.02e-25

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: 105.60  E-value: 2.02e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSgRLVAIKSIRKDKIKDEqdllhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDLY 142
Cdd:cd14058   1 VGRGSFGVVCKARWRN-QIVAVKIIESESEKKA-----FEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 143 DYI---SERPRLSERDARHFFRQIVSALHYCHQ---NGIVHRDLKLENILLDANG-NIKIADFGLSNLYHKGKFLQTfcG 215
Cdd:cd14058  75 NVLhgkEPKPIYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGtVLKICDFGTACDISTHMTNNK--G 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27229182 216 SPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFD--GQDHKTLVKQISNGAyREP-----PKP 277
Cdd:cd14058 153 SAAWMAPEVFEGSKY-SEKCDVFSWGIILWEVITRRKPFDhiGGPAFRIMWAVHNGE-RPPlikncPKP 219
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
53-254 2.36e-25

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: 105.95  E-value: 2.36e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLET-----LGKGTYGKVKKARE-SSGRLVAIKSIrkdKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENS 126
Cdd:cd06624   1 LEYEYEYDESgervvLGKGTFGVVYAARDlSTQVRIAIKEI---PERDSREVQPLHEEIALHSRLSHKNIVQYLGSVSED 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 127 SKIVIVMEYASRGDLYDYISER--PRLSERDA-RHFFRQIVSALHYCHQNGIVHRDLKLENILLDA-NGNIKIADFGLSN 202
Cdd:cd06624  78 GFFKIFMEQVPGGSLSALLRSKwgPLKDNENTiGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSK 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 27229182 203 -LYHKGKFLQTFCGSPLYASPEIVN-GKPYVGPEVDSWSLGVLLYILVHGTMPF 254
Cdd:cd06624 158 rLAGINPCTETFTGTLQYMAPEVIDkGQRGYGPPADIWSLGCTIIEMATGKPPF 211
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
63-269 2.84e-25

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


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 105.12  E-value: 2.84e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKA--RESSGRL--VAIKSIRKDKIK-DEQDLLhirREIEIMSSLNHPHIIAIHEVFEnSSKIVIVMEYAS 137
Cdd:cd05060   3 LGHGNFGSVRKGvyLMKSGKEveVAVKTLKQEHEKaGKKEFL---REASVMAQLDHPCIVRLIGVCK-GEPLMLVMELAP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 138 RGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS------NLYHK----G 207
Cdd:cd05060  79 LGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSralgagSDYYRattaG 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27229182 208 KFlqtfcgsPL--YAsPEIVN-GKpyVGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNG 269
Cdd:cd05060 159 RW-------PLkwYA-PECINyGK--FSSKSDVWSYGVTLWeAFSYGAKPYGEMKGPEVIAMLESG 214
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
53-303 2.96e-25

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: 106.68  E-value: 2.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDK----IKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFE-NS 126
Cdd:cd14041   4 LNDRYLLLHLLGRGGFSEVYKAFDlTEQRYVAVKIHQLNKnwrdEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 127 SKIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQ--NGIVHRDLKLENILL---DANGNIKIADFGLS 201
Cdd:cd14041  84 DSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLvngTACGEIKITDFGLS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 202 NLYHKGKF--------LQTFCGSPLYASPE-IVNGK--PYVGPEVDSWSLGVLLYILVHGTMPF-DGQDHKTLVKQ---I 266
Cdd:cd14041 164 KIMDDDSYnsvdgmelTSQGAGTYWYLPPEcFVVGKepPKISNKVDVWSVGVIFYQCLYGRKPFgHNQSQQDILQEntiL 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 27229182 267 SNGAYREPPKP---SDACGLIRWLLMVNPTRRATLEDVAS 303
Cdd:cd14041 244 KATEVQFPPKPvvtPEAKAFIRRCLAYRKEDRIDVQQLAC 283
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
63-258 2.98e-25

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: 105.50  E-value: 2.98e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKArESSGRLVAIKSIRKDKikdEQDLL----HIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd14146   2 IGVGGFGKVYRA-TWKGQEVAVKAARQDP---DEDIKataeSVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYIS-----ERPRLSERDARHFF----RQIVSALHYCHQNGIV---HRDLKLENILL--------DANGNIKIADF 198
Cdd:cd14146  78 GTLNRALAaanaaPGPRRARRIPPHILvnwaVQIARGMLYLHEEAVVpilHRDLKSSNILLlekiehddICNKTLKITDF 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 199 GLSNLYHKGKFLQTfCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQD 258
Cdd:cd14146 158 GLAREWHRTTKMSA-AGTYAWMAPEVIKSSLF-SKGSDIWSYGVLLWELLTGEVPYRGID 215
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
63-299 3.26e-25

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 105.06  E-value: 3.26e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSGRLVAIKSIRKDKIkDEQDLLhirREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDLY 142
Cdd:cd05034   3 LGAGQFGEVWMGVWNGTTKVAVKTLKPGTM-SPEAFL---QEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 143 DYISERP--RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKG--------KFlqt 212
Cdd:cd05034  79 DYLRTGEgrALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDDeytaregaKF--- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 fcgsPL-YASPEIVN-GKPYVGPEVdsWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGaYREpPKPSDaCGLIRWLLM 289
Cdd:cd05034 156 ----PIkWTAPEAALyGRFTIKSDV--WSFGILLYeIVTYGRVPYPGMTNREVLEQVERG-YRM-PKPPG-CPDELYDIM 226
                       250
                ....*....|....*
gi 27229182 290 V-----NPTRRATLE 299
Cdd:cd05034 227 LqcwkkEPEERPTFE 241
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
54-297 3.88e-25

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: 105.67  E-value: 3.88e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLET--LGKGTYGKVKKARES-SGRLVAIKSIRKDKIKdEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIV 130
Cdd:cd14049   3 RYLNEFEEIarLGKGGYGKVYKVRNKlDGQYYAIKKILIKKVT-KRDCMKVLREVKVLAGLQHPNIVGYHTAWMEHVQLM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 --IVMEYASRgDLYDYISER---PRLSE--------RDARH---FFRQIVSALHYCHQNGIVHRDLKLENILLDANG-NI 193
Cdd:cd14049  82 lyIQMQLCEL-SLWDWIVERnkrPCEEEfksapytpVDVDVttkILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDiHV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 194 KIADFGL------------------SNLYHKGKFlqtfcGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVhgtMPFD 255
Cdd:cd14049 161 RIGDFGLacpdilqdgndsttmsrlNGLTHTSGV-----GTCLYAAPEQLEGSHY-DFKSDMYSIGVILLELF---QPFG 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 27229182 256 GQDHKT-LVKQISNGAYreppkPSDACG-------LIRWLLMVNPTRRAT 297
Cdd:cd14049 232 TEMERAeVLTQLRNGQI-----PKSLCKrwpvqakYIKLLTSTEPSERPS 276
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
54-303 4.28e-25

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: 105.20  E-value: 4.28e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKA----RESSGRLVAIKSIRKDKIKDEQDLlhIRREIEIMSSLNHPHIIAIHEVFENSSkI 129
Cdd:cd05056   5 REDITLGRCIGEGQFGDVYQGvymsPENEKIAVAVKTCKNCTSPSVREK--FLQEAYIMRQFDHPHIVKLIGVITENP-V 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 130 VIVMEYASRGDLYDYIS-ERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGK 208
Cdd:cd05056  82 WIVMELAPLGELRSYLQvNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDES 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTFCGS-PL-YASPEIVNGKPYVGPEvDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGayREPPKPsDACGLIR 285
Cdd:cd05056 162 YYKASKGKlPIkWMAPESINFRRFTSAS-DVWMFGVCMWeILMLGVKPFQGVKNNDVIGRIENG--ERLPMP-PNCPPTL 237
                       250       260
                ....*....|....*....|...
gi 27229182 286 WLLM-----VNPTRRATLEDVAS 303
Cdd:cd05056 238 YSLMtkcwaYDPSKRPRFTELKA 260
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
61-258 4.54e-25

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: 105.12  E-value: 4.54e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKAReSSGRLVAIKSIRKDKIKD-EQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRG 139
Cdd:cd14145  12 EIIGIGGFGKVYRAI-WIGDEVAVKAARHDPDEDiSQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYISERpRLSERDARHFFRQIVSALHYCHQNGIV---HRDLKLENILL--------DANGNIKIADFGLSNLYHKGK 208
Cdd:cd14145  91 PLNRVLSGK-RIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILIlekvengdLSNKILKITDFGLAREWHRTT 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTfCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQD 258
Cdd:cd14145 170 KMSA-AGTYAWMAPEVIRSSMF-SKGSDVWSYGVLLWELLTGEVPFRGID 217
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
56-256 4.71e-25

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 105.67  E-value: 4.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   56 RYEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKiKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:PLN00009   3 QYEKVEKIGEGTYGVVYKARDRvTNETIALKKIRLEQ-EDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  135 YASRgDLYDYISERPRLSE--RDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN-IKIADFGLSNLYhkGKFLQ 211
Cdd:PLN00009  82 YLDL-DLKKHMDSSPDFAKnpRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNaLKLADFGLARAF--GIPVR 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 27229182  212 TFCGSPL---YASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDG 256
Cdd:PLN00009 159 TFTHEVVtlwYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPG 206
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
57-276 4.79e-25

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: 107.07  E-value: 4.79e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd05627   4 FESLKVIGRGAFGEVRLVqKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIMEF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL-------------SN 202
Cdd:cd05627  84 LPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLctglkkahrtefyRN 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 203 LYH-----------------------KGKFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDH 259
Cdd:cd05627 164 LTHnppsdfsfqnmnskrkaetwkknRRQLAYSTVGTPDYIAPEVFMQTGY-NKLCDWWSLGVIMYEMLIGYPPFCSETP 242
                       250       260
                ....*....|....*....|.
gi 27229182 260 KTLVKQISNgaYRE----PPK 276
Cdd:cd05627 243 QETYRKVMN--WKEtlvfPPE 261
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
60-253 6.58e-25

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


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 104.77  E-value: 6.58e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  60 LETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd06641   9 LEKIGKGSFGEVFKGIDnRTQKVVAIKIIDLEEAEDEIE--DIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQT-FCGSP 217
Cdd:cd06641  87 GSALDLLEPGP-LDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN*FVGTP 165
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 27229182 218 LYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMP 253
Cdd:cd06641 166 FWMAPEVIKQSAY-DSKADIWSLGITAIELARGEPP 200
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
63-304 6.84e-25

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: 106.30  E-value: 6.84e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARES-SGRLVAIKSIRK--DKIKDEQDLLhirREIEIMSSLNHPHIIAIHEVF-----ENSSKIVIVME 134
Cdd:cd07858  13 IGRGAYGIVCSAKNSeTNEKVAIKKIANafDNRIDAKRTL---REIKLLRHLDHENVIAIKDIMppphrEAFNDVYIVYE 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRgDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYH-KGKFLQTF 213
Cdd:cd07858  90 LMDT-DLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTSeKGDFMTEY 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CGSPLYASPE-IVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISN--GAYRE----------------- 273
Cdd:cd07858 169 VVTRWYRAPElLLNCSEY-TTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITEllGSPSEedlgfirnekarryirs 247
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 27229182 274 -------------PPKPSDACGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd07858 248 lpytprqsfarlfPHANPLAIDLLEKMLVFDPSKRITVEEALAH 291
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
57-256 7.58e-25

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: 104.77  E-value: 7.58e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKikDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd07844   2 YKKLDKLGEGSYATVYKGRSKlTGQLVALKEIRLEH--EEGAPFTAIREASLLKDLKHANIVTLHDIIHTKKTLTLVFEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRgDLYDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLyhKGKFLQTFC 214
Cdd:cd07844  80 LDT-DLKQYMDDCGGgLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARA--KSVPSKTYS 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 27229182 215 GSPL---YASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDG 256
Cdd:cd07844 157 NEVVtlwYRPPDVLLGSTEYSTSLDMWGVGCIFYEMATGRPLFPG 201
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
63-304 8.65e-25

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: 104.72  E-value: 8.65e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKsirKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd06657  28 IGEGSTGIVCIATvKSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISErPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL-SNLYHKGKFLQTFCGSPLYA 220
Cdd:cd06657 105 TDIVTH-TRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRKSLVGTPYWM 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 221 SPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAyrePPKPSDAC-------GLIRWLLMVNPT 293
Cdd:cd06657 184 APELISRLPY-GPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNL---PPKLKNLHkvspslkGFLDRLLVRDPA 259
                       250
                ....*....|.
gi 27229182 294 RRATLEDVASH 304
Cdd:cd06657 260 QRATAAELLKH 270
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
54-300 1.02e-24

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: 104.03  E-value: 1.02e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIkDEQDLLhirREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd05068   7 RKSLKLLRKLGSGQFGEVWEGLWNNTTPVAVKTLKPGTM-DPEDFL---REAQIMKKLRHPKLIQLYAVCTLEEPIYIIT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYISER------PRLSERDArhffrQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKG 207
Cdd:cd05068  83 ELMKHGSLLEYLQGKgrslqlPQLIDMAA-----QVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKVE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 208 KFLQTFCGSPL---YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGaYREPPKPSdaCGL 283
Cdd:cd05068 158 DEYEAREGAKFpikWTAPEAANYNRFS-IKSDVWSFGILLTeIVTYGRIPYPGMTNAEVLQQVERG-YRMPCPPN--CPP 233
                       250       260
                ....*....|....*....|..
gi 27229182 284 IRWLLMV-----NPTRRATLED 300
Cdd:cd05068 234 QLYDIMLecwkaDPMERPTFET 255
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
56-267 1.17e-24

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: 105.35  E-value: 1.17e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKdKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSK-IVIVM 133
Cdd:cd07856  11 RYSDLQPVGMGAFGLVCSARDQlTGQNVAVKKIMK-PFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISPLEdIYFVT 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRgDLYDYISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLyhKGKFLQTF 213
Cdd:cd07856  90 ELLGT-DLHRLLTSRP-LEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARI--QDPQMTGY 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 27229182 214 CGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHktlVKQIS 267
Cdd:cd07856 166 VSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDH---VNQFS 216
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
54-247 2.08e-24

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: 103.56  E-value: 2.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHrYEFLETLGKGTYGKVKKAR-----ESSGRLVAIKSIRKDKikdEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSK 128
Cdd:cd14205   4 RH-LKFLQQLGKGNFGSVEMCRydplqDNTGEVVAVKKLQHST---EEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 --IVIVMEYASRGDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYH 205
Cdd:cd14205  80 rnLRLIMEYLPYGSLRDYLQKhKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLP 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 27229182 206 KGKFLQTF---CGSPL--YASPEIVNGKPYVGPEVdsWSLGVLLYIL 247
Cdd:cd14205 160 QDKEYYKVkepGESPIfwYAPESLTESKFSVASDV--WSFGVVLYEL 204
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
59-276 2.26e-24

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 102.72  E-value: 2.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  59 FLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQdllhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd05112   8 FVQEIGSGQFGLVHLGYWLNKDKVAIKTIREGAMSEED----FIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEH 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYI-SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTfCGSP 217
Cdd:cd05112  84 GCLSDYLrTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTSS-TGTK 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27229182 218 L---YASPEIVNGKPYvGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAYREPPK 276
Cdd:cd05112 163 FpvkWSSPEVFSFSRY-SSKSDVWSFGVLMWeVFSEGKIPYENRSNSEVVEDINAGFRLYKPR 224
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
63-304 2.48e-24

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: 103.58  E-value: 2.48e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARES-SGRLVAIKsirKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd06658  30 IGEGSTGIVCIATEKhTGKQVAVK---KMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGAL 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISErPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL-SNLYHKGKFLQTFCGSPLYA 220
Cdd:cd06658 107 TDIVTH-TRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFcAQVSKEVPKRKSLVGTPYWM 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 221 SPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAyrePPKPSDAC-------GLIRWLLMVNPT 293
Cdd:cd06658 186 APEVISRLPY-GTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNL---PPRVKDSHkvssvlrGFLDLMLVREPS 261
                       250
                ....*....|.
gi 27229182 294 RRATLEDVASH 304
Cdd:cd06658 262 QRATAQELLQH 272
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
60-253 2.51e-24

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


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 103.21  E-value: 2.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  60 LETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd06640   9 LERIGKGSFGEVFKGIDNrTQQVVAIKIIDLEEAEDEIE--DIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKF-LQTFCGSP 217
Cdd:cd06640  87 GSALDLLRAGP-FDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIkRNTFVGTP 165
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 27229182 218 LYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMP 253
Cdd:cd06640 166 FWMAPEVIQQSAY-DSKADIWSLGITAIELAKGEPP 200
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
56-244 2.59e-24

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


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 104.37  E-value: 2.59e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARES-SGRLVAIKSIRK--DKIKDEQDLLhirREIEIMSSLNHPHIIAIHEVFENSSK---- 128
Cdd:cd07855   6 RYEPIETIGSGAYGVVCSAIDTkSGQKVAIKKIPNafDVVTTAKRTL---RELKILRHFKHDNIIAIRDILRPKVPyadf 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 --IVIVMEYAsRGDLYDYI-SERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLyh 205
Cdd:cd07855  83 kdVYVVLDLM-ESDLHHIIhSDQP-LTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARG-- 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 27229182 206 kgkflqtFCGSPL---YASPEIVNGKPYVGPE-----------VDSWSLGVLL 244
Cdd:cd07855 159 -------LCTSPEehkYFMTEYVATRWYRAPElmlslpeytqaIDMWSVGCIF 204
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
55-244 2.64e-24

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: 103.57  E-value: 2.64e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  55 HRYEFLETLGKGTYGKVKKARE--SSGRLVAIKSIRKdKIKDEQDLLHIRREIEIM---SSLNHPHIIAIHEV-----FE 124
Cdd:cd07862   1 QQYECVAEIGEGAYGKVFKARDlkNGGRFVALKRVRV-QTGEEGMPLSTIREVAVLrhlETFEHPNVVRLFDVctvsrTD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 125 NSSKIVIVMEYASRgDLYDYISERPR--LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN 202
Cdd:cd07862  80 RETKLTLVFEHVDQ-DLTTYLDKVPEpgVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLAR 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27229182 203 LYHKGKFLQTFCGSPLYASPEIVNGKPYVGPeVDSWSLGVLL 244
Cdd:cd07862 159 IYSFQMALTSVVVTLWYRAPEVLLQSSYATP-VDLWSVGCIF 199
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
56-308 3.02e-24

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: 104.02  E-value: 3.02e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARESS---GRLVAIKSIRK---DKIKDEQDLlhirREIEIMSSL-NHPHIIAIHE---VFEN 125
Cdd:cd07857   1 RYELIKELGQGAYGIVCSARNAEtseEETVAIKKITNvfsKKILAKRAL----RELKLLRHFrGHKNITCLYDmdiVFPG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 126 SSKIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYH 205
Cdd:cd07857  77 NFNELYLYEELMEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 206 KGK-----FLQTFCGSPLYASPEI-VNGKPYVgPEVDSWSLGVLLYILVHGTMPFDGQDH----------------KTLV 263
Cdd:cd07857 157 ENPgenagFMTEYVATRWYRAPEImLSFQSYT-KAIDVWSVGCILAELLGRKPVFKGKDYvdqlnqilqvlgtpdeETLS 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27229182 264 KQISNGAY-------REPPKP---------SDACGLIRWLLMVNPTRRATLEDVASHWWVN 308
Cdd:cd07857 236 RIGSPKAQnyirslpNIPKKPfesifpnanPLALDLLEKLLAFDPTKRISVEEALEHPYLA 296
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
57-276 3.55e-24

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: 102.83  E-value: 3.55e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEF-------LETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLhiRREIE-IMSSLNHPHIIAIHEVFENSS 127
Cdd:cd06616   1 YEFtaedlkdLGEIGRGAFGTVNKMLhKPSGTIMAVKRIRSTVDEKEQKRL--LMDLDvVMRSSDCPYIVKFYGALFREG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 128 KIVIVMEY--ASRGDLYDYI--SERPRLSERDARHFFRQIVSALHYCHQN-GIVHRDLKLENILLDANGNIKIADFGLSn 202
Cdd:cd06616  79 DCWICMELmdISLDKFYKYVyeVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGIS- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 203 lyhkGKFLQTFcgsplyASPEIVNGKPYVGPE--------------VDSWSLGVLLYILVHGTMPFDGQDhkTLVKQISN 268
Cdd:cd06616 158 ----GQLVDSI------AKTRDAGCRPYMAPEridpsasrdgydvrSDVWSLGITLYEVATGKFPYPKWN--SVFDQLTQ 225

                ....*...
gi 27229182 269 GAYREPPK 276
Cdd:cd06616 226 VVKGDPPI 233
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
63-304 3.97e-24

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: 102.47  E-value: 3.97e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDE--QDLLHIRREIEIMSSLNHPHIIAIHEVFENSSK--IVIVMEYAS 137
Cdd:cd06651  15 LGQGAFGRVYLCYDvDTGRELAAKQVQFDPESPEtsKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIFMEYMP 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 138 RGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFG----LSNLYHKGKFLQTF 213
Cdd:cd06651  95 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskrLQTICMSGTGIRSV 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAyREPPKPSDACGLIRWLL---MV 290
Cdd:cd06651 175 TGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQP-TNPQLPSHISEHARDFLgciFV 252
                       250
                ....*....|....
gi 27229182 291 NPTRRATLEDVASH 304
Cdd:cd06651 253 EARHRPSAEELLRH 266
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
57-304 5.04e-24

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: 102.26  E-value: 5.04e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARESSGRL-VAIKSIR---KDKIKDEqdllhIRREIEIMSSLNHPHIIAIHEVF--------- 123
Cdd:cd14048   8 FEPIQCLGRGGFGVVFEAKNKVDDCnYAVKRIRlpnNELAREK-----VLREVRALAKLDHPGIVRYFNAWlerppegwq 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 124 --ENSSKIVIVMEYASRGDLYDYISERPRLSERD---ARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADF 198
Cdd:cd14048  83 ekMDEVYLYIQMQLCRKENLKDWMNRRCTMESRElfvCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 199 GLSNLYHKGKFLQTF-------------CGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHgtmPFDGQDHKTL-VK 264
Cdd:cd14048 163 GLVTAMDQGEPEQTVltpmpayakhtgqVGTRLYMSPEQIHGNQY-SEKVDIFALGLILFELIY---SFSTQMERIRtLT 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 27229182 265 QISNGAY-----REPPKPSDacgLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd14048 239 DVRKLKFpalftNKYPEERD---MVQQMLSPSPSERPEAHEVIEH 280
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
57-275 5.12e-24

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: 102.38  E-value: 5.12e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKK-ARESSGRLVAIKSIrkDKIKDEQDllHIRREIEIMSSL-NHPHIIAIHEVFENSSKIV---- 130
Cdd:cd06639  24 WDIIETIGKGTYGKVYKvTNKKDGSLAAVKIL--DPISDVDE--EIEAEYNILRSLpNHPNVVKFYGMFYKADQYVggql 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 -IVMEYASRGDLYDYISE----RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYH 205
Cdd:cd06639 100 wLVLELCNGGSVTELVKGllkcGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 179
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27229182 206 KGKFLQ-TFCGSPLYASPEIVNGKPYVGPEVDS----WSLGVLLYILVHGTMP-FDGQDHKTLVKqisngAYREPP 275
Cdd:cd06639 180 SARLRRnTSVGTPFWMAPEVIACEQQYDYSYDArcdvWSLGITAIELADGDPPlFDMHPVKALFK-----IPRNPP 250
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
60-254 6.23e-24

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: 104.32  E-value: 6.23e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  60 LETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd05626   6 IKTLGIGAFGEVCLACKvDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIPG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL---------SNLYHKGKF 209
Cdd:cd05626  86 GDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLctgfrwthnSKYYQKGSH 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 210 LQ---------------------------------------TFCGSPLYASPEIVNGKPYVgPEVDSWSLGVLLYILVHG 250
Cdd:cd05626 166 IRqdsmepsdlwddvsncrcgdrlktleqratkqhqrclahSLVGTPNYIAPEVLLRKGYT-QLCDWWSVGVILFEMLVG 244

                ....
gi 27229182 251 TMPF 254
Cdd:cd05626 245 QPPF 248
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
57-256 6.30e-24

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: 102.76  E-value: 6.30e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKikDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd07872   8 YIKLEKLGEGTYATVFKGRSKlTENLVALKEIRLEH--EEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRgDLYDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLyhKGKFLQTFC 214
Cdd:cd07872  86 LDK-DLKQYMDDCGNiMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARA--KSVPTKTYS 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 27229182 215 GSPL---YASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDG 256
Cdd:cd07872 163 NEVVtlwYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPG 207
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
56-266 6.55e-24

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: 103.32  E-value: 6.55e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARES-SGRLVAIKSIRkDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSK-----I 129
Cdd:cd07859   1 RYKIQEVIGKGSYGVVCSAIDThTGEKVAIKKIN-DVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLPPSRrefkdI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 130 VIVMEYASrGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS----NLYH 205
Cdd:cd07859  80 YVVFELME-SDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLArvafNDTP 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27229182 206 KGKFLQTFCGSPLYASPEIVNG--KPYVgPEVDSWSLGVLLYILVHGTMPFDGqdhKTLVKQI 266
Cdd:cd07859 159 TAIFWTDYVATRWYRAPELCGSffSKYT-PAIDIWSIGCIFAEVLTGKPLFPG---KNVVHQL 217
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
57-276 8.94e-24

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: 103.58  E-value: 8.94e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd05628   3 FESLKVIGRGAFGEVRLVqKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL-------------SN 202
Cdd:cd05628  83 LPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLctglkkahrtefyRN 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 203 LYHKGKFLQTF-----------------------CGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDH 259
Cdd:cd05628 163 LNHSLPSDFTFqnmnskrkaetwkrnrrqlafstVGTPDYIAPEVFMQTGY-NKLCDWWSLGVIMYEMLIGYPPFCSETP 241
                       250       260
                ....*....|....*....|.
gi 27229182 260 KTLVKQISNgaYRE----PPK 276
Cdd:cd05628 242 QETYKKVMN--WKEtlifPPE 260
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
53-249 9.56e-24

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: 101.03  E-value: 9.56e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEqdllhirREIEIMSSLNHPHIIAIHEVF-------E 124
Cdd:cd14047   4 FRQDFKEIELIGSGGFGQVFKAKhRIDGKTYAIKRVKLNNEKAE-------REVKALAKLDHPNIVRYNGCWdgfdydpE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 125 NSSK---------IVIVMEYASRGDLYDYISER--PRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNI 193
Cdd:cd14047  77 TSSSnssrsktkcLFIQMEFCEKGTLESWIEKRngEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKV 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27229182 194 KIADFGL------SNLYHKGKflqtfcGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVH 249
Cdd:cd14047 157 KIGDFGLvtslknDGKRTKSK------GTLSYMSPEQISSQDY-GKEVDIYALGLILFELLH 211
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
63-258 1.04e-23

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: 100.93  E-value: 1.04e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAReSSGRLVAIKSIRKDKIKD-EQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd14061   2 IGVGGFGKVYRGI-WRGEEVAVKAARQDPDEDiSVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERpRLSERDARHFFRQIVSALHYCHQNG---IVHRDLKLENILLD--------ANGNIKIADFGLSNLYHKGKFL 210
Cdd:cd14061  81 NRVLAGR-KIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILeaienedlENKTLKITDFGLAREWHKTTRM 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 27229182 211 QTfCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQD 258
Cdd:cd14061 160 SA-AGTYAWMAPEVIKSSTF-SKASDVWSYGVLLWELLTGEVPYKGID 205
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
49-267 1.32e-23

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: 102.47  E-value: 1.32e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  49 HKHnLRHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLhirrEIEIMSSL------NHPHIIAIHE 121
Cdd:cd14225  38 HDH-IAYRYEILEVIGKGSFGQVVKALDhKTNEHVAIKIIRNKKRFHHQALV----EVKILDALrrkdrdNSHNVIHMKE 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 122 VFENSSKIVIVMEYASRgDLYDYISER--PRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANG--NIKIAD 197
Cdd:cd14225 113 YFYFRNHLCITFELLGM-NLYELIKKNnfQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGqsSIKVID 191
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 198 FGLSNLYHKGKFlqTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHktlVKQIS 267
Cdd:cd14225 192 FGSSCYEHQRVY--TYIQSRFYRSPEVILGLPY-SMAIDMWSLGCILAELYTGYPLFPGENE---VEQLA 255
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
59-301 1.67e-23

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 100.32  E-value: 1.67e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  59 FLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKdEQDLLHirrEIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd05114   8 FMKELGSGLFGVVRLGKWRAQYKVAIKAIREGAMS-EEDFIE---EAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMEN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISERPRLSERDARHFFRQ-IVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTfCGSP 217
Cdd:cd05114  84 GCLLNYLRQRRGKLSRDMLLSMCQdVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTSS-SGAK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 218 L---YASPEIVNGKPYvGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNG--AYReppkPSDACGLIRWLLMV- 290
Cdd:cd05114 163 FpvkWSPPEVFNYSKF-SSKSDVWSFGVLMWeVFTEGKMPFESKSNYEVVEMVSRGhrLYR----PKLASKSVYEVMYSc 237
                       250
                ....*....|....
gi 27229182 291 ---NPTRRATLEDV 301
Cdd:cd05114 238 wheKPEGRPTFADL 251
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
63-255 2.08e-23

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: 100.42  E-value: 2.08e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSGRLVAIKSIR-KDKIKDEQDLlhiRREIEIMSSLNHPHIIAIHE-VFENSSKIvIVMEYASRGD 140
Cdd:cd14066   1 IGSGGFGTVYKGVLENGTVVAVKRLNeMNCAASKKEF---LTELEMLGRLRHPNLVRLLGyCLESDEKL-LVYEYMPNGS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 141 LYDYISERP---------RLSerdarhFFRQIVSALHYCHQNG---IVHRDLKLENILLDANGNIKIADFGLSNLYHKGK 208
Cdd:cd14066  77 LEDRLHCHKgspplpwpqRLK------IAKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSE 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQT---FCGSPLYASPEIVNGKpYVGPEVDSWSLGVLLYILVHGTMPFD 255
Cdd:cd14066 151 SVSKtsaVKGTIGYLAPEYIRTG-RVSTKSDVYSFGVVLLELLTGKPAVD 199
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
61-275 2.12e-23

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 99.83  E-value: 2.12e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKD-EQDLLhirREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd05041   1 EKIGRGNFGDVYRGVlKPDNTEVAVKTCRETLPPDlKRKFL---QEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYI-SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKF-LQTFCGS 216
Cdd:cd05041  78 GSLLTFLrKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEEDGEYtVSDGLKQ 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27229182 217 -PL-YASPEIVNGKPYVGpEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGaYREPP 275
Cdd:cd05041 158 iPIkWTAPEALNYGRYTS-ESDVWSFGILLWeIFSLGATPYPGMSNQQTREQIESG-YRMPA 217
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
63-261 2.20e-23

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: 101.28  E-value: 2.20e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQD---LLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd14223   8 IGRGGFGEVYGCRKAdTGKMYAMKCLDKKRIKMKQGetlALNERIMLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKfLQTFCGSPL 218
Cdd:cd14223  88 GDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKK-PHASVGTHG 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 27229182 219 YASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFdgQDHKT 261
Cdd:cd14223 167 YMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPF--RQHKT 207
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
53-303 3.56e-23

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: 100.13  E-value: 3.56e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKI----KDEQDLLHIRREIEIMSSLNHPHIIAIHEVFE-NS 126
Cdd:cd14040   4 LNERYLLLHLLGRGGFSEVYKAFDlYEQRYAAVKIHQLNKSwrdeKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDT 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 127 SKIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQ--NGIVHRDLKLENILL---DANGNIKIADFGLS 201
Cdd:cd14040  84 DTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLvdgTACGEIKITDFGLS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 202 NLYHKGKF-------LQTFCGSPLYASPE-IVNGK--PYVGPEVDSWSLGVLLYILVHGTMPF-DGQDHKTLVKQ---IS 267
Cdd:cd14040 164 KIMDDDSYgvdgmdlTSQGAGTYWYLPPEcFVVGKepPKISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntiLK 243
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 27229182 268 NGAYREPPKP---SDACGLIRWLLMVNPTRRATLEDVAS 303
Cdd:cd14040 244 ATEVQFPVKPvvsNEAKAFIRRCLAYRKEDRFDVHQLAS 282
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
51-261 3.72e-23

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: 101.29  E-value: 3.72e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  51 HNLRHRYEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQD---LLHIRREIEIMSSLNHPHIIAIHEVFENS 126
Cdd:cd05633   1 HLTMNDFSVHRIIGRGGFGEVYGCRKAdTGKMYAMKCLDKKRIKMKQGetlALNERIMLSLVSTGDCPFIVCMTYAFHTP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 127 SKIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHK 206
Cdd:cd05633  81 DKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSK 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27229182 207 GKfLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFdgQDHKT 261
Cdd:cd05633 161 KK-PHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPF--RQHKT 212
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
56-257 3.93e-23

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: 100.86  E-value: 3.93e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDLLhirrEIEIMSSLNHP------HIIAIHEVFENSSK 128
Cdd:cd14226  14 RYEIDSLIGKGSFGQVVKAYDHvEQEWVAIKIIKNKKAFLNQAQI----EVRLLELMNKHdtenkyYIVRLKRHFMFRNH 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IVIVMEYASRgDLYDYI--SERPRLSERDARHFFRQIVSALHYCHQN--GIVHRDLKLENILLdANGN---IKIADFGLS 201
Cdd:cd14226  90 LCLVFELLSY-NLYDLLrnTNFRGVSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPENILL-CNPKrsaIKIIDFGSS 167
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27229182 202 NlyHKGKFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVllyILV--HGTMP-FDGQ 257
Cdd:cd14226 168 C--QLGQRIYQYIQSRFYRSPEVLLGLPY-DLAIDMWSLGC---ILVemHTGEPlFSGA 220
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
57-256 4.86e-23

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: 99.65  E-value: 4.86e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIrkdKIKDEQDL-LHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd07870   2 YLNLEKLGEGSYATVYKGiSRINGQLVALKVI---SMKTEEGVpFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YAsRGDLYDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNlyHKGKFLQTF 213
Cdd:cd07870  79 YM-HTDLAQYMIQHPGgLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLAR--AKSIPSQTY 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 27229182 214 CGSPL---YASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDG 256
Cdd:cd07870 156 SSEVVtlwYRPPDVLLGATDYSSALDIWGAGCIFIEMLQGQPAFPG 201
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
57-256 5.10e-23

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: 99.77  E-value: 5.10e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKikDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd07869   7 YEKLEKLGEGSYATVYKGKSKvNGKLVALKVIRLQE--EEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 AsRGDLYDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLyhKGKFLQTFC 214
Cdd:cd07869  85 V-HTDLCQYMDKHPGgLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARA--KSVPSHTYS 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 27229182 215 GSPL---YASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDG 256
Cdd:cd07869 162 NEVVtlwYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPG 206
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
56-242 6.00e-23

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: 98.68  E-value: 6.00e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARESSGR-LVAIKSIR---KDKIKDEQDLLhirREIEIMSSLNHPHIIAIHEVFENSSKIVI 131
Cdd:cd06607   2 IFEDLREIGHGSFGAVYYARNKRTSeVVAIKKMSysgKQSTEKWQDII---KEVKFLRQLRHPNTIEYKGCYLREHTAWL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEY--ASRGDLYDyISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGkf 209
Cdd:cd06607  79 VMEYclGSASDIVE-VHKKP-LQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLVCPA-- 154
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 27229182 210 lQTFCGSPLYASPEIV---NGKPYVGpEVDSWSLGV 242
Cdd:cd06607 155 -NSFVGTPYWMAPEVIlamDEGQYDG-KVDVWSLGI 188
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
63-244 7.89e-23

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: 98.48  E-value: 7.89e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGK-VKKARESSGRLVAIKSIRKdkiKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd14222   1 LGKGFFGQaIKVTHKATGKVMVMKELIR---CDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQ---------- 211
Cdd:cd14222  78 KDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKKKPppdkpttkkr 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 27229182 212 -----------TFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLL 244
Cdd:cd14222 158 tlrkndrkkryTVVGNPYWMAPEMLNGKSY-DEKVDIFSFGIVL 200
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
54-245 7.99e-23

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 99.28  E-value: 7.99e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKV-------------KKARESSGR--LVAIKSIRKDKIKDEQ-DLLhirREIEIMSSLNHPHII 117
Cdd:cd05097   4 RQQLRLKEKLGEGQFGEVhlceaeglaeflgEGAPEFDGQpvLVAVKMLRADVTKTARnDFL---KEIKIMSRLKNPNII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 118 AIHEVFENSSKIVIVMEYASRGDLYDYISER------------PRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENI 185
Cdd:cd05097  81 RLLGVCVSDDPLCMITEYMENGDLNQFLSQReiestfthanniPSVSIANLLYMAVQIASGMKYLASLNFVHRDLATRNC 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27229182 186 LLDANGNIKIADFGLS-NLYHKGKF-LQTFCGSPL--YASPEIVNGKPYVGPevDSWSLGVLLY 245
Cdd:cd05097 161 LVGNHYTIKIADFGMSrNLYSGDYYrIQGRAVLPIrwMAWESILLGKFTTAS--DVWAFGVTLW 222
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
57-256 9.33e-23

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: 98.75  E-value: 9.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDkIKDEQDLLHIRREIEIMSSLNH-PHI---IAIHEVFEN-SSKIV 130
Cdd:cd07837   3 YEKLEKIGEGTYGKVYKARDkNTGKLVALKKTRLE-MEEEGVPSTALREVSLLQMLSQsIYIvrlLDVEHVEENgKPLLY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 IVMEYASRgDLYDYISERPR-----LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLD-ANGNIKIADFGLSNLY 204
Cdd:cd07837  82 LVFEYLDT-DLKKFIDSYGRgphnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDkQKGLLKIADLGLGRAF 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 205 --------HKGKFLqtfcgspLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDG 256
Cdd:cd07837 161 tipiksytHEIVTL-------WYRAPEVLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPG 213
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
59-303 1.04e-22

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 98.55  E-value: 1.04e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  59 FLETLGKGTYGKVKK------ARESSGRLVAIKSIrkdKIKDEQDLLH-IRREIEIMSSLNHPHIIAIHEVFENSSKIVI 131
Cdd:cd05091  10 FMEELGEDRFGKVYKghlfgtAPGEQTQAVAIKTL---KDKAEGPLREeFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDYISERP----------------RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKI 195
Cdd:cd05091  87 IFSYCSHGDLHEFLVMRSphsdvgstdddktvksTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKI 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 196 ADFGLSNLYHKGKFLQTFCGSPL---YASPE-IVNGKPYVgpEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNga 270
Cdd:cd05091 167 SDLGLFREVYAADYYKLMGNSLLpirWMSPEaIMYGKFSI--DSDIWSYGVVLWeVFSYGLQPYCGYSNQDVIEMIRN-- 242
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 27229182 271 yREPPKPSDACGLIRWLLMVN-----PTRRATLEDVAS 303
Cdd:cd05091 243 -RQVLPCPDDCPAWVYTLMLEcwnefPSRRPRFKDIHS 279
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
51-256 1.44e-22

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: 99.47  E-value: 1.44e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  51 HNLRHRYEFLETLGKGTYGKVKKARES-SGRLVAIKSIrkdKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSK- 128
Cdd:cd07854   1 FDLGSRYMDLRPLGCGSNGLVFSAVDSdCDKRVAVKKI---VLTDPQSVKHALREIKIIRRLDHDNIVKVYEVLGPSGSd 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 -------------IVIVMEYASrGDLYDYIsERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNI-K 194
Cdd:cd07854  78 ltedvgsltelnsVYIVQEYME-TDLANVL-EQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlK 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27229182 195 IADFGLSNLY-----HKGKFLQTFCgSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDG 256
Cdd:cd07854 156 IGDFGLARIVdphysHKGYLSEGLV-TKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAG 221
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
57-304 1.51e-22

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: 98.16  E-value: 1.51e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIrkDKIKDEQDllHIRREIEIMSSL-NHPHIIAIHEVF-----ENSSKI 129
Cdd:cd06638  20 WEIIETIGKGTYGKVFKVlNKKNGSKAAVKIL--DPIHDIDE--EIEAEYNILKALsDHPNVVKFYGMYykkdvKNGDQL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 130 VIVMEYASRGDLYD----YISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYH 205
Cdd:cd06638  96 WLVLELCNGGSVTDlvkgFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 206 KGKFLQ-TFCGSPLYASPEIVNGKPYVGP----EVDSWSLGVLLYILVHGTMPF-DGQDHKTLVKQISNgayrEPPK--- 276
Cdd:cd06638 176 STRLRRnTSVGTPFWMAPEVIACEQQLDStydaRCDVWSLGITAIELGDGDPPLaDLHPMRALFKIPRN----PPPTlhq 251
                       250       260       270
                ....*....|....*....|....*....|..
gi 27229182 277 ----PSDACGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd06638 252 pelwSNEFNDFIRKCLTKDYEKRPTVSDLLQH 283
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
61-306 1.97e-22

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: 97.34  E-value: 1.97e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARESSGRLVAIKSIRKD--KIKDeqdllhirREIEIM-SSLNHPHIIAIHEVFENSSKIVIVMEY-- 135
Cdd:cd13982   7 KVLGYGSEGTIVFRGTFDGRPVAVKRLLPEffDFAD--------REVQLLrESDEHPNVIRYFCTEKDRQFLYIALELca 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASrgdLYDYIsERPRLSERDARHFF------RQIVSALHYCHQNGIVHRDLKLENILLDA-----NGNIKIADFGLSNLY 204
Cdd:cd13982  79 AS---LQDLV-ESPRESKLFLRPGLepvrllRQIASGLAHLHSLNIVHRDLKPQNILISTpnahgNVRAMISDFGLCKKL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 205 HKGKflQTF------CGSPLYASPEIVNGKPYVGP--EVDSWSLG-VLLYILVHGTMPFDgqdhKTLVKQ--ISNGAY-- 271
Cdd:cd13982 155 DVGR--SSFsrrsgvAGTSGWIAPEMLSGSTKRRQtrAVDIFSLGcVFYYVLSGGSHPFG----DKLEREanILKGKYsl 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 27229182 272 ----REPPKPSDACGLIRWLLMVNPTRRATLEDVASH--WW 306
Cdd:cd13982 229 dkllSLGEHGPEAQDLIERMIDFDPEKRPSAEEVLNHpfFW 269
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
54-247 2.41e-22

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: 97.66  E-value: 2.41e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHrYEFLETLGKGTYGKVKKAR-----ESSGRLVAIKSIRKDKIKDEQDLlhiRREIEIMSSLNHPHIIAIHEVFENSSK 128
Cdd:cd05081   4 RH-LKYISQLGKGNFGSVELCRydplgDNTGALVAVKQLQHSGPDQQRDF---QREIQILKALHSDFIVKYRGVSYGPGR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 --IVIVMEYASRGDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYH 205
Cdd:cd05081  80 rsLRLVMEYLPSGCLRDFLQRhRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLP 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 27229182 206 KGK---FLQTFCGSPLY-ASPEIVNGKPYvGPEVDSWSLGVLLYIL 247
Cdd:cd05081 160 LDKdyyVVREPGQSPIFwYAPESLSDNIF-SRQSDVWSFGVVLYEL 204
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
54-299 3.15e-22

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 96.49  E-value: 3.15e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLlhirREIEIMSSLNHPHIIAIHEVFeNSSKIVIVM 133
Cdd:cd05067   6 RETLKLVERLGAGQFGEVWMGYYNGHTKVAIKSLKQGSMSPDAFL----AEANLMKQLQHQRLVRLYAVV-TQEPIYIIT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYI--SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFL- 210
Cdd:cd05067  81 EYMENGSLVDFLktPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTa 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 QTFCGSPL-YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGaYREpPKPsDACGLIRWLL 288
Cdd:cd05067 161 REGAKFPIkWTAPEAINYGTFT-IKSDVWSFGILLTeIVTHGRIPYPGMTNPEVIQNLERG-YRM-PRP-DNCPEELYQL 236
                       250
                ....*....|....*.
gi 27229182 289 MV-----NPTRRATLE 299
Cdd:cd05067 237 MRlcwkeRPEDRPTFE 252
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
63-254 3.21e-22

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: 96.59  E-value: 3.21e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAReSSGRLVAIKSIRKDKIKD-EQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd14148   2 IGVGGFGKVYKGL-WRGEEVAVKAARQDPDEDiAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERpRLSERDARHFFRQIVSALHYCHQNGIV---HRDLKLENILL--------DANGNIKIADFGLSNLYHKGKFL 210
Cdd:cd14148  81 NRALAGK-KVPPHVLVNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILIlepienddLSGKTLKITDFGLAREWHKTTKM 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 27229182 211 QTfCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF 254
Cdd:cd14148 160 SA-AGTYAWMAPEVIRLSLF-SKSSDVWSFGVLLWELLTGEVPY 201
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
54-276 4.24e-22

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 96.69  E-value: 4.24e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKA------RESSGRLVAIKSIRKD-KIKDEQDLLhirREIEIMSSLNHPHIIAIHEVFENS 126
Cdd:cd05036   5 RKNLTLIRALGQGAFGEVYEGtvsgmpGDPSPLQVAVKTLPELcSEQDEMDFL---MEALIMSKFNHPNIVRCIGVCFQR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 127 SKIVIVMEYASRGDLYDYISE-RPR------LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN---IKIA 196
Cdd:cd05036  82 LPRFILLELMAGGDLKSFLREnRPRpeqpssLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPgrvAKIG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 197 DFGL------SNLYHKGkflqtfcGSPL----YASPE-----IVNGKpyvgpeVDSWSLGVLLY-ILVHGTMPFDGQDHK 260
Cdd:cd05036 162 DFGMardiyrADYYRKG-------GKAMlpvkWMPPEafldgIFTSK------TDVWSFGVLLWeIFSLGYMPYPGKSNQ 228
                       250
                ....*....|....*.
gi 27229182 261 TLVKQISNGAYREPPK 276
Cdd:cd05036 229 EVMEFVTSGGRMDPPK 244
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
56-266 6.79e-22

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: 97.42  E-value: 6.79e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKikdeQDLLHIRR---EIEIMSSLNHPHIIAIHEVFENSSKI-- 129
Cdd:cd07877  18 RYQNLSPVGSGAYGSVCAAFDTkTGLRVAVKKLSRPF----QSIIHAKRtyrELRLLKHMKHENVIGLLDVFTPARSLee 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 130 ---VIVMEYASRGDLYDyISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNlyHK 206
Cdd:cd07877  94 fndVYLVTHLMGADLNN-IVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLAR--HT 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 207 GKFLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQI 266
Cdd:cd07877 171 DDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLI 230
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
58-301 7.30e-22

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 95.43  E-value: 7.30e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  58 EFLETLGKGTYGKVKKArESSGRLVAIKSIRKDKIKdeQDLLhirREIEIMSSLNHPHIIAIHEVF-ENSSKIVIVMEYA 136
Cdd:cd05082   9 KLLQTIGKGEFGDVMLG-DYRGNKVAVKCIKNDATA--QAFL---AEASVMTQLRHSNLVQLLGVIvEEKGGLYIVTEYM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 137 SRGDLYDYISERPR--LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNlyhKGKFLQTFC 214
Cdd:cd05082  83 AKGSLVDYLRSRGRsvLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTK---EASSTQDTG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 215 GSPL-YASPEIVNGKPYvGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAYREPPkpsDACGLIRWLLM--- 289
Cdd:cd05082 160 KLPVkWTAPEALREKKF-STKSDVWSFGILLWeIYSFGRVPYPRIPLKDVVPRVEKGYKMDAP---DGCPPAVYDVMknc 235
                       250
                ....*....|....
gi 27229182 290 --VNPTRRATLEDV 301
Cdd:cd05082 236 whLDAAMRPSFLQL 249
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
61-303 1.26e-21

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 94.75  E-value: 1.26e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARES-SGR---LVAIKSIrKDKIKDEQ--DLLHirrEIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd05033  10 KVIGGGEFGEVCSGSLKlPGKkeiDVAIKTL-KSGYSDKQrlDFLT---EASIMGQFDHPNVIRLEGVVTKSRPVMIVTE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTF 213
Cdd:cd05033  86 YMENGSLDKFLREnDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSEATYTT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CG--SPL-YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGaYREPPkPSDaCGLIRWLLM 289
Cdd:cd05033 166 KGgkIPIrWTAPEAIAYRKFT-SASDVWSFGIVMWeVMSYGERPYWDMSNQDVIKAVEDG-YRLPP-PMD-CPSALYQLM 241
                       250
                ....*....|....*....
gi 27229182 290 V-----NPTRRATLEDVAS 303
Cdd:cd05033 242 LdcwqkDRNERPTFSQIVS 260
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
54-274 1.63e-21

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: 94.72  E-value: 1.63e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLlhirREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd05072   6 RESIKLVKKLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFL----EEANLMKTLQHDKLVRLYAVVTKEEPIYIIT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYIS--ERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFL- 210
Cdd:cd05072  82 EYMAKGSLLDFLKsdEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTa 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27229182 211 QTFCGSPL-YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGaYREP 274
Cdd:cd05072 162 REGAKFPIkWTAPEAINFGSFT-IKSDVWSFGILLYeIVTYGKIPYPGMSNSDVMSALQRG-YRMP 225
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
56-256 1.74e-21

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 95.75  E-value: 1.74e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARES--SGRLVAIKSIRKdkikdeQDLLHI--RREIEIMSSLNHP------HIIAIHEVFEN 125
Cdd:cd14135   1 RYRVYGYLGKGVFSNVVRARDLarGNQEVAIKIIRN------NELMHKagLKELEILKKLNDAdpddkkHCIRLLRHFEH 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 126 SSKIVIVMEYASrGDLYDYISERPR---LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN-IKIADFGLS 201
Cdd:cd14135  75 KNHLCLVFESLS-MNLREVLKKYGKnvgLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNtLKLCDFGSA 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27229182 202 NLYHKG---KFLQtfcgSPLYASPEIVNGKPYVGPeVDSWSLGVLLYILVHGTMPFDG 256
Cdd:cd14135 154 SDIGENeitPYLV----SRFYRAPEIILGLPYDYP-IDMWSVGCTLYELYTGKILFPG 206
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
54-303 1.88e-21

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 94.72  E-value: 1.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKA------RESSGRLVAIKSIRKDKIKDEQdlLHIRREIEIMSSLNHPHIIAIHEVFENSS 127
Cdd:cd05032   5 REKITLIRELGQGSFGMVYEGlakgvvKGEPETRVAIKTVNENASMRER--IEFLNEASVMKEFNCHHVVRLLGVVSTGQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 128 KIVIVMEYASRGDLYDYI-SERPRLSER------DARHFFR---QIVSALHYCHQNGIVHRDLKLENILLDANGNIKIAD 197
Cdd:cd05032  83 PTLVVMELMAKGDLKSYLrSRRPEAENNpglgppTLQKFIQmaaEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGD 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 198 FGL------SNLYHK-GKFLQtfcgsPL-YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISN 268
Cdd:cd05032 163 FGMtrdiyeTDYYRKgGKGLL-----PVrWMAPESLKDGVFT-TKSDVWSFGVVLWeMATLAEQPYQGLSNEEVLKFVID 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 27229182 269 GAYREPPkpsDACGLIRWLLM-----VNPTRRATLEDVAS 303
Cdd:cd05032 237 GGHLDLP---ENCPDKLLELMrmcwqYNPKMRPTFLEIVS 273
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
63-275 2.13e-21

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 94.26  E-value: 2.13e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKA---RESSGRLVAIKSIRKDK----IKDEqdllhIRREIEIMSSLNHPHIIAIHEVFENSSkIVIVMEY 135
Cdd:cd05116   3 LGSGNFGTVKKGyyqMKKVVKTVAVKILKNEAndpaLKDE-----LLREANVMQQLDNPYIVRMIGICEAES-WMLVMEM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL------YHKGkf 209
Cdd:cd05116  77 AELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKAlradenYYKA-- 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27229182 210 lQTFCGSPL-YASPEIVNGKPYvGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAYREPP 275
Cdd:cd05116 155 -QTHGKWPVkWYAPECMNYYKF-SSKSDVWSFGVLMWeAFSYGQKPYKGMKGNEVTQMIEKGERMECP 220
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
61-301 2.45e-21

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


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 93.95  E-value: 2.45e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKA--RESSGRL--VAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFEnSSKIVIVMEYA 136
Cdd:cd05040   1 EKLGDGSFGVVRRGewTTPSGKViqVAVKCLKSDVLSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVL-SSPLMMVTELA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 137 SRGDLYDyiserpRLseRDARHFF---------RQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKG 207
Cdd:cd05040  80 PLGSLLD------RL--RKDQGHFlistlcdyaVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALPQN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 208 K--FLQTFCGSPLYA--SPEIVNGKPYVGPEvDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQI-SNGAYREPPK--PSD 279
Cdd:cd05040 152 EdhYVMQEHRKVPFAwcAPESLKTRKFSHAS-DVWMFGVTLWeMFTYGEEPWLGLNGSQILEKIdKEGERLERPDdcPQD 230
                       250       260
                ....*....|....*....|..
gi 27229182 280 ACGLIRWLLMVNPTRRATLEDV 301
Cdd:cd05040 231 IYNVMLQCWAHKPADRPTFVAL 252
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
63-264 2.85e-21

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: 94.04  E-value: 2.85e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDLLHIRREiEIMSSL-----NHPHIIAIHEVFENSSKIVIVMEYA 136
Cdd:cd05606   2 IGRGGFGEVYGCRKAdTGKMYAMKCLDKKRIKMKQGETLALNE-RIMLSLvstggDCPFIVCMTYAFQTPDKLCFILDLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 137 SRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKfLQTFCGS 216
Cdd:cd05606  81 NGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFSKKK-PHASVGT 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 27229182 217 PLYASPEIV-NGKPYVGPeVDSWSLGVLLYILVHGTMPFdgQDHKTLVK 264
Cdd:cd05606 160 HGYMAPEVLqKGVAYDSS-ADWFSLGCMLYKLLKGHSPF--RQHKTKDK 205
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
56-266 2.88e-21

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: 95.50  E-value: 2.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARESSGRL-VAIKSIRKDKikdeQDLLHIRR---EIEIMSSLNHPHIIAIHEVF------EN 125
Cdd:cd07878  16 RYQNLTPVGSGAYGSVCSAYDTRLRQkVAVKKLSRPF----QSLIHARRtyrELRLLKHMKHENVIGLLDVFtpatsiEN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 126 SSKIVIVMEYASrGDLYDyISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNlyH 205
Cdd:cd07878  92 FNEVYLVTNLMG-ADLNN-IVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLAR--Q 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27229182 206 KGKFLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQI 266
Cdd:cd07878 168 ADDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRI 228
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
63-280 3.01e-21

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: 94.87  E-value: 3.01e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARES-SGRLVAIK---SIRKDKIKDEQdllhiRREIEIMSSLNHPHIIAIHEVFE--NSSKIVIVMEYA 136
Cdd:cd13988   1 LGQGATANVFRGRHKkTGDLYAVKvfnNLSFMRPLDVQ-----MREFEVLKKLNHKNIVKLFAIEEelTTRHKVLVMELC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 137 SRGDLYDyISERPR----LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENIL--LDANGN--IKIADFGLS-NLYHKG 207
Cdd:cd13988  76 PCGSLYT-VLEEPSnaygLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQsvYKLTDFGAArELEDDE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 208 KFLQTFcGSPLYASPEIVN--------GKPYvGPEVDSWSLGVLLYILVHGTMPF----DGQDHKTLVKQISNGayrepp 275
Cdd:cd13988 155 QFVSLY-GTEEYLHPDMYEravlrkdhQKKY-GATVDLWSIGVTFYHAATGSLPFrpfeGPRRNKEVMYKIITG------ 226

                ....*
gi 27229182 276 KPSDA 280
Cdd:cd13988 227 KPSGA 231
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
57-254 3.98e-21

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


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 94.40  E-value: 3.98e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIrkDKIKDEQDllHIRREIEIMSSLNHPHIIAIHE---VFEN----SSK 128
Cdd:cd06637   8 FELVELVGNGTYGQVYKGRHvKTGQLAAIKVM--DVTGDEEE--EIKQEINMLKKYSHHRNIATYYgafIKKNppgmDDQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IVIVMEYASRGDLYDYI--SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-NLYH 205
Cdd:cd06637  84 LWLVMEFCGAGSVTDLIknTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSaQLDR 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 27229182 206 KGKFLQTFCGSPLYASPEIV----NGKPYVGPEVDSWSLGVLLYILVHGTMPF 254
Cdd:cd06637 164 TVGRRNTFIGTPYWMAPEVIacdeNPDATYDFKSDLWSLGITAIEMAEGAPPL 216
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
57-254 5.01e-21

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 93.53  E-value: 5.01e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARE-SSGRLVAIKSIrkDKIKDEQDllHIRREIEIMSSLNHPHIIAIHE-VFENSS------K 128
Cdd:cd06636  18 FELVEVVGNGTYGQVYKGRHvKTGQLAAIKVM--DVTEDEEE--EIKLEINMLKKYSHHRNIATYYgAFIKKSppghddQ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IVIVMEYASRGDLYDYI--SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-NLYH 205
Cdd:cd06636  94 LWLVMEFCGAGSVTDLVknTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSaQLDR 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 27229182 206 KGKFLQTFCGSPLYASPEIV----NGKPYVGPEVDSWSLGVLLYILVHGTMPF 254
Cdd:cd06636 174 TVGRRNTFIGTPYWMAPEVIacdeNPDATYDYRSDIWSLGITAIEMAEGAPPL 226
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
63-303 8.25e-21

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


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 92.68  E-value: 8.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAReSSGRLVAIKSIRKDKIK-----------DEQDLLH-------IRREIEIMSSLNHPHIIAIheVFE 124
Cdd:cd14000   2 LGDGGFGSVYRAS-YKGEPVAVKIFNKHTSSnfanvpadtmlRHLRATDamknfrlLRQELTVLSHLHHPSIVYL--LGI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 125 NSSKIVIVMEYASRGDLYDYISERPRLSERDARHFFR----QIVSALHYCHQNGIVHRDLKLENIL---LDANG--NIKI 195
Cdd:cd14000  79 GIHPLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQrialQVADGLRYLHSAMIIYRDLKSHNVLvwtLYPNSaiIIKI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 196 ADFGLSN-LYHKGkfLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNG----- 269
Cdd:cd14000 159 ADYGISRqCCRMG--AKGSEGTPGFRAPEIARGNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHGGlrppl 236
                       250       260       270
                ....*....|....*....|....*....|....
gi 27229182 270 AYREPPKPSDACGLIRWLLMVNPTRRATLEDVAS 303
Cdd:cd14000 237 KQYECAPWPEVEVLMKKCWKENPQQRPTAVTVVS 270
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
54-297 1.04e-20

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: 92.87  E-value: 1.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKA-------RESSGRLVAIKSIRKDKikDEQDLLHIRREIEIMSSL-NHPHIIAIHEVFEN 125
Cdd:cd05053  11 RDRLTLGKPLGEGAFGQVVKAeavgldnKPNEVVTVAVKMLKDDA--TEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 126 SSKIVIVMEYASRGDLYDYISER----------------PRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDA 189
Cdd:cd05053  89 DGPLYVVVEYASKGNLREFLRARrppgeeaspddprvpeEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVTE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 190 NGNIKIADFGLSNLYHKGKFLQTFCGSPL---YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQ 265
Cdd:cd05053 169 DNVMKIADFGLARDIHHIDYYRKTTNGRLpvkWMAPEALFDRVYT-HQSDVWSFGVLLWeIFTLGGSPYPGIPVEELFKL 247
                       250       260       270
                ....*....|....*....|....*....|....
gi 27229182 266 ISNGAYREPPK--PSDACGLIRWLLMVNPTRRAT 297
Cdd:cd05053 248 LKEGHRMEKPQncTQELYMLMRDCWHEVPSQRPT 281
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
101-304 1.66e-20

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: 91.27  E-value: 1.66e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 101 IRREIEIMSSLNHPHII-----AIHEVFENSS-KIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNG 174
Cdd:cd14012  45 LEKELESLKKLRHPNLVsylafSIERRGRSDGwKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNG 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 175 IVHRDLKLENILLDAN---GNIKIADFGLSNLYHK--GKFLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVH 249
Cdd:cd14012 125 VVHKSLHAGNVLLDRDagtGIVKLTDYSLGKTLLDmcSRGSLDEFKQTYWLPPELAQGSKSPTRKTDVWDLGLLFLQMLF 204
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 27229182 250 gtmpfdGQDhkTLVKQISNGAYREPPK-PSDACGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd14012 205 ------GLD--VLEKYTSPNPVLVSLDlSASLQDFLSKCLSLDPKKRPTALELLPH 252
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
61-301 2.13e-20

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 90.84  E-value: 2.13e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDeqdlLHIR--REIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd05085   2 ELLGKGNFGEVYKGTLKDKTPVAVKTCKEDLPQE----LKIKflSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYI-SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCGS- 216
Cdd:cd05085  78 GDFLSFLrKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSSGLKQi 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 217 PL-YASPEIVNGKPYVGpEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAYREPPK--PSDACGLIRWLLMVNP 292
Cdd:cd05085 158 PIkWTAPEALNYGRYSS-ESDVWSFGILLWeTFSLGVCPYPGMTNQQAREQVEKGYRMSAPQrcPEDIYKIMQRCWDYNP 236

                ....*....
gi 27229182 293 TRRATLEDV 301
Cdd:cd05085 237 ENRPKFSEL 245
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
58-269 2.16e-20

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 91.26  E-value: 2.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  58 EFLETLGKGTYGKVKKARESSGrlVAIKSIRKDKIKDEQDLLhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYAS 137
Cdd:cd14063   3 EIKEVIGKGRFGRVHRGRWHGD--VAIKLLNIDYLNEEQLEA-FKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLCK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 138 RGDLYDYISER-PRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDaNGNIKIADFGLSNLYHKGKFLQTFCGS 216
Cdd:cd14063  80 GRTLYSLIHERkEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLE-NGRVVITDFGLFSLSGLLQPGRREDTL 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27229182 217 PL------YASPEIVNG----------KPYVgPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNG 269
Cdd:cd14063 159 VIpngwlcYLAPEIIRAlspdldfeesLPFT-KASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCG 226
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
56-259 2.18e-20

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: 92.86  E-value: 2.18e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKDKikdeQDLLHIRR---EIEIMSSLNHPHIIAIHEVF------EN 125
Cdd:cd07850   1 RYQNLKPIGSGAQGIVCAAYDTvTGQNVAIKKLSRPF----QNVTHAKRayrELVLMKLVNHKNIIGLLNVFtpqkslEE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 126 SSKIVIVMEYASrGDLYDYIS---ERPRLSerdarHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN 202
Cdd:cd07850  77 FQDVYLVMELMD-ANLCQVIQmdlDHERMS-----YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 27229182 203 LYHKGKFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDH 259
Cdd:cd07850 151 TAGTSFMMTPYVVTRYYRAPEVILGMGY-KENVDIWSVGCIMGEMIRGTVLFPGTDH 206
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
54-204 2.30e-20

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 92.01  E-value: 2.30e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVK-----------------KARESSGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHI 116
Cdd:cd05051   4 REKLEFVEKLGEGQFGEVHlceanglsdltsddfigNDNKDEPVLVAVKMLRPDASKNARE--DFLKEVKIMSQLKDPNI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 117 IAIHEVFENSSKIVIVMEYASRGDLYDYISER------------PRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLEN 184
Cdd:cd05051  82 VRLLGVCTRDEPLCMIVEYMENGDLNQFLQKHeaetqgasatnsKTLSYGTLLYMATQIASGMKYLESLNFVHRDLATRN 161
                       170       180
                ....*....|....*....|.
gi 27229182 185 ILLDANGNIKIADFGLS-NLY 204
Cdd:cd05051 162 CLVGPNYTIKIADFGMSrNLY 182
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
49-258 2.55e-20

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: 93.27  E-value: 2.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  49 HKHnLRHRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQdllhIRREIEIMSSL------NHPHIIAIHE 121
Cdd:cd14224  60 HDH-IAYRYEVLKVIGKGSFGQVVKAYDhKTHQHVALKMVRNEKRFHRQ----AAEEIRILEHLkkqdkdNTMNVIHMLE 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 122 VFENSSKIVIVMEYASRgDLYDYISERP--RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANG--NIKIAD 197
Cdd:cd14224 135 SFTFRNHICMTFELLSM-NLYELIKKNKfqGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGrsGIKVID 213
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27229182 198 FGLSNLYHKGkfLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQD 258
Cdd:cd14224 214 FGSSCYEHQR--IYTYIQSRFYRAPEVILGARY-GMPIDMWSFGCILAELLTGYPLFPGED 271
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
56-304 3.01e-20

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


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 91.33  E-value: 3.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARESS--GRLVAIKSIRKDKIKdEQDLLHIRREIEIMSSL---NHPHIIAIHEVFENSSKIV 130
Cdd:cd14052   1 RFANVELIGSGEFSQVYKVSERVptGKVYAVKKLKPNYAG-AKDRLRRLEEVSILRELtldGHDNIVQLIDSWEYHGHLY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 IVMEYASRGDLYDYISERPRLSERDARHFFRQIV---SALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKG 207
Cdd:cd14052  80 IQTELCENGSLDVFLSELGLLGRLDEFRVWKILVelsLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWPLI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 208 KFLQTFcGSPLYASPEIVNGKPYvGPEVDSWSLGVLLY-ILVHGTMPFDGQ-------------------DHKTLVKQIS 267
Cdd:cd14052 160 RGIERE-GDREYIAPEILSEHMY-DKPADIFSLGLILLeAAANVVLPDNGDawqklrsgdlsdaprlsstDLHSASSPSS 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 27229182 268 NGAYREPPKPSDACGL---IRWLLMVNPTRRATLEDVASH 304
Cdd:cd14052 238 NPPPDPPNMPILSGSLdrvVRWMLSPEPDRRPTADDVLAT 277
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
104-245 6.09e-20

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 92.37  E-value: 6.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  104 EIEIMSSLNHPHIIAIHEVFE-NSSKIVIVMEYasRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKL 182
Cdd:PHA03212 133 EAHILRAINHPSIIQLKGTFTyNKFTCLILPRY--KTDLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKA 210
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27229182  183 ENILLDANGNIKIADFGLS--------NLYHKgkflqtFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLY 245
Cdd:PHA03212 211 ENIFINHPGDVCLGDFGAAcfpvdinaNKYYG------WAGTIATNAPELLARDPY-GPAVDIWSAGIVLF 274
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
71-280 6.42e-20

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: 90.14  E-value: 6.42e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  71 VKKARESSGRLVAIKSIRKDKIKDEQdllhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDLYDYISERP- 149
Cdd:cd13992  17 VKKVGVYGGRTVAIKHITFSRTEKRT----ILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREi 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 150 ------RLSerdarhFFRQIVSALHYCH-QNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQtFCGSP----- 217
Cdd:cd13992  93 kmdwmfKSS------FIKDIVKGMNYLHsSSIGYHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNHQ-LDEDAqhkkl 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27229182 218 LYASPEIVNGKPYVG---PEVDSWSLGVLLYILVHGTMPFDGQDHKTLV-KQISNGayREPPKPSDA 280
Cdd:cd13992 166 LWTAPELLRGSLLEVrgtQKGDVYSFAIILYEILFRSDPFALEREVAIVeKVISGG--NKPFRPELA 230
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
63-254 6.86e-20

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: 89.51  E-value: 6.86e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAReSSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIA-IHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd14064   1 IGSGSFGKVYKGR-CRNKIVAIKRYRANTYCSKSDVDMFCREVSILCRLNHPCVIQfVGACLDDPSQFAIVTQYVSGGSL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERPRLSERDARHFFR-QIVSALHYCHQ--NGIVHRDLKLENILLDANGNIKIADFGLSnlyhkgKFLQTF----- 213
Cdd:cd14064  80 FSLLHEQKRVIDLQSKLIIAvDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGES------RFLQSLdednm 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 27229182 214 ---CGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPF 254
Cdd:cd14064 154 tkqPGNLRWMAPEVFTQCTRYSIKADVFSYALCLWELLTGEIPF 197
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
56-295 7.49e-20

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: 91.08  E-value: 7.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLLhirREIEIMSSLN--HPHIIAIHE----------- 121
Cdd:cd13977   1 KYSLIREVGRGSYGVVYEAvVRRTGARVAVKKIRCNAPENVELAL---REFWALSSIQrqHPNVIQLEEcvlqrdglaqr 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 122 -------------VFENSSK------------IVIVMEYASRGDLYDYISERpRLSERDARHFFRQIVSALHYCHQNGIV 176
Cdd:cd13977  78 mshgssksdlyllLVETSLKgercfdprsacyLWFVMEFCDGGDMNEYLLSR-RPDRQTNTSFMLQLSSALAFLHRNQIV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 177 HRDLKLENILLDANGN---IKIADFGLSNLYhKGK-------------FLQTFCGSPLYASPEIVNGkpYVGPEVDSWSL 240
Cdd:cd13977 157 HRDLKPDNILISHKRGepiLKVADFGLSKVC-SGSglnpeepanvnkhFLSSACGSDFYMAPEVWEG--HYTAKADIFAL 233
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27229182 241 GVLLYILVHGTMPFDGQDHKTLV-KQISNG--------AYREPPK-------------PSDACGLIRWLLMVNPTRR 295
Cdd:cd13977 234 GIIIWAMVERITFRDGETKKELLgTYIQQGkeivplgeALLENPKlelqiplkkkksmNDDMKQLLRDMLAANPQER 310
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
60-257 7.93e-20

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: 92.03  E-value: 7.93e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  60 LETLGKGTYGKVKKARESSGR-LVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd05625   6 IKTLGIGAFGEVCLARKVDTKaLYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLY---HKGKFLQT--- 212
Cdd:cd05625  86 GDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFrwtHDSKYYQSgdh 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 ------------------FCGSPLYA-------------SPEIVNGKPYVGPEV----------DSWSLGVLLYILVHGT 251
Cdd:cd05625 166 lrqdsmdfsnewgdpencRCGDRLKPlerraarqhqrclAHSLVGTPNYIAPEVllrtgytqlcDWWSVGVILFEMLVGQ 245

                ....*.
gi 27229182 252 MPFDGQ 257
Cdd:cd05625 246 PPFLAQ 251
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
59-269 1.05e-19

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx 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: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 89.17  E-value: 1.05e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  59 FLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLlhirREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd05113   8 FLKELGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSEDEFI----EEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMAN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFcGSP 217
Cdd:cd05113  84 GCLLNYLREmRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSV-GSK 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 27229182 218 L---YASPEIVNGKPYvGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNG 269
Cdd:cd05113 163 FpvrWSPPEVLMYSKF-SSKSDVWAFGVLMWeVYSLGKMPYERFTNSETVEHVSQG 217
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
54-301 1.08e-19

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk 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: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 89.89  E-value: 1.08e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKARES---SGR---LVAIKSIRKDKIKDEQdlLHIRREIEIMSSLNHPHIIAIHEVFENSS 127
Cdd:cd05050   4 RNNIEYVRDIGQGAFGRVFQARAPgllPYEpftMVAVKMLKEEASADMQ--ADFQREAALMAEFDHPNIVKLLGVCAVGK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 128 KIVIVMEYASRGDLYDYISER----------------------PRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENI 185
Cdd:cd05050  82 PMCLLFEYMAYGDLNEFLRHRspraqcslshstssarkcglnpLPLSCTEQLCIAKQVAAGMAYLSERKFVHRDLATRNC 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 186 LLDANGNIKIADFGLS-NLYhkgkfLQTFCGS------PL-YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDG 256
Cdd:cd05050 162 LVGENMVVKIADFGLSrNIY-----SADYYKAsendaiPIrWMPPESIFYNRYT-TESDVWAYGVVLWeIFSYGMQPYYG 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 27229182 257 QDHKTLVKQISNGAYREPPK--PSDACGLIRWLLMVNPTRRATLEDV 301
Cdd:cd05050 236 MAHEEVIYYVRDGNVLSCPDncPLELYNLMRLCWSKLPSDRPSFASI 282
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
63-244 1.45e-19

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: 88.86  E-value: 1.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKA--RESSGRLVAIKSIRKDkikdEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGD 140
Cdd:cd14221   1 LGKGCFGQAIKVthRETGEVMVMKELIRFD----EETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 141 LYDYI----SERPrLSERDArhFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQ----- 211
Cdd:cd14221  77 LRGIIksmdSHYP-WSQRVS--FAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQPeglrs 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 27229182 212 ----------TFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLL 244
Cdd:cd14221 154 lkkpdrkkryTVVGNPYWMAPEMINGRSY-DEKVDVFSFGIVL 195
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
54-299 1.57e-19

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: 90.02  E-value: 1.57e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKA--------RESSGRLVAIKSIrKDKIKDeQDLLHIRREIEIMSSLN-HPHIIAIHEVFE 124
Cdd:cd05099  11 RDRLVLGKPLGEGCFGQVVRAeaygidksRPDQTVTVAVKML-KDNATD-KDLADLISEMELMKLIGkHKNIINLLGVCT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 125 NSSKIVIVMEYASRGDLYDYISER-----------PRLSE-----RDARHFFRQIVSALHYCHQNGIVHRDLKLENILLD 188
Cdd:cd05099  89 QEGPLYVIVEYAAKGNLREFLRARrppgpdytfdiTKVPEeqlsfKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVT 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 189 ANGNIKIADFGLSNLYHKGKFLQTFCGSPL---YASPEIVNGKPYVGpEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVK 264
Cdd:cd05099 169 EDNVMKIADFGLARGVHDIDYYKKTSNGRLpvkWMAPEALFDRVYTH-QSDVWSFGILMWeIFTLGGSPYPGIPVEELFK 247
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 27229182 265 QISNGAYREPPK--PSDACGLIRWLLMVNPTRRATLE 299
Cdd:cd05099 248 LLREGHRMDKPSncTHELYMLMRECWHAVPTQRPTFK 284
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
62-310 1.66e-19

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: 89.21  E-value: 1.66e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  62 TLGKGTYGKVKKAR----ESSGRLVAIKSIRKDkIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKI------VI 131
Cdd:cd05074  16 MLGKGEFGSVREAQlkseDGSFQKVAVKMLKAD-IFSSSDIEEFLREAACMKEFDHPNVIKLIGVSLRSRAKgrlpipMV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDY-----ISERP-RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYH 205
Cdd:cd05074  95 ILPFMKHGDLHTFllmsrIGEEPfTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGLSKKIY 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 206 KGKFLQTFCGSPL---YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQ-ISNGAYREPPK-PSD 279
Cdd:cd05074 175 SGDYYRQGCASKLpvkWLALESLADNVYT-THSDVWAFGVTMWeIMTRGQTPYAGVENSEIYNYlIKGNRLKQPPDcLED 253
                       250       260       270
                ....*....|....*....|....*....|.
gi 27229182 280 ACGLIRWLLMVNPTRRATLEDVASHWWVNWG 310
Cdd:cd05074 254 VYELMCQCWSPEPKCRPSFQHLRDQLELIWG 284
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
63-301 1.93e-19

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: 88.83  E-value: 1.93e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-----ESSGRLVAIKSIRKDKikDEQDLLHIRREIEIMSSLNHPHIIAIHEVF--ENSSKIVIVMEY 135
Cdd:cd05079  12 LGEGHFGKVELCRydpegDNTGEQVAVKSLKPES--GGNHIADLKKEIEILRNLYHENIVKYKGICteDGGNGIKLIMEF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTF- 213
Cdd:cd05079  90 LPSGSLKEYLPRnKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVk 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 --CGSPL--YASPEIVNGKPYVGPEVdsWSLGVLLYILV------HGTM--------PFDGQDHKT-LVKQISNGAY--R 272
Cdd:cd05079 170 ddLDSPVfwYAPECLIQSKFYIASDV--WSFGVTLYELLtycdseSSPMtlflkmigPTHGQMTVTrLVRVLEEGKRlpR 247
                       250       260
                ....*....|....*....|....*....
gi 27229182 273 EPPKPSDACGLIRWLLMVNPTRRATLEDV 301
Cdd:cd05079 248 PPNCPEEVYQLMRKCWEFQPSKRTTFQNL 276
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
63-303 2.06e-19

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: 88.05  E-value: 2.06e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLlhirREIEIMSSLNHPHIIAIHEVFeNSSKIVIVMEYASRGDLY 142
Cdd:cd14203   3 LGQGCFGEVWMGTWNGTTKVAIKTLKPGTMSPEAFL----EEAQIMKKLRHDKLVQLYAVV-SEEPIYIVTEFMSKGSLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 143 DYISER-------PRLSERDArhffrQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFlqTFC- 214
Cdd:cd14203  78 DFLKDGegkylklPQLVDMAA-----QIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEY--TARq 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 215 GS--PL-YASPE-IVNGKPYVGPEVdsWSLGVLLYILV-HGTMPFDGQDHKTLVKQISNGaYREPPKPSDACGLIRWLLM 289
Cdd:cd14203 151 GAkfPIkWTAPEaALYGRFTIKSDV--WSFGILLTELVtKGRVPYPGMNNREVLEQVERG-YRMPCPPGCPESLHELMCQ 227
                       250
                ....*....|....*..
gi 27229182 290 V---NPTRRATLEDVAS 303
Cdd:cd14203 228 CwrkDPEERPTFEYLQS 244
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
57-254 2.14e-19

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: 89.28  E-value: 2.14e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKArESSGRLVAIKSIRKDKiKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIV---M 133
Cdd:cd08216   4 YEIGKCFKGGGVVHLAKH-KPTNTLVAVKKINLES-DSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVtplM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYD-YISERprLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIAdfGLSNLYH---KGKF 209
Cdd:cd08216  82 AYGSCRDLLKtHFPEG--LPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLS--GLRYAYSmvkHGKR 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 27229182 210 LQTFCGSPLYA-------SPEIV--NGKPYvGPEVDSWSLGVLLYILVHGTMPF 254
Cdd:cd08216 158 QRVVHDFPKSSeknlpwlSPEVLqqNLLGY-NEKSDIYSVGITACELANGVVPF 210
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
53-266 3.10e-19

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


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 89.63  E-value: 3.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLETLGKGTYGKVKKARES-SGRLVAIKSIRKdkiKDEQDLLHIR--REIEIMSSLNHPHIIAIHEVF------ 123
Cdd:cd07880  13 VPDRYRDLKQVGSGAYGTVCSALDRrTGAKVAIKKLYR---PFQSELFAKRayRELRLLKHMKHENVIGLLDVFtpdlsl 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 124 ENSSKIVIVMEYAsrGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNl 203
Cdd:cd07880  90 DRFHDFYLVMPFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLAR- 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27229182 204 yHKGKFLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQI 266
Cdd:cd07880 167 -QTDSEMTGYVVTRWYRAPEVILNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEI 228
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
63-244 3.43e-19

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: 87.55  E-value: 3.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIKSIRKDkikDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd14065   1 LGKGFFGEVYKVTHrETGKVMVMKELKRF---DEQR--SFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYI-SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL---DANGNIKIADFGLSNL-----YHKG--KFL 210
Cdd:cd14065  76 EELLkSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREmpdekTKKPdrKKR 155
                       170       180       190
                ....*....|....*....|....*....|....
gi 27229182 211 QTFCGSPLYASPEIVNGKPYVGpEVDSWSLGVLL 244
Cdd:cd14065 156 LTVVGSPYWMAPEMLRGESYDE-KVDVFSFGIVL 188
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
57-307 3.59e-19

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


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 88.65  E-value: 3.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARES-SGRLVAIKSIR---KDKIKDEqdllhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd06615   3 FEKLGELGAGNGGVVTKVLHRpSGLIMARKLIHleiKPAIRNQ-----IIRELKVLHECNSPYIVGFYGAFYSDGEISIC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQN-GIVHRDLKLENILLDANGNIKIADFGLSNLYHKgKFLQ 211
Cdd:cd06615  78 MEHMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID-SMAN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKPYVgPEVDSWSLGVLLYILVHGTMPFDGQDHKTL-------VKQISNGAYRE----------- 273
Cdd:cd06615 157 SFVGTRSYMSPERLQGTHYT-VQSDIWSLGLSLVEMAIGRYPIPPPDAKELeamfgrpVSEGEAKESHRpvsghppdspr 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27229182 274 ---------------PPK-PSDA-----CGLIRWLLMVNPTRRATLEDVASHWWV 307
Cdd:cd06615 236 pmaifelldyivnepPPKlPSGAfsdefQDFVDKCLKKNPKERADLKELTKHPFI 290
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
60-242 4.13e-19

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


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 88.56  E-value: 4.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  60 LETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY--A 136
Cdd:cd06633  26 LHEIGHGSFGAVYFATNShTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYclG 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 137 SRGDLYDyISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGkflQTFCGS 216
Cdd:cd06633 106 SASDLLE-VHKKP-LQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPA---NSFVGT 180
                       170       180
                ....*....|....*....|....*....
gi 27229182 217 PLYASPEIV---NGKPYVGpEVDSWSLGV 242
Cdd:cd06633 181 PYWMAPEVIlamDEGQYDG-KVDIWSLGI 208
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
63-303 4.90e-19

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 87.39  E-value: 4.90e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLlhirREIEIMSSLNHPHIIAIHEVFeNSSKIVIVMEYASRGDLY 142
Cdd:cd05073  19 LGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVEAFL----AEANVMKTLQHDKLVKLHAVV-TKEPIYIITEFMAKGSLL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 143 DYIS--ERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFL-QTFCGSPL- 218
Cdd:cd05073  94 DFLKsdEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTaREGAKFPIk 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 219 YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGaYREPpkPSDACGLIRWLLMV-----NP 292
Cdd:cd05073 174 WTAPEAINFGSFT-IKSDVWSFGILLMeIVTYGRIPYPGMSNPEVIRALERG-YRMP--RPENCPEELYNIMMrcwknRP 249
                       250
                ....*....|.
gi 27229182 293 TRRATLEDVAS 303
Cdd:cd05073 250 EERPTFEYIQS 260
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
61-279 4.96e-19

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 87.40  E-value: 4.96e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARESSGRLVAIKSIRKDK-IKDEQDLLHIRREIEIMSSL-NHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd05047   1 DVIGEGNFGQVLKARIKKDGLRMDAAIKRMKeYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYI----------------SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS- 201
Cdd:cd05047  81 GNLLDFLrksrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSr 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 202 --NLYHKgkflQTFCGSPL-YASPEIVNGKPYVgPEVDSWSLGVLLYILVH-GTMPFDGQDHKTLVKQISNGAYREPPKP 277
Cdd:cd05047 161 gqEVYVK----KTMGRLPVrWMAIESLNYSVYT-TNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGYRLEKPLN 235

                ..
gi 27229182 278 SD 279
Cdd:cd05047 236 CD 237
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
62-303 5.35e-19

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, 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. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 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: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 87.52  E-value: 5.35e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  62 TLGKGTYGKVKKAR------ESSGRLVAIKSIrkDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd05046  12 TLGRGEFGEVFLAKakgieeEGGETLVLVKAL--QKTKDENLQSEFRRELDMFRKLSHKNVVRLLGLCREAEPHYMILEY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYI---------SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSN---- 202
Cdd:cd05046  90 TDLGDLKQFLratkskdekLKPPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSKdvyn 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 203 -LYHkgKFLQTFCgsPL-YASPEIVNGKPYvGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAYREPPK--- 276
Cdd:cd05046 170 sEYY--KLRNALI--PLrWLAPEAVQEDDF-STKSDVWSFGVLMWeVFTQGELPFYGLSDEEVLNRLQAGKLELPVPegc 244
                       250       260
                ....*....|....*....|....*..
gi 27229182 277 PSDACGLIRWLLMVNPTRRATLEDVAS 303
Cdd:cd05046 245 PSRLYKLMTRCWAVNPKDRPSFSELVS 271
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
51-302 5.44e-19

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


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 87.52  E-value: 5.44e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  51 HNLRHRYEFLETLGKGTYGKVKKAR------ESSGRLVAIKSIRKDKIKDEQDLLHirREIEIMSSLNHPHIIAIHEVFE 124
Cdd:cd05049   1 HIKRDTIVLKRELGEGAFGKVFLGEcynlepEQDKMLVAVKTLKDASSPDARKDFE--REAELLTNLQHENIVKFYGVCT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 125 NSSKIVIVMEYASRGDLYDYI--------------SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDAN 190
Cdd:cd05049  79 EGDPLLMVFEYMEHGDLNKFLrshgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 191 GNIKIADFGLS------NLYHKGkflqtfcGSPL----YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDGQDH 259
Cdd:cd05049 159 LVVKIGDFGMSrdiystDYYRVG-------GHTMlpirWMPPESILYRKFT-TESDVWSFGVVLWeIFTYGKQPWFQLSN 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 27229182 260 KTLVKQISNGAYREPPK--PSDACGLIRWLLMVNPTRRATLEDVA 302
Cdd:cd05049 231 TEVIECITQGRLLQRPRtcPSEVYAVMLGCWKREPQQRLNIKDIH 275
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
34-287 6.03e-19

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 90.14  E-value: 6.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   34 SPKPLmkkqAVKRHHHKHNLRHRYEFLETLGKGTYGK-----VKKARESSGRLVAIKSIRKDKIKDEQDL---------- 98
Cdd:PHA03210 131 GPVPL----AQAKLKHDDEFLAHFRVIDDLPAGAFGKificaLRASTEEAEARRGVNSTNQGKPKCERLIakrvkagsra 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   99 -LHIRREIEIMSSLNHPHIIAIHEVFENSSKI-VIVMEYasRGDLYDYI-------SERPRLSErdARHFFRQIVSALHY 169
Cdd:PHA03210 207 aIQLENEILALGRLNHENILKIEEILRSEANTyMITQKY--DFDLYSFMydeafdwKDRPLLKQ--TRAIMKQLLCAVEY 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  170 CHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGK--FLQTFCGSPLYASPEIVNGKPYVgpEV-DSWSLG-VLLY 245
Cdd:PHA03210 283 IHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKEReaFDYGWVGTVATNSPEILAGDGYC--EItDIWSCGlILLD 360
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 27229182  246 ILVHGTMPFDG---QDHKTLVKQISNGAYREPPKPSDACGLIRWL 287
Cdd:PHA03210 361 MLSHDFCPIGDgggKPGKQLLKIIDSLSVCDEEFPDPPCKLFDYI 405
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
63-303 7.07e-19

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 87.33  E-value: 7.07e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR------ESSGRLVAIKSIRKDKIKDEQDLlhiRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYA 136
Cdd:cd05092  13 LGEGAFGKVFLAEchnllpEQDKMLVAVKALKEATESARQDF---QREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYM 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 137 SRGDLYDYI-SERP--------------RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS 201
Cdd:cd05092  90 RHGDLNRFLrSHGPdakildggegqapgQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMS 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 202 NLYHKGKFLQTFCGSPL---YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAYREPPK- 276
Cdd:cd05092 170 RDIYSTDYYRVGGRTMLpirWMPPESILYRKFT-TESDIWSFGVVLWeIFTYGKQPWYQLSNTEAIECITQGRELERPRt 248
                       250       260
                ....*....|....*....|....*...
gi 27229182 277 -PSDACGLIRWLLMVNPTRRATLEDVAS 303
Cdd:cd05092 249 cPPEVYAIMQGCWQREPQQRHSIKDIHS 276
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
63-244 7.53e-19

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: 86.79  E-value: 7.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKV-KKARESSGRLVAIKSIRKdkiKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd14154   1 LGKGFFGQAiKVTHRETGEVMVMKELIR---FDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL----------------- 203
Cdd:cd14154  78 KDVLKDMARpLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLiveerlpsgnmspsetl 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 27229182 204 YHKG----KFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLL 244
Cdd:cd14154 158 RHLKspdrKKRYTVVGNPYWMAPEMLNGRSY-DEKVDIFSFGIVL 201
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
58-304 8.03e-19

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: 87.09  E-value: 8.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  58 EFLETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLLHIRREIEiMSSLNHPHIIAIHEVFENSSKIVIVMEY- 135
Cdd:cd06617   4 EVIEELGRGAYGVVDKMRhVPTGTIMAVKRIRATVNSQEQKRLLMDLDIS-MRSVDCPYTVTFYGALFREGDVWICMEVm 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 -ASRGDLYDYISERPRLSERDA-RHFFRQIVSALHYCHQN-GIVHRDLKLENILLDANGNIKIADFGLSNlYHKGKFLQT 212
Cdd:cd06617  83 dTSLDKFYKKVYDKGLTIPEDIlGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISG-YLVDSVAKT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 F-CGSPLYASPEIVNG----KPYvGPEVDSWSLGVLLYILVHGTMPFDgqDHKTLVKQISNGAYREPPK-PSDACGL--- 283
Cdd:cd06617 162 IdAGCKPYMAPERINPelnqKGY-DVKSDVWSLGITMIELATGRFPYD--SWKTPFQQLKQVVEEPSPQlPAEKFSPefq 238
                       250       260
                ....*....|....*....|...
gi 27229182 284 --IRWLLMVNPTRRATLEDVASH 304
Cdd:cd06617 239 dfVNKCLKKNYKERPNYPELLQH 261
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
61-295 9.22e-19

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes 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: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 86.14  E-value: 9.22e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRG 139
Cdd:cd05084   2 ERIGRGNFGEVFSGRlRADNTPVAVKSCRETLPPDLKA--KFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYI-SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQT--FCGS 216
Cdd:cd05084  80 DFLTFLrTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEDGVYAATggMKQI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 217 PL-YASPEIVNGKPYvGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAYREPPK--PSDACGLIRWLLMVNP 292
Cdd:cd05084 160 PVkWTAPEALNYGRY-SSESDVWSFGILLWeTFSLGAVPYANLSNQQTREAVEQGVRLPCPEncPDEVYRLMEQCWEYDP 238

                ...
gi 27229182 293 TRR 295
Cdd:cd05084 239 RKR 241
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
56-290 9.39e-19

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 86.70  E-value: 9.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKA-----RESSGRLVAIKSIRKDKikDEQDLLHIRREIEIMSSLNHPHIIAIHEVFEnSSKIV 130
Cdd:cd05057   8 ELEKGKVLGSGAFGTVYKGvwipeGEKVKIPVAIKVLREET--GPKANEEILDEAYVMASVDHPHLVRLLGICL-SSQVQ 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 IVMEYASRGDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL------ 203
Cdd:cd05057  85 LITQLMPLGCLLDYVRNhRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLldvdek 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 204 -YH--KGKFlqtfcgsPL-YASPEIVNGKPYVGpEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAYREPPkps 278
Cdd:cd05057 165 eYHaeGGKV-------PIkWMALESIQYRIYTH-KSDVWSYGVTVWeLMTFGAKPYEGIPAVEIPDLLEKGERLPQP--- 233
                       250
                ....*....|..
gi 27229182 279 DACGLIRWLLMV 290
Cdd:cd05057 234 PICTIDVYMVLV 245
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
53-266 1.06e-18

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 88.75  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   53 LRHRYEFLETLGKGTYGKV---KKARESSGRLVAIKSIRKDKIKDeqdllhirREIEIMSSLNHPHIIAIHEVFENSSKI 129
Cdd:PHA03207  90 VRMQYNILSSLTPGSEGEVfvcTKHGDEQRKKVIVKAVTGGKTPG--------REIDILKTISHRAIINLIHAYRWKSTV 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  130 VIVMEYaSRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFG----LSNLYH 205
Cdd:PHA03207 162 CMVMPK-YKCDLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGaackLDAHPD 240
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27229182  206 KGKfLQTFCGSPLYASPEIVNGKPYVGpEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQI 266
Cdd:PHA03207 241 TPQ-CYGWSGTLETNSPELLALDPYCA-KTDIWSAGLVLFEMSVKNVTLFGKQVKSSSSQL 299
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
63-266 1.24e-18

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 86.78  E-value: 1.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAReSSGRLVAIKSIRKDKIKDEQDLL-HIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd14158  23 LGEGGFGVVFKGY-INDKNVAVKKLAAMVDISTEDLTkQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNGSL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYIS---ERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNlyHKGKFLQTF----- 213
Cdd:cd14158 102 LDRLAclnDTPPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLAR--ASEKFSQTImteri 179
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 27229182 214 CGSPLYASPEIVNGKpyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQI 266
Cdd:cd14158 180 VGTTAYMAPEALRGE--ITPKSDIFSFGVVLLEIITGLPPVDENRDPQLLLDI 230
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
63-301 1.38e-18

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: 86.03  E-value: 1.38e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEqdllhirrEIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd13991  14 IGRGSFGEVHRMEDkQTGFQCAVKKVRLEVFRAE--------ELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGSL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANG-NIKIADFGLSNLYHK---GKFLQT---FC 214
Cdd:cd13991  86 GQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHAECLDPdglGKSLFTgdyIP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 215 GSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNgayrEPPK----PSDACGL----IRW 286
Cdd:cd13991 166 GTETHMAPEVVLGKP-CDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIAN----EPPPlreiPPSCAPLtaqaIQA 240
                       250
                ....*....|....*
gi 27229182 287 LLMVNPTRRATLEDV 301
Cdd:cd13991 241 GLRKEPVHRASAAEL 255
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
63-255 1.63e-18

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: 86.01  E-value: 1.63e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQdlLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDLY 142
Cdd:cd14664   1 IGRGGAGTVYKGVMPNGTLVAVKRLKGEGTQGGD--HGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 143 DYISERPRLSER---DARHffRQIVSALH---YCHQNG---IVHRDLKLENILLDANGNIKIADFGLSNL--YHKGKFLQ 211
Cdd:cd14664  79 ELLHSRPESQPPldwETRQ--RIALGSARglaYLHHDCsplIIHRDVKSNNILLDEEFEAHVADFGLAKLmdDKDSHVMS 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 27229182 212 TFCGSPLYASPEIV-NGKpyVGPEVDSWSLGVLLYILVHGTMPFD 255
Cdd:cd14664 157 SVAGSYGYIAPEYAyTGK--VSEKSDVYSYGVVLLELITGKRPFD 199
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
55-254 1.98e-18

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: 85.70  E-value: 1.98e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  55 HRYEFLETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd06619   1 QDIQYQEILGHGNGGTVYKAYHlLTRRILAVKVIPLDITVELQK--QIMSELEILYKCDSPYIIGFYGAFFVENRISICT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYiserPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYhKGKFLQTF 213
Cdd:cd06619  79 EFMDGGSLDVY----RKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQL-VNSIAKTY 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 27229182 214 CGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPF 254
Cdd:cd06619 154 VGTNAYMAPERISGEQY-GIHSDVWSLGISFMELALGRFPY 193
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
57-244 1.98e-18

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: 86.73  E-value: 1.98e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQdllhIRREIEIMSSLNHP-----HIIAIHEVFENSSKIV 130
Cdd:cd14211   1 YEVLEFLGRGTFGQVVKCwKRGTNEIVAIKILKNHPSYARQ----GQIEVSILSRLSQEnadefNFVRAYECFQHKNHTC 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 IVMEYASRgDLYDYISE---RPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN----IKIADFGLSNl 203
Cdd:cd14211  77 LVFEMLEQ-NLYDFLKQnkfSP-LPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRqpyrVKVIDFGSAS- 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27229182 204 yHKGKFLQ-TFCGSPLYASPEIVNGKPYVgPEVDSWSLGVLL 244
Cdd:cd14211 154 -HVSKAVCsTYLQSRYYRAPEIILGLPFC-EAIDMWSLGCVI 193
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
57-277 2.03e-18

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: 86.65  E-value: 2.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKV-KKARESSGRLVAIKSIR---KDKIKDEqdllhIRREIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd06650   7 FEKISELGAGNGGVVfKVSHKPSGLVMARKLIHleiKPAIRNQ-----IIRELQVLHECNSPYIVGFYGAFYSDGEISIC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQ-NGIVHRDLKLENILLDANGNIKIADFGLSnlyhkGKFL- 210
Cdd:cd06650  82 MEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREkHKIMHRDVKPSNILVNSRGEIKLCDFGVS-----GQLId 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27229182 211 ---QTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVK----QISNGAYREPPKP 277
Cdd:cd06650 157 smaNSFVGTRSYMSPERLQGTHY-SVQSDIWSMGLSLVEMAVGRYPIPPPDAKELELmfgcQVEGDAAETPPRP 229
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
63-301 2.14e-18

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 85.55  E-value: 2.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKSIRKDKIKDEQDLlhirREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDL 141
Cdd:cd05052  14 LGGGQYGEVYEGVwKKYNLTVAVKTLKEDTMEVEEFL----KEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 YDYISERPRlSERDA---RHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLY-------HKG-KFl 210
Cdd:cd05052  90 LDYLRECNR-EELNAvvlLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMtgdtytaHAGaKF- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 qtfcgsPL-YASPEivnGKPY--VGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAYREPPK--PSDACGLI 284
Cdd:cd05052 168 ------PIkWTAPE---SLAYnkFSIKSDVWAFGVLLWeIATYGMSPYPGIDLSQVYELLEKGYRMERPEgcPPKVYELM 238
                       250
                ....*....|....*..
gi 27229182 285 RWLLMVNPTRRATLEDV 301
Cdd:cd05052 239 RACWQWNPSDRPSFAEI 255
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
63-199 2.31e-18

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: 81.72  E-value: 2.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKA-RESSGRLVAIKSIRkdkIKDEQDLLHIRREIEIMSSL-NH-PHIIAIHEVFENSSKIVIVMEYASRG 139
Cdd:cd13968   1 MGEGASAKVFWAeGECTTIGVAVKIGD---DVNNEEGEDLESEMDILRRLkGLeLNIPKVLVTEDVDGPNILLMELVKGG 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYISERpRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFG 199
Cdd:cd13968  78 TLIAYTQEE-ELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
62-303 2.59e-18

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: 85.78  E-value: 2.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  62 TLGKGTYGKVKK--ARESSGR----LVAIKSIRKDKIKDE-QDLLhirREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd05045   7 TLGEGEFGKVVKatAFRLKGRagytTVAVKMLKENASSSElRDLL---SEFNLLKQVNHPHVIKLYGACSQDGPLLLIVE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPR------------------------LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDAN 190
Cdd:cd05045  84 YAKYGSLRSFLRESRKvgpsylgsdgnrnssyldnpderaLTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 191 GNIKIADFGLS-NLYHKGKFLQTFCGS-PL-YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQI 266
Cdd:cd05045 164 RKMKISDFGLSrDVYEEDSYVKRSKGRiPVkWMAIESLFDHIYT-TQSDVWSFGVLLWeIVTLGGNPYPGIAPERLFNLL 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 27229182 267 SNGAYREPPkpsDACGLIRWLLMVN-----PTRRATLEDVAS 303
Cdd:cd05045 243 KTGYRMERP---ENCSEEMYNLMLTcwkqePDKRPTFADISK 281
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
63-301 2.62e-18

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: 85.64  E-value: 2.62e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR-ESSGRLVAIKSIRKDkikDEQDLLHIRREIEIMSSLN-HPHIIAI--------HEVFENSSKIVIV 132
Cdd:cd14036   8 IAEGGFAFVYEAQdVGTGKEYALKRLLSN---EEEKNKAIIQEINFMKKLSgHPNIVQFcsaasigkEESDQGQAEYLLL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYAsRGDLYDYISE---RPRLSERDARHFFRQIVSALHYCHQNG--IVHRDLKLENILLDANGNIKIADFGLSN---LY 204
Cdd:cd14036  85 TELC-KGQLVDFVKKveaPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATteaHY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 205 -------HKGKFLQ---TFCGSPLYASPEIVN---GKPyVGPEVDSWSLGVLLYILVHGTMPFdgQDHKTLvkQISNGAY 271
Cdd:cd14036 164 pdyswsaQKRSLVEdeiTRNTTPMYRTPEMIDlysNYP-IGEKQDIWALGCILYLLCFRKHPF--EDGAKL--RIINAKY 238
                       250       260       270
                ....*....|....*....|....*....|...
gi 27229182 272 REPPKPSDAC---GLIRWLLMVNPTRRATLEDV 301
Cdd:cd14036 239 TIPPNDTQYTvfhDLIRSTLKVNPEERLSITEI 271
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
61-302 3.01e-18

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk 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: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 84.92  E-value: 3.01e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKArESSGRLVAIKSIRKDKIKdeQDLLHirrEIEIMSSLNHPHIIAIHEVFENSSkIVIVMEYASRGD 140
Cdd:cd05083  12 EIIGEGEFGAVLQG-EYMGQKVAVKNIKCDVTA--QAFLE---ETAVMTKLQHKNLVRLLGVILHNG-LYIVMELMSKGN 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 141 LYDYISERPR--LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFcgsPL 218
Cdd:cd05083  85 LVNFLRSRGRalVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVGSMGVDNSRL---PV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 219 -YASPEIVNGKPYvGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAYREPPK--PSDACGLIRWLLMVNPTR 294
Cdd:cd05083 162 kWTAPEALKNKKF-SSKSDVWSYGVLLWeVFSYGRAPYPKMSVKEVKEAVEKGYRMEPPEgcPPDVYSIMTSCWEAEPGK 240

                ....*...
gi 27229182 295 RATLEDVA 302
Cdd:cd05083 241 RPSFKKLR 248
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
63-303 4.31e-18

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: 84.74  E-value: 4.31e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLlhirREIEIMSSLNHPHIIAIHEVFeNSSKIVIVMEYASRGDLY 142
Cdd:cd05069  20 LGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPEAFL----QEAQIMKKLRHDKLVPLYAVV-SEEPIYIVTEFMGKGSLL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 143 DYISE-------RPRLSERDArhffrQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFL-QTFC 214
Cdd:cd05069  95 DFLKEgdgkylkLPQLVDMAA-----QIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTaRQGA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 215 GSPL-YASPE-IVNGKPYVgpEVDSWSLGVLLYILV-HGTMPFDGQDHKTLVKQISNGaYREP-PK--PSDACGLIRWLL 288
Cdd:cd05069 170 KFPIkWTAPEaALYGRFTI--KSDVWSFGILLTELVtKGRVPYPGMVNREVLEQVERG-YRMPcPQgcPESLHELMKLCW 246
                       250
                ....*....|....*
gi 27229182 289 MVNPTRRATLEDVAS 303
Cdd:cd05069 247 KKDPDERPTFEYIQS 261
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
51-276 4.94e-18

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


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 85.09  E-value: 4.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  51 HNLRHRYEFLETLGKGTYGKVKKAR------ESSGRLVAIKSIRKDKIKDEQDLlhiRREIEIMSSLNHPHIIAIHEVFE 124
Cdd:cd05093   1 HIKRHNIVLKRELGEGAFGKVFLAEcynlcpEQDKILVAVKTLKDASDNARKDF---HREAELLTNLQHEHIVKFYGVCV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 125 NSSKIVIVMEYASRGDLYDYI-------------SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANG 191
Cdd:cd05093  78 EGDPLIMVFEYMKHGDLNKFLrahgpdavlmaegNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 192 NIKIADFGLSNLYHKGKFLQTFCGSPL---YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQIS 267
Cdd:cd05093 158 LVKIGDFGMSRDVYSTDYYRVGGHTMLpirWMPPESIMYRKFT-TESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECIT 236

                ....*....
gi 27229182 268 NGAYREPPK 276
Cdd:cd05093 237 QGRVLQRPR 245
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
56-259 5.09e-18

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 86.24  E-value: 5.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARESS-GRLVAIKSIRKdKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVF------ENSSK 128
Cdd:cd07876  22 RYQQLKPIGSGAQGIVCAAFDTVlGINVAVKKLSR-PFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFtpqkslEEFQD 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IVIVMEYASrGDLYDYIseRPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGK 208
Cdd:cd07876 101 VYLVMELMD-ANLCQVI--HMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNF 177
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 27229182 209 FLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDH 259
Cdd:cd07876 178 MMTPYVVTRYYRAPEVILGMGY-KENVDIWSVGCIMGELVKGSVIFQGTDH 227
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
56-311 5.17e-18

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: 85.91  E-value: 5.17e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARESS-GRLVAIKSIRKdKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVF------ENSSK 128
Cdd:cd07874  18 RYQNLKPIGSGAQGIVCAAYDAVlDRNVAIKKLSR-PFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFtpqkslEEFQD 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IVIVMEYASrGDLYDYIseRPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGK 208
Cdd:cd07874  97 VYLVMELMD-ANLCQVI--QMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSF 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 209 FLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDH-------------------KTLVKQISNG 269
Cdd:cd07874 174 MMTPYVVTRYYRAPEVILGMGY-KENVDIWSVGCIMGEMVRHKILFPGRDYidqwnkvieqlgtpcpefmKKLQPTVRNY 252
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27229182 270 AYREPP------------------------KPSDACGLIRWLLMVNPTRRATLEDVASHWWVNWGY 311
Cdd:cd07874 253 VENRPKyagltfpklfpdslfpadsehnklKASQARDLLSKMLVIDPAKRISVDEALQHPYINVWY 318
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
54-301 5.77e-18

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: 85.06  E-value: 5.77e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKA------RESSGRL--VAIKSIRKDKikDEQDLLHIRREIEIMSSL-NHPHIIAIHEVFE 124
Cdd:cd05098  12 RDRLVLGKPLGEGCFGQVVLAeaigldKDKPNRVtkVAVKMLKSDA--TEKDLSDLISEMEMMKMIgKHKNIINLLGACT 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 125 NSSKIVIVMEYASRGDLYDYI-SERP---------------RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLD 188
Cdd:cd05098  90 QDGPLYVIVEYASKGNLREYLqARRPpgmeycynpshnpeeQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 189 ANGNIKIADFGLS-NLYHKGKFLQTFCGS-PL-YASPEIVNGKPYVGpEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVK 264
Cdd:cd05098 170 EDNVMKIADFGLArDIHHIDYYKKTTNGRlPVkWMAPEALFDRIYTH-QSDVWSFGVLLWeIFTLGGSPYPGVPVEELFK 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 27229182 265 QISNGAYREppKPSDaCGLIRWLLMVN-----PTRRATLEDV 301
Cdd:cd05098 249 LLKEGHRMD--KPSN-CTNELYMMMRDcwhavPSQRPTFKQL 287
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
63-297 5.81e-18

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: 83.85  E-value: 5.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKArESSGRLVAIKSIRKdkikdEQDLLHIRREIEIMSSLNHPHIIAIheVFENSSKIVIVMEYASRGDL- 141
Cdd:cd14068   2 LGDGGFGSVYRA-VYRGEDVAVKIFNK-----HTSFRLLRQELVVLSHLHHPSLVAL--LAAGTAPRMLVMELAPKGSLd 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 142 ----YDYISERPRLSERDARHffrqIVSALHYCHQNGIVHRDLKLENILL-----DANGNIKIADFGLSNlYHKGKFLQT 212
Cdd:cd14068  74 allqQDNASLTRTLQHRIALH----VADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQ-YCCRMGIKT 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISngAYREPPKPSDACG--------- 282
Cdd:cd14068 149 SEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYdILTCGERIVEGLKFPNEFDELA--IQGKLPDPVKEYGcapwpgvea 226
                       250
                ....*....|....*
gi 27229182 283 LIRWLLMVNPTRRAT 297
Cdd:cd14068 227 LIKDCLKENPQCRPT 241
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
63-289 6.34e-18

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA 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: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 84.15  E-value: 6.34e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVkkareSSGRL---------VAIKSIRKDKI-KDEQDLLhirREIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:cd05066  12 IGAGEFGEV-----CSGRLklpgkreipVAIKTLKAGYTeKQRRDFL---SEASIMGQFDHPNIIHLEGVVTRSKPVMIV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 133 MEYASRGDLYDYiserprLSERDARH-------FFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYH 205
Cdd:cd05066  84 TEYMENGSLDAF------LRKHDGQFtviqlvgMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 206 ---KGKFLQTFCGSPL-YASPEIVNGKPYVGPEvDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGaYREPPkPSDA 280
Cdd:cd05066 158 ddpEAAYTTRGGKIPIrWTAPEAIAYRKFTSAS-DVWSYGIVMWeVMSYGERPYWEMSNQDVIKAIEEG-YRLPA-PMDC 234

                ....*....
gi 27229182 281 CGLIRWLLM 289
Cdd:cd05066 235 PAALHQLML 243
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
56-266 6.39e-18

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: 85.34  E-value: 6.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKdKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSS------K 128
Cdd:cd07879  16 RYTSLKQVGSGAYGSVCSAiDKRTGEKVAIKKLSR-PFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVsgdefqD 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IVIVMEYAsRGDLYDYISERprLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNlyHKGK 208
Cdd:cd07879  95 FYLVMPYM-QTDLQKIMGHP--LSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLAR--HADA 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27229182 209 FLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQI 266
Cdd:cd07879 170 EMTGYVVTRWYRAPEVILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQI 227
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
61-291 6.48e-18

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 84.15  E-value: 6.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKAR-ESSGR---LVAIKSIrKDKIKDEQ--DLLhirREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd05065  10 EVIGAGEFGEVCRGRlKLPGKreiFVAIKTL-KSGYTEKQrrDFL---SEASIMGQFDHPNIIHLEGVVTKSRPVMIITE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERP-RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSnlyhkgKFLQTF 213
Cdd:cd05065  86 FMENGALDSFLRQNDgQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLS------RFLEDD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CGSPLYAS------------PEIVNGKPYVGPEvDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGaYREPPKPSda 280
Cdd:cd05065 160 TSDPTYTSslggkipirwtaPEAIAYRKFTSAS-DVWSYGIVMWeVMSYGERPYWDMSNQDVINAIEQD-YRLPPPMD-- 235
                       250
                ....*....|.
gi 27229182 281 CGLIRWLLMVN 291
Cdd:cd05065 236 CPTALHQLMLD 246
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
59-301 6.66e-18

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: 84.29  E-value: 6.66e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  59 FLETLGKGTYGKVKKAR-----ESSGRLVAIKSIRKdkIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd05090   9 FMEELGECAFGKIYKGHlylpgMDHAQLVAIKTLKD--YNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYISERP-----------------RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIA 196
Cdd:cd05090  87 EFMNQGDLHEFLIMRSphsdvgcssdedgtvksSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKIS 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 197 DFGLSNLYHKGKF--LQTFCGSPL-YASPE-IVNGKpyVGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAY 271
Cdd:cd05090 167 DLGLSREIYSSDYyrVQNKSLLPIrWMPPEaIMYGK--FSSDSDIWSFGVVLWeIFSFGLQPYYGFSNQEVIEMVRKRQL 244
                       250       260       270
                ....*....|....*....|....*....|..
gi 27229182 272 REPPK--PSDACGLIRWLLMVNPTRRATLEDV 301
Cdd:cd05090 245 LPCSEdcPPRMYSLMTECWQEIPSRRPRFKDI 276
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
54-299 6.74e-18

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: 84.35  E-value: 6.74e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLlhirREIEIMSSLNHPHIIAIHEVFeNSSKIVIVM 133
Cdd:cd05070   8 RESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFL----EEAQIMKKLKHDKLVQLYAVV-SEEPIYIVT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYISE-------RPRLSERDArhffrQIVSALHYCHQNGIVHRDLKLENILLdANGNI-KIADFGLSNLYH 205
Cdd:cd05070  83 EYMSKGSLLDFLKDgegralkLPNLVDMAA-----QVAAGMAYIERMNYIHRDLRSANILV-GNGLIcKIADFGLARLIE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 206 KGKFL-QTFCGSPL-YASPE-IVNGKPYVgpEVDSWSLGVLLYILV-HGTMPFDGQDHKTLVKQISNGaYREPPkPSDaC 281
Cdd:cd05070 157 DNEYTaRQGAKFPIkWTAPEaALYGRFTI--KSDVWSFGILLTELVtKGRVPYPGMNNREVLEQVERG-YRMPC-PQD-C 231
                       250       260
                ....*....|....*....|...
gi 27229182 282 GLIRWLLMV-----NPTRRATLE 299
Cdd:cd05070 232 PISLHELMIhcwkkDPEERPTFE 254
pknD PRK13184
serine/threonine-protein kinase PknD;
56-275 7.77e-18

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 87.90  E-value: 7.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   56 RYEFLETLGKGTYGKVKKARESS-GRLVAIKSIRKDKIKDEqdLLHIR--REIEIMSSLNHPHIIAIHEVFENSSKIVIV 132
Cdd:PRK13184   3 RYDIIRLIGKGGMGEVYLAYDPVcSRRVALKKIREDLSENP--LLKKRflREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  133 MEYA---SRGDLYDYISERPRLSERDARH--------FFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL- 200
Cdd:PRK13184  81 MPYIegyTLKSLLKSVWQKESLSKELAEKtsvgaflsIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAa 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  201 ----------------------SNLYHKGKFLqtfcGSPLYASPEIVNGKPyVGPEVDSWSLGVLLYILVHGTMPFDGQD 258
Cdd:PRK13184 161 ifkkleeedlldidvdernicySSMTIPGKIV----GTPDYMAPERLLGVP-ASESTDIYALGVILYQMLTLSFPYRRKK 235
                        250       260
                 ....*....|....*....|...
gi 27229182  259 HKTLV--KQISN----GAYREPP 275
Cdd:PRK13184 236 GRKISyrDVILSpievAPYREIP 258
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
63-304 9.08e-18

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: 85.57  E-value: 9.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYG---KVKKAResSGRLVAIKSIrkdkIKDEQDLLHIRR---EIEIMSSLNH------------PHIIAIHEVFe 124
Cdd:cd07853   8 IGYGAFGvvwSVTDPR--DGKRVALKKM----PNVFQNLVSCKRvfrELKMLCFFKHdnvlsaldilqpPHIDPFEEIY- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 125 nsskiviVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLY 204
Cdd:cd07853  81 -------VVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 205 H--KGKFLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISN-------------- 268
Cdd:cd07853 154 EpdESKHMTQEVVTQYYRAPEILMGSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDllgtpsleamrsac 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27229182 269 -GA----YREPPKPSD--------------ACGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd07853 234 eGArahiLRGPHKPPSlpvlytlssqatheAVHLLCRMLVFDPDKRISAADALAH 288
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
56-256 9.68e-18

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: 83.66  E-value: 9.68e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARE-SSGRLVAIKsIRKDKIKDEQdllhIRREIEIMSSLN-HPHIIAIHEVFENSSKIVIVM 133
Cdd:cd14016   1 RYKLVKKIGSGSFGEVYLGIDlKTGEEVAIK-IEKKDSKHPQ----LEYEAKVYKLLQgGPGIPRLYWFGQEGDYNVMVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRgDLYDYISERPR---------LSErdarhffrQIVSALHYCHQNGIVHRDLKLENILLDANGNIK---IADFGLS 201
Cdd:cd14016  76 DLLGP-SLEDLFNKCGRkfslktvlmLAD--------QMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGLA 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27229182 202 NLY-------H----KGKflqTFCGSPLYASpeiVN---GKpyvgpeVDSW-----SLG-VLLYiLVHGTMPFDG 256
Cdd:cd14016 147 KKYrdprtgkHipyrEGK---SLTGTARYAS---INahlGI------EQSRrddleSLGyVLIY-FLKGSLPWQG 208
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
63-304 1.05e-17

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: 83.59  E-value: 1.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSK----IVIVMEYASR 138
Cdd:cd14032   9 LGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrcIVLVTELMTS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISERPRLSERDARHFFRQIVSALHYCHQNG--IVHRDLKLENILLDA-NGNIKIADFGLSNLyHKGKFLQTFCG 215
Cdd:cd14032  89 GTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLATL-KRASFAKSVIG 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 216 SPLYASPEIVngKPYVGPEVDSWSLGVLLYILVHGTMPF-DGQDHKTLVKQISNG---AYREPPKPSDACGLIRWLLMVN 291
Cdd:cd14032 168 TPEFMAPEMY--EEHYDESVDVYAFGMCMLEMATSEYPYsECQNAAQIYRKVTCGikpASFEKVTDPEIKEIIGECICKN 245
                       250
                ....*....|...
gi 27229182 292 PTRRATLEDVASH 304
Cdd:cd14032 246 KEERYEIKDLLSH 258
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
54-245 1.07e-17

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 84.27  E-value: 1.07e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVK----------KARE-----SSGR--LVAIKSIRKDKIKDEQ-DLLhirREIEIMSSLNHPH 115
Cdd:cd05095   4 RKLLTFKEKLGEGQFGEVHlceaegmekfMDKDfalevSENQpvLVAVKMLRADANKNARnDFL---KEIKIMSRLKDPN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 116 IIAIHEVFENSSKIVIVMEYASRGDLYDYIS-ERPR-----------LSERDARHFFRQIVSALHYCHQNGIVHRDLKLE 183
Cdd:cd05095  81 IIRLLAVCITDDPLCMITEYMENGDLNQFLSrQQPEgqlalpsnaltVSYSDLRFMAAQIASGMKYLSSLNFVHRDLATR 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27229182 184 NILLDANGNIKIADFGLS-NLYHKGKF-LQTFCGSPL-YASPE-IVNGKPYVGPEVdsWSLGVLLY 245
Cdd:cd05095 161 NCLVGKNYTIKIADFGMSrNLYSGDYYrIQGRAVLPIrWMSWEsILLGKFTTASDV--WAFGVTLW 224
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
57-262 1.15e-17

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: 84.72  E-value: 1.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLlHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYA 136
Cdd:cd06649   7 FERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRN-QIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 137 SRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQ-NGIVHRDLKLENILLDANGNIKIADFGLSNLYHKgKFLQTFCG 215
Cdd:cd06649  86 DGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREkHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID-SMANSFVG 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 27229182 216 SPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTL 262
Cdd:cd06649 165 TRSYMSPERLQGTHY-SVQSDIWSMGLSLVELAIGRYPIPPPDAKEL 210
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
54-256 1.65e-17

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: 83.69  E-value: 1.65e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKA------RESSGRLVAIKSIRKDKIKDEQDLLhiRREIEIMSSL-NHPHIIAIHEVFENS 126
Cdd:cd05055  34 RNNLSFGKTLGAGAFGKVVEAtayglsKSDAVMKVAVKMLKPTAHSSEREAL--MSELKIMSHLgNHENIVNLLGACTIG 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 127 SKIVIVMEYASRGDLYDYISERPR--LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL---- 200
Cdd:cd05055 112 GPILVITEYCCYGDLLNFLRRKREsfLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLardi 191
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27229182 201 ---SNLYHKGK-FLqtfcgsPL-YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDG 256
Cdd:cd05055 192 mndSNYVVKGNaRL------PVkWMAPESIFNCVYT-FESDVWSYGILLWeIFSLGSNPYPG 246
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
58-279 1.82e-17

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 83.51  E-value: 1.82e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  58 EFLETLGKGTYGKVKKA---RESSGRLVAIKSIRKdkIKDEQDLLHIRREIEIMSSL-NHPHIIAIHEVFENSSKIVIVM 133
Cdd:cd05089   5 KFEDVIGEGNFGQVIKAmikKDGLKMNAAIKMLKE--FASENDHRDFAGELEVLCKLgHHPNIINLLGACENRGYLYIAI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYISER----------------PRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIAD 197
Cdd:cd05089  83 EYAPYGNLLDFLRKSrvletdpafakehgtaSTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIAD 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 198 FGLS---NLYHKgkflQTFCGSPL-YASPEIVNGKPYVgPEVDSWSLGVLLYILVH-GTMPFDGQDHKTLVKQISNGAYR 272
Cdd:cd05089 163 FGLSrgeEVYVK----KTMGRLPVrWMAIESLNYSVYT-TKSDVWSFGVLLWEIVSlGGTPYCGMTCAELYEKLPQGYRM 237

                ....*..
gi 27229182 273 EPPKPSD 279
Cdd:cd05089 238 EKPRNCD 244
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
63-304 2.06e-17

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 82.85  E-value: 2.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSK----IVIVMEYASR 138
Cdd:cd14031  18 LGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESVLKgkkcIVLVTELMTS 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISERPRLSERDARHFFRQIVSALHYCHQNG--IVHRDLKLENILLDA-NGNIKIADFGLSNLYhKGKFLQTFCG 215
Cdd:cd14031  98 GTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLATLM-RTSFAKSVIG 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 216 SPLYASPEIVngKPYVGPEVDSWSLGVLLYILVHGTMPF-DGQDHKTLVKQISNG----AYREPPKPsDACGLIRWLLMV 290
Cdd:cd14031 177 TPEFMAPEMY--EEHYDESVDVYAFGMCMLEMATSEYPYsECQNAAQIYRKVTSGikpaSFNKVTDP-EVKEIIEGCIRQ 253
                       250
                ....*....|....
gi 27229182 291 NPTRRATLEDVASH 304
Cdd:cd14031 254 NKSERLSIKDLLNH 267
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
56-259 2.12e-17

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: 84.33  E-value: 2.12e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  56 RYEFLETLGKGTYGKVKKARESS-GRLVAIKSIRKdKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVF------ENSSK 128
Cdd:cd07875  25 RYQNLKPIGSGAQGIVCAAYDAIlERNVAIKKLSR-PFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFtpqkslEEFQD 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 129 IVIVMEYASrGDLYDYIseRPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGK 208
Cdd:cd07875 104 VYIVMELMD-ANLCQVI--QMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSF 180
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 27229182 209 FLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDH 259
Cdd:cd07875 181 MMTPYVVTRYYRAPEVILGMGY-KENVDIWSVGCIMGEMIKGGVLFPGTDH 230
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
54-204 2.33e-17

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 83.06  E-value: 2.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVK-----------------KARESSGRLVAIKSIRKDKIKDEQ-DLLhirREIEIMSSLNHPH 115
Cdd:cd05096   4 RGHLLFKEKLGEGQFGEVHlcevvnpqdlptlqfpfNVRKGRPLLVAVKILRPDANKNARnDFL---KEVKILSRLKDPN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 116 IIAIHEVFENSSKIVIVMEYASRGDLYDYISER-------------------PRLSERDARHFFRQIVSALHYCHQNGIV 176
Cdd:cd05096  81 IIRLLGVCVDEDPLCMITEYMENGDLNQFLSSHhlddkeengndavppahclPAISYSSLLHVALQIASGMKYLSSLNFV 160
                       170       180
                ....*....|....*....|....*....
gi 27229182 177 HRDLKLENILLDANGNIKIADFGLS-NLY 204
Cdd:cd05096 161 HRDLATRNCLVGENLTIKIADFGMSrNLY 189
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
104-245 3.60e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 84.56  E-value: 3.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  104 EIEIMSSLNHPHIIAIHEVFENSSKIVIVM-EYasRGDLYDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLK 181
Cdd:PHA03211 210 EARLLRRLSHPAVLALLDVRVVGGLTCLVLpKY--RSDLYTYLGARLRpLGLAQVTAVARQLLSAIDYIHGEGIIHRDIK 287
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27229182  182 LENILLDANGNIKIADFGLSNlyhkgkFLQTFCGSPLY---------ASPEIVNGKPYVgPEVDSWSLGVLLY 245
Cdd:PHA03211 288 TENVLVNGPEDICLGDFGAAC------FARGSWSTPFHygiagtvdtNAPEVLAGDPYT-PSVDIWSAGLVIF 353
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
57-257 3.62e-17

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 84.32  E-value: 3.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   57 YEFLETLGKGTYGKVKKA--RESSGRlVAIKSIRkdkikdeQDLLHIRREIEIMSSLNHPHIIAIH-----EVFENSSKI 129
Cdd:PTZ00036  68 YKLGNIIGNGSFGVVYEAicIDTSEK-VAIKKVL-------QDPQYKNRELLIMKNLNHINIIFLKdyyytECFKKNEKN 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  130 V---IVMEYASRgDLYDYISERPR----LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN-IKIADFGLS 201
Cdd:PTZ00036 140 IflnVVMEFIPQ-TVHKYMKHYARnnhaLPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGSA 218
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 27229182  202 NLYHKGKFLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQ 257
Cdd:PTZ00036 219 KNLLAGQRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQ 274
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
104-304 4.06e-17

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: 81.59  E-value: 4.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 104 EIEIMSSLNHPHIIAIHEVFENSSK----IVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNG--IVH 177
Cdd:cd14033  50 EVEMLKGLQHPNIVRFYDSWKSTVRghkcIILVTELMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCppILH 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 178 RDLKLENILLDA-NGNIKIADFGLSNLyHKGKFLQTFCGSPLYASPEIVNGKpyVGPEVDSWSLGVLLYILVHGTMPF-D 255
Cdd:cd14033 130 RDLKCDNIFITGpTGSVKIGDLGLATL-KRASFAKSVIGTPEFMAPEMYEEK--YDEAVDVYAFGMCILEMATSEYPYsE 206
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 27229182 256 GQDHKTLVKQISNGayREPP-----KPSDACGLIRWLLMVNPTRRATLEDVASH 304
Cdd:cd14033 207 CQNAAQIYRKVTSG--IKPDsfykvKVPELKEIIEGCIRTDKDERFTIQDLLEH 258
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
63-301 5.11e-17

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 81.98  E-value: 5.11e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKAR------ESSGRLVAIKSIRKDKIKDEQDLlhiRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYA 136
Cdd:cd05094  13 LGEGAFGKVFLAEcynlspTKDKMLVAVKTLKDPTLAARKDF---QREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEYM 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 137 SRGDLYDY-----------ISERPRLSERD-----ARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL 200
Cdd:cd05094  90 KHGDLNKFlrahgpdamilVDGQPRQAKGElglsqMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDFGM 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 201 SNLYHKGKFLQTFCGSPL---YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAYREPPK 276
Cdd:cd05094 170 SRDVYSTDYYRVGGHTMLpirWMPPESIMYRKFT-TESDVWSFGVILWeIFTYGKQPWFQLSNTEVIECITQGRVLERPR 248
                       250       260
                ....*....|....*....|....*..
gi 27229182 277 --PSDACGLIRWLLMVNPTRRATLEDV 301
Cdd:cd05094 249 vcPKEVYDIMLGCWQREPQQRLNIKEI 275
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
63-249 5.97e-17

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: 81.48  E-value: 5.97e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKV-----KKARESSGRLVAIKSIRKDKikDEQDLLHIRREIEIMSSLNHPHIIAIHEVF-ENSSKIV-IVMEY 135
Cdd:cd05080  12 LGEGHFGKVslycyDPTNDGTGEMVAVKALKADC--GPQHRSGWKQEIDILKTLYHENIVKYKGCCsEQGGKSLqLIMEY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISeRPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKF---LQT 212
Cdd:cd05080  90 VPLGSLRDYLP-KHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEGHEyyrVRE 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPL--YASPEIVNGKPYVGPEVdsWSLGVLLY-ILVH 249
Cdd:cd05080 169 DGDSPVfwYAPECLKEYKFYYASDV--WSFGVTLYeLLTH 206
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
61-303 6.61e-17

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: 81.00  E-value: 6.61e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARESSGRL-VAIKSIRKDKIKDEQDLlhiRREIEIMSSL-NHPHIIAIH-EVFE------NSSKIVI 131
Cdd:cd13975   6 RELGRGQYGVVYACDSWGGHFpCALKSVVPPDDKHWNDL---ALEFHYTRSLpKHERIVSLHgSVIDysygggSSIAVLL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRgDLYDYIseRPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNlyHKGKFLQ 211
Cdd:cd13975  83 IMERLHR-DLYTGI--KAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCK--PEAMMSG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPLYASPEIVNGKpyVGPEVDSWSLGVLLYILVHG--TMP-----FDGQDHktLVKQISNGAYREP-PKPSDACgl 283
Cdd:cd13975 158 SIVGTPIHMAPELFSGK--YDNSVDVYAFGILFWYLCAGhvKLPeafeqCASKDH--LWNNVRKGVRPERlPVFDEEC-- 231
                       250       260
                ....*....|....*....|....*
gi 27229182 284 irWLLMV-----NPTRRATLEDVAS 303
Cdd:cd13975 232 --WNLMEacwsgDPSQRPLLGIVQP 254
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
54-275 6.73e-17

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: 81.99  E-value: 6.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKV--------KKARESSGRLVAIKSIRKDKIkdEQDLLHIRREIEIMSSL-NHPHIIAIHEVFE 124
Cdd:cd05101  23 RDKLTLGKPLGEGCFGQVvmaeavgiDKDKPKEAVTVAVKMLKDDAT--EKDLSDLVSEMEMMKMIgKHKNIINLLGACT 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 125 NSSKIVIVMEYASRGDLYDYI-SERP----------RLSE-----RDARHFFRQIVSALHYCHQNGIVHRDLKLENILLD 188
Cdd:cd05101 101 QDGPLYVIVEYASKGNLREYLrARRPpgmeysydinRVPEeqmtfKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVT 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 189 ANGNIKIADFGLSNLYHKGKFLQTFCGSPL---YASPEIVNGKPYVGpEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVK 264
Cdd:cd05101 181 ENNVMKIADFGLARDINNIDYYKKTTNGRLpvkWMAPEALFDRVYTH-QSDVWSFGVLMWeIFTLGGSPYPGIPVEELFK 259
                       250
                ....*....|.
gi 27229182 265 QISNGAYREPP 275
Cdd:cd05101 260 LLKEGHRMDKP 270
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
63-244 6.91e-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: 82.04  E-value: 6.91e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSGR---LVAIKSIRKDKIKdeqdlLHIRREIEIMSSLNHPHIIAIHEVFENSS--KIVIVMEYAS 137
Cdd:cd07867  10 VGRGTYGHVYKAKRKDGKdekEYALKQIEGTGIS-----MSACREIALLRELKHPNVIALQKVFLSHSdrKVWLLFDYAE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 138 RgDLYDYI--------SERP-RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL----DANGNIKIADFGLSNLY 204
Cdd:cd07867  85 H-DLWHIIkfhraskaNKKPmQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLF 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 27229182 205 HKG----KFLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLL 244
Cdd:cd07867 164 NSPlkplADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIF 207
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
63-277 1.19e-16

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: 80.50  E-value: 1.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLlhirREIEIMSSLNHPHIIAIHEVFeNSSKIVIVMEYASRGDLY 142
Cdd:cd05071  17 LGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFL----QEAQVMKKLRHEKLVQLYAVV-SEEPIYIVTEYMSKGSLL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 143 DYISER-------PRLSErdarhFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFL-QTFC 214
Cdd:cd05071  92 DFLKGEmgkylrlPQLVD-----MAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTaRQGA 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27229182 215 GSPL-YASPE-IVNGKPYVgpEVDSWSLGVLLYIL-VHGTMPFDGQDHKTLVKQISNGaYREPPKP 277
Cdd:cd05071 167 KFPIkWTAPEaALYGRFTI--KSDVWSFGILLTELtTKGRVPYPGMVNREVLDQVERG-YRMPCPP 229
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
60-242 1.23e-16

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: 81.25  E-value: 1.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  60 LETLGKGTYGKVKKARES-SGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY--A 136
Cdd:cd06635  30 LREIGHGSFGAVYFARDVrTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYclG 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 137 SRGDLYDyISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGkflQTFCGS 216
Cdd:cd06635 110 SASDLLE-VHKKP-LQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPA---NSFVGT 184
                       170       180
                ....*....|....*....|....*....
gi 27229182 217 PLYASPEIV---NGKPYVGpEVDSWSLGV 242
Cdd:cd06635 185 PYWMAPEVIlamDEGQYDG-KVDVWSLGI 212
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
63-275 1.28e-16

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


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 80.38  E-value: 1.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKA---RESSGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSkIVIVMEYASRG 139
Cdd:cd05115  12 LGSGNFGCVKKGvykMRKKQIDVAIKVLKQGNEKAVRD--EMMREAQIMHQLDNPYIVRMIGVCEAEA-LMLVMEMASGG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYIS-ERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS------NLYHKGKflqT 212
Cdd:cd05115  89 PLNKFLSgKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSkalgadDSYYKAR---S 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27229182 213 FCGSPL-YASPEIVNGKPYvGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAYREPP 275
Cdd:cd05115 166 AGKWPLkWYAPECINFRKF-SSRSDVWSYGVTMWeAFSYGQKPYKKMKGPEVMSFIEQGKRMDCP 229
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
61-228 1.41e-16

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 80.39  E-value: 1.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKAReSSGRLVAIKSIRKdkiKDEQDLLHirrEIEIMSS--LNHPHI---IAIHEVFENSS-KIVIVME 134
Cdd:cd14056   1 KTIGKGRYGEVWLGK-YRGEKVAVKIFSS---RDEDSWFR---ETEIYQTvmLRHENIlgfIAADIKSTGSWtQLWLITE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISERPrLSERDARHFFRQIVSALHYCH--------QNGIVHRDLKLENILLDANGNIKIADFGLSNLYHK 206
Cdd:cd14056  74 YHEHGSLYDYLQRNT-LDTEEALRLAYSAASGLAHLHteivgtqgKPAIAHRDLKSKNILVKRDGTCCIADLGLAVRYDS 152
                       170       180
                ....*....|....*....|....*..
gi 27229182 207 GKFL-----QTFCGSPLYASPEIVNGK 228
Cdd:cd14056 153 DTNTidippNPRVGTKRYMAPEVLDDS 179
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
60-242 1.50e-16

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: 80.84  E-value: 1.50e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  60 LETLGKGTYGKVKKARE-SSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY--A 136
Cdd:cd06634  20 LREIGHGSFGAVYFARDvRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEYclG 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 137 SRGDLYDyISERPrLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGkflQTFCGS 216
Cdd:cd06634 100 SASDLLE-VHKKP-LQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAPA---NSFVGT 174
                       170       180
                ....*....|....*....|....*....
gi 27229182 217 PLYASPEIV---NGKPYVGpEVDSWSLGV 242
Cdd:cd06634 175 PYWMAPEVIlamDEGQYDG-KVDVWSLGI 202
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
63-255 1.53e-16

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: 80.24  E-value: 1.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSGRLVAIKSIRK--DKIKDEQDLLhirREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGD 140
Cdd:cd14027   1 LDSGGFGKVSLCFHRTQGLVVLKTVYTgpNCIEHNEALL---EEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 141 LYDYISERPRLSERDARhFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGL--SNLYHK------------ 206
Cdd:cd14027  78 LMHVLKKVSVPLSVKGR-IILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLasFKMWSKltkeehneqrev 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 27229182 207 GKFLQTFCGSPLYASPE---IVNGKPyvGPEVDSWSLGVLLYILVHGTMPFD 255
Cdd:cd14027 157 DGTAKKNAGTLYYMAPEhlnDVNAKP--TEKSDVYSFAIVLWAIFANKEPYE 206
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
61-289 1.56e-16

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


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 80.02  E-value: 1.56e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKAR-ESSGR---LVAIKSIRKDKI-KDEQDLLhirREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd05063  11 KVIGAGEFGEVFRGIlKMPGRkevAVAIKTLKPGYTeKQRQDFL---SEASIMGQFSHHNIIRLEGVVTKFKPAMIITEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERP-RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYH---KGKFLQ 211
Cdd:cd05063  88 MENGALDKYLRDHDgEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEddpEGTYTT 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 212 TFCGSPL-YASPEIVNGKPYVGPEvDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQIsNGAYRePPKPSDACGLIRWLLM 289
Cdd:cd05063 168 SGGKIPIrWTAPEAIAYRKFTSAS-DVWSFGIVMWeVMSFGERPYWDMSNHEVMKAI-NDGFR-LPAPMDCPSAVYQLML 244
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
55-269 2.95e-16

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 82.86  E-value: 2.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182    55 HRYEFLETLGKGTYGKV-----KKAREssgrLVAIKSIRKDKIKdEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSS-- 127
Cdd:PTZ00266   13 NEYEVIKKIGNGRFGEVflvkhKRTQE----FFCWKAISYRGLK-EREKSQLVIEVNVMRELKHKNIVRYIDRFLNKAnq 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   128 KIVIVMEYASRGDLYDYISERPRLSERDARH----FFRQIVSALHYCHQ-----NG--IVHRDLKLENILL--------- 187
Cdd:PTZ00266   88 KLYILMEFCDAGDLSRNIQKCYKMFGKIEEHaivdITRQLLHALAYCHNlkdgpNGerVLHRDLKPQNIFLstgirhigk 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   188 ------DANGN--IKIADFGLSNLYHKGKFLQTFCGSPLYASPEIV--NGKPYvGPEVDSWSLGVLLYILVHGTMPF-DG 256
Cdd:PTZ00266  168 itaqanNLNGRpiAKIGDFGLSKNIGIESMAHSCVGTPYYWSPELLlhETKSY-DDKSDMWALGCIIYELCSGKTPFhKA 246
                         250
                  ....*....|...
gi 27229182   257 QDHKTLVKQISNG 269
Cdd:PTZ00266  247 NNFSQLISELKRG 259
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
52-267 3.28e-16

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: 80.52  E-value: 3.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  52 NLRHRYEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLLhirrEIEIMSSLNHP-----HIIAIHEVFEN 125
Cdd:cd14228  12 SMTNSYEVLEFLGRGTFGQVAKCwKRSTKEIVAIKILKNHPSYARQGQI----EVSILSRLSSEnadeyNFVRSYECFQH 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 126 SSKIVIVMEYASRgDLYDYISER--PRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL----DANGNIKIADFG 199
Cdd:cd14228  88 KNHTCLVFEMLEQ-NLYDFLKQNkfSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFG 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27229182 200 LSNLYHKGkFLQTFCGSPLYASPEIVNGKPYVgPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQIS 267
Cdd:cd14228 167 SASHVSKA-VCSTYLQSRYYRAPEIILGLPFC-EAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYIS 232
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
57-267 3.80e-16

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: 80.07  E-value: 3.80e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLLhirrEIEIMSSLNHPH-----IIAIHEVFENSSKIV 130
Cdd:cd14229   2 YEVLDFLGRGTFGQVVKCwKRGTNEIVAVKILKNHPSYARQGQI----EVGILARLSNENadefnFVRAYECFQHRNHTC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 IVMEYASRgDLYDYISER--PRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL----DANGNIKIADFGlSNLY 204
Cdd:cd14229  78 LVFEMLEQ-NLYDFLKQNkfSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFG-SASH 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27229182 205 HKGKFLQTFCGSPLYASPEIVNGKPYVgPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQIS 267
Cdd:cd14229 156 VSKTVCSTYLQSRYYRAPEIILGLPFC-EAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYIS 217
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
59-301 3.88e-16

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 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: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 78.88  E-value: 3.88e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  59 FLETLGKGTYGKVKKARESSG---RLVAIKSIRKDKikDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd05087   1 YLKEIGHGWFGKVFLGEVNSGlssTQVVVKELKASA--SVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYI---------SERPRLSERDARhffrQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHK 206
Cdd:cd05087  79 CPLGDLKGYLrscraaesmAPDPLTLQRMAC----EVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHCKYK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 207 GKFLQTF--CGSPL-YASPEI---VNGKPYVGPEVDS---WSLGVLLYILVH-GTMPFDG-QDHKTLVKQISNGAYREpP 275
Cdd:cd05087 155 EDYFVTAdqLWVPLrWIAPELvdeVHGNLLVVDQTKQsnvWSLGVTIWELFElGNQPYRHySDRQVLTYTVREQQLKL-P 233
                       250       260       270
                ....*....|....*....|....*....|..
gi 27229182 276 KPSDACGLI-RW-----LLMVNPTRRATLEDV 301
Cdd:cd05087 234 KPQLKLSLAeRWyevmqFCWLQPEQRPTAEEV 265
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
63-269 6.71e-16

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: 78.55  E-value: 6.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSK----IVIVMEYASR 138
Cdd:cd14030  33 IGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTVKgkkcIVLVTELMTS 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 139 GDLYDYISERPRLSERDARHFFRQIVSALHYCHQNG--IVHRDLKLENILLDA-NGNIKIADFGLSNLyHKGKFLQTFCG 215
Cdd:cd14030 113 GTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLATL-KRASFAKSVIG 191
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27229182 216 SPLYASPEIVNGKpyVGPEVDSWSLGVLLYILVHGTMPF-DGQDHKTLVKQISNG 269
Cdd:cd14030 192 TPEFMAPEMYEEK--YDESVDVYAFGMCMLEMATSEYPYsECQNAAQIYRRVTSG 244
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
54-275 6.99e-16

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: 79.29  E-value: 6.99e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKV--------KKARESSGRLVAIKSIRKDKIkdEQDLLHIRREIEIMSSL-NHPHIIAIHEVFE 124
Cdd:cd05100  11 RTRLTLGKPLGEGCFGQVvmaeaigiDKDKPNKPVTVAVKMLKDDAT--DKDLSDLVSEMEMMKMIgKHKNIINLLGACT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 125 NSSKIVIVMEYASRGDLYDYI-SERP---------------RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLD 188
Cdd:cd05100  89 QDGPLYVLVEYASKGNLREYLrARRPpgmdysfdtcklpeeQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 189 ANGNIKIADFGLSNLYHKGKFLQTFCGSPL---YASPEIVNGKPYVGpEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVK 264
Cdd:cd05100 169 EDNVMKIADFGLARDVHNIDYYKKTTNGRLpvkWMAPEALFDRVYTH-QSDVWSFGVLLWeIFTLGGSPYPGIPVEELFK 247
                       250
                ....*....|.
gi 27229182 265 QISNGAYREPP 275
Cdd:cd05100 248 LLKEGHRMDKP 258
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
63-291 1.65e-15

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 77.07  E-value: 1.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKK------ARESSGRL-VAIKSIRKDKIKDEQ-DLLhirREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd05044   3 LGSGAFGEVFEgtakdiLGDGSGETkVAVKTLRKGATDQEKaEFL---KEAHLMSNFKHPNILKLLGVCLDNDPQYIILE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYI-------SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGN----IKIADFGLSNL 203
Cdd:cd05044  80 LMEGGDLLSYLraarptaFTPPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDYrervVKIGDFGLARD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 204 YHKGKFLQTFcGSPL----YASPE-IVNGkpYVGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAYREPPkp 277
Cdd:cd05044 160 IYKNDYYRKE-GEGLlpvrWMAPEsLVDG--VFTTQSDVWAFGVLMWeILTLGQQPYPARNNLEVLHFVRAGGRLDQP-- 234
                       250
                ....*....|....
gi 27229182 278 sDACGLIRWLLMVN 291
Cdd:cd05044 235 -DNCPDDLYELMLR 247
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
52-267 2.02e-15

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: 78.21  E-value: 2.02e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  52 NLRHRYEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLLhirrEIEIMSSLNHP-----HIIAIHEVFEN 125
Cdd:cd14227  12 SMTNTYEVLEFLGRGTFGQVVKCwKRGTNEIVAIKILKNHPSYARQGQI----EVSILARLSTEsaddyNFVRAYECFQH 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 126 SSKIVIVMEYASRgDLYDYISER--PRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL-DANGN---IKIADFG 199
Cdd:cd14227  88 KNHTCLVFEMLEQ-NLYDFLKQNkfSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvDPSRQpyrVKVIDFG 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27229182 200 LSNLYHKGkFLQTFCGSPLYASPEIVNGKPYVgPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQIS 267
Cdd:cd14227 167 SASHVSKA-VCSTYLQSRYYRAPEIILGLPFC-EAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYIS 232
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
29-245 2.30e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 77.99  E-value: 2.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182   29 DGLIKSpkplmkKQAVKRHHHKHNlrhrYEFLETLGKGTYGKVKKA-RESSGRLVAIKSIRKDKIKDEQDLLHirreiei 107
Cdd:PHA03209  50 DGLIPT------KQKAREVVASLG----YTVIKTLTPGSEGRVFVAtKPGQPDPVVLKIGQKGTTLIEAMLLQ------- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  108 msSLNHPHIIAIHEVFENSSKIVIVMEYAsRGDLYDYISERPR-LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENIL 186
Cdd:PHA03209 113 --NVNHPSVIRMKDTLVSGAITCMVLPHY-SSDLYTYLTKRSRpLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIF 189
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 27229182  187 LDANGNIKIADFGLSNLYHKGKFLQTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLY 245
Cdd:PHA03209 190 INDVDQVCIGDLGAAQFPVVAPAFLGLAGTVETNAPEVLARDKY-NSKADIWSAGIVLF 247
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
63-269 2.33e-15

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 76.93  E-value: 2.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQD------LLHI------------RREIEIMSSLNHPHIIAIHEVfe 124
Cdd:cd14067   1 LGQGGSGTVIYRARYQGQPVAVKRFHIKKCKKRTDgsadtmLKHLraadamknfsefRQEASMLHSLQHPCIVYLIGI-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 125 NSSKIVIVMEYASRGDLYDYISERPR------LSERDARHFFRQIVSALHYCHQNGIVHRDLKLENIL---LDANG--NI 193
Cdd:cd14067  79 SIHPLCFALELAPLGSLNTVLEENHKgssfmpLGHMLTFKIAYQIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQEhiNI 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27229182 194 KIADFGLS-NLYHKGKFlqTFCGSPLYASPEIVNGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNG 269
Cdd:cd14067 159 KLSDYGISrQSFHEGAL--GVEGTPGYQAPEIRPRIVY-DEKVDMFSYGMVLYELLSGQRPSLGHHQLQIAKKLSKG 232
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
63-244 3.27e-15

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: 77.41  E-value: 3.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSGRL---VAIKSIRKDKIKdeqdlLHIRREIEIMSSLNHPHIIAIHEVFENSS--KIVIVMEYAS 137
Cdd:cd07868  25 VGRGTYGHVYKAKRKDGKDdkdYALKQIEGTGIS-----MSACREIALLRELKHPNVISLQKVFLSHAdrKVWLLFDYAE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 138 RgDLYDYI--------SERP-RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL----DANGNIKIADFGLSNLY 204
Cdd:cd07868 100 H-DLWHIIkfhraskaNKKPvQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLF 178
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 27229182 205 HKG----KFLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLL 244
Cdd:cd07868 179 NSPlkplADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIF 222
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
60-254 3.57e-15

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: 75.82  E-value: 3.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  60 LETLGKGTYGKVKKARESSGrlVAIKSIRKDKIKDEQdLLHIRREIEIMSSLNHPHIIaIHEVFENSSKIVIVMEYASRG 139
Cdd:cd14150   5 LKRIGTGSFGTVFRGKWHGD--VAVKILKVTEPTPEQ-LQAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQWCEGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYIS-ERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL---YHKGKFLQTFCG 215
Cdd:cd14150  81 SLYRHLHvTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVktrWSGSQQVEQPSG 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 27229182 216 SPLYASPEIV---NGKPYVGpEVDSWSLGVLLYILVHGTMPF 254
Cdd:cd14150 161 SILWMAPEVIrmqDTNPYSF-QSDVYAYGVVLYELMSGTLPY 201
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
63-256 5.02e-15

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: 75.12  E-value: 5.02e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSgrLVAIKSIrkdKIKD--EQDLLHIRREIEIMSSLNHPHIIAIHEVFeNSSKIVIVMEYASRGD 140
Cdd:cd14062   1 IGSGSFGTVYKGRWHG--DVAVKKL---NVTDptPSQLQAFKNEVAVLRKTRHVNILLFMGYM-TKPQLAIVTQWCEGSS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 141 LYDYIserprlsERDARHF--------FRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQT 212
Cdd:cd14062  75 LYKHL-------HVLETKFemlqlidiARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKTRWSGSQQ 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 F---CGSPLYASPEIV---NGKPYVgPEVDSWSLGVLLYILVHGTMPFDG 256
Cdd:cd14062 148 FeqpTGSILWMAPEVIrmqDENPYS-FQSDVYAFGIVLYELLTGQLPYSH 196
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
54-328 6.18e-15

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR 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: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 75.78  E-value: 6.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKK--AR-----ESSGRlVAIKSIRKDKIKDEQdlLHIRREIEIMSSLNHPHIIAIHEVFENS 126
Cdd:cd05061   5 REKITLLRELGQGSFGMVYEgnARdiikgEAETR-VAVKTVNESASLRER--IEFLNEASVMKGFTCHHVVRLLGVVSKG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 127 SKIVIVMEYASRGDLYDYI------SE----RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIA 196
Cdd:cd05061  82 QPTLVVMELMAHGDLKSYLrslrpeAEnnpgRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 197 DFGL------SNLYHKGkflqtfcGSPL----YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQ 265
Cdd:cd05061 162 DFGMtrdiyeTDYYRKG-------GKGLlpvrWMAPESLKDGVFT-TSSDMWSFGVVLWeITSLAEQPYQGLSNEQVLKF 233
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27229182 266 ISNGAYREPPK--PSDACGLIRWLLMVNPTRRATLEDVAshwwvnwgyttgvgeqEALREGGHPS 328
Cdd:cd05061 234 VMDGGYLDQPDncPERVTDLMRMCWQFNPKMRPTFLEIV----------------NLLKDDLHPS 282
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
58-295 1.11e-14

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 75.44  E-value: 1.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  58 EF--LETLGKGTYGKVKKAR-----ESSGRLVAIKSIRK-DKIKDEQDLLHirrEIEIMSSLNHPHIIAIHEVFENSSkI 129
Cdd:cd05108   8 EFkkIKVLGSGAFGTVYKGLwipegEKVKIPVAIKELREaTSPKANKEILD---EAYVMASVDNPHVCRLLGICLTST-V 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 130 VIVMEYASRGDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL----- 203
Cdd:cd05108  84 QLITQLMPFGCLLDYVREhKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLlgaee 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 204 --YHK--GKFlqtfcgsPL-YASPEIVNGKPYVGpEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGAyREPPKP 277
Cdd:cd05108 164 keYHAegGKV-------PIkWMALESILHRIYTH-QSDVWSYGVTVWeLMTFGSKPYDGIPASEISSILEKGE-RLPQPP 234
                       250       260
                ....*....|....*....|.
gi 27229182 278 ---SDACGLIRWLLMVNPTRR 295
Cdd:cd05108 235 ictIDVYMIMVKCWMIDADSR 255
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
63-244 1.19e-14

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: 74.09  E-value: 1.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSGRLVAIKSIRKDKIkdeqDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDLY 142
Cdd:cd14156   1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDV----DQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 143 DYIS-ERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIK---IADFGLSNLY-----HKGKFLQTF 213
Cdd:cd14156  77 ELLArEELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVgempaNDPERKLSL 156
                       170       180       190
                ....*....|....*....|....*....|.
gi 27229182 214 CGSPLYASPEIVNGKPYvGPEVDSWSLGVLL 244
Cdd:cd14156 157 VGSAFWMAPEMLRGEPY-DRKVDVFSFGIVL 186
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
61-245 1.69e-14

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 74.40  E-value: 1.69e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKAReSSGRLVAIKsirkdkIKDEQDLLHIRREIEIMSSLNHPH------IIAIHEVFENSSKIVIVME 134
Cdd:cd13998   1 EVIGKGRFGEVWKAS-LKNEPVAVK------IFSSRDKQSWFREKEIYRTPMLKHenilqfIAADERDTALRTELWLVTA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYIS-------ERPRLSERDAR---HFFRQIVSALHycHQNGIVHRDLKLENILLDANGNIKIADFGLSnLY 204
Cdd:cd13998  74 FHPNGSL*DYLSlhtidwvSLCRLALSVARglaHLHSEIPGCTQ--GKPAIAHRDLKSKNILVKNDGTCCIADFGLA-VR 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 27229182 205 HKGKFLQtfcgSPLYASPEiVNGKPYVGPEV----------------DSWSLGVLLY 245
Cdd:cd13998 151 LSPSTGE----EDNANNGQ-VGTKRYMAPEVlegainlrdfesfkrvDIYAMGLVLW 202
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
60-201 1.94e-14

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: 74.18  E-value: 1.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  60 LETLGKGTYGKVKKARESSGRL-VAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASR 138
Cdd:cd14026   2 LRYLSRGAFGTVSRARHADWRVtVAIKCLKLDSPVGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTN 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27229182 139 GDLYDYISER---PRLSERDARHFFRQIVSALHYCHQNG--IVHRDLKLENILLDANGNIKIADFGLS 201
Cdd:cd14026  82 GSLNELLHEKdiyPDVAWPLRLRILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLS 149
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
58-279 2.77e-14

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 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: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 73.88  E-value: 2.77e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  58 EFLETLGKGTYGKVKKARESSGRL---VAIKSIRKDKIKDeqDLLHIRREIEIMSSLN-HPHIIAIHEVFENSSKIVIVM 133
Cdd:cd05088  10 KFQDVIGEGNFGQVLKARIKKDGLrmdAAIKRMKEYASKD--DHRDFAGELEVLCKLGhHPNIINLLGACEHRGYLYLAI 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYI----------------SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIAD 197
Cdd:cd05088  88 EYAPHGNLLDFLrksrvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 198 FGLS---NLYHKgkflQTFCGSPL-YASPEIVNGKPYVgPEVDSWSLGVLLYILVH-GTMPFDGQDHKTLVKQISNGAYR 272
Cdd:cd05088 168 FGLSrgqEVYVK----KTMGRLPVrWMAIESLNYSVYT-TNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGYRL 242

                ....*..
gi 27229182 273 EPPKPSD 279
Cdd:cd05088 243 EKPLNCD 249
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
63-301 3.19e-14

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk 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: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 73.39  E-value: 3.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARESSGRLVA---IKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRG 139
Cdd:cd05042   3 IGNGWFGKVLLGEIYSGTSVAqvvVKELKASANPKEQD--TFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDLG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYI-SERPRLS-ERDARHFFR---QIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQT-- 212
Cdd:cd05042  81 DLKAYLrSEREHERgDSDTRTLQRmacEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAHSRYKEDYIETdd 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 213 FCGSPL-YASPEIV---NGKPYVGPEVDS---WSLGVLLYILVH-GTMPFDGQDHKTLVKQISNGAYREPPKP------S 278
Cdd:cd05042 161 KLWFPLrWTAPELVtefHDRLLVVDQTKYsniWSLGVTLWELFEnGAQPYSNLSDLDVLAQVVREQDTKLPKPqlelpyS 240
                       250       260
                ....*....|....*....|...
gi 27229182 279 DACGLIRWLLMVNPTRRATLEDV 301
Cdd:cd05042 241 DRWYEVLQFCWLSPEQRPAAEDV 263
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
60-256 4.08e-14

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 73.07  E-value: 4.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  60 LETLGKGTYGKVKKA-----RESSGRLVAIKSIrKDKiKDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSkIVIVME 134
Cdd:cd05111  12 LKVLGSGVFGTVHKGiwipeGDSIKIPVAIKVI-QDR-SGRQSFQAVTDHMLAIGSLDHAYIVRLLGICPGAS-LQLVTQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYH--KGKFLQ 211
Cdd:cd05111  89 LLPLGSLLDHVRQhRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLYpdDKKYFY 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 27229182 212 TFCGSPL-YASPEIVNGKPYVGpEVDSWSLGVLLY-ILVHGTMPFDG 256
Cdd:cd05111 169 SEAKTPIkWMALESIHFGKYTH-QSDVWSYGVTVWeMMTFGAEPYAG 214
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
61-297 4.43e-14

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (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. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM 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: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 72.95  E-value: 4.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKAR----ESSGRLVAIKSIRKDkIKDEQDLLHIRREIEIMSSLNHPHIIAIHEV-FENSSK-----IV 130
Cdd:cd05035   5 KILGEGEFGSVMEAQlkqdDGSQLKVAVKTMKVD-IHTYSEIEEFLSEAACMKDFDHPNVMRLIGVcFTASDLnkppsPM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 131 IVMEYASRGDLYDY-----ISERP-RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLY 204
Cdd:cd05035  84 VILPFMKHGDLHSYllysrLGGLPeKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 205 HKGKFLQTFCGSPL---YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGA-YREPPK-PS 278
Cdd:cd05035 164 YSGDYYRQGRISKMpvkWIALESLADNVYT-SKSDVWSFGVTMWeIATRGQTPYPGVENHEIYDYLRNGNrLKQPEDcLD 242
                       250
                ....*....|....*....
gi 27229182 279 DACGLIRWLLMVNPTRRAT 297
Cdd:cd05035 243 EVYFLMYFCWTVDPKDRPT 261
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
58-269 4.48e-14

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: 73.08  E-value: 4.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  58 EFLETLGKGTYGKVKKAR---ESSGRLVAIKSIRKDKIKdeqdllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVME 134
Cdd:cd14152   3 ELGELIGQGRWGKVHRGRwhgEVAIRLLEIDGNNQDHLK------LFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 135 YASRGDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDaNGNIKIADFGL---SNLYHKGKF- 209
Cdd:cd14152  77 FCKGRTLYSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLfgiSGVVQEGRRe 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27229182 210 --LQTFCGSPLYASPEIVN----GK-----PYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNG 269
Cdd:cd14152 156 neLKLPHDWLCYLAPEIVRemtpGKdedclPF-SKAADVYAFGTIWYELQARDWPLKNQPAEALIWQIGSG 225
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
79-301 7.87e-14

Pseudokinase domain of the unknown subfamily 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: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 72.20  E-value: 7.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  79 GRLVAIKSIRKDKIKDEQdllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDLYD-YISERPRLSERDAR 157
Cdd:cd14045  30 GRTVAIKKIAKKSFTLSK---RIRKEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDvLLNEDIPLNWGFRF 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 158 HFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSnLYHKGKFLQTFCG-----SPLYASPEIVNgKPYVG 232
Cdd:cd14045 107 SFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLT-TYRKEDGSENASGyqqrlMQVYLPPENHS-NTDTE 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27229182 233 PEV--DSWSLGVLLYILVHGTMPFDGQDHKT-------LVKQISNGAYREPPKPSDACGLIRWLLMVNPTRRATLEDV 301
Cdd:cd14045 185 PTQatDVYSYAIILLEIATRNDPVPEDDYSLdeawcppLPELISGKTENSCPCPADYVELIRRCRKNNPAQRPTFEQI 262
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
53-260 1.01e-13

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 72.58  E-value: 1.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLETLGKGTYGKVKKA--RESSGRLVAIKSIRK-DKIKDEQdllhiRREIEIMSSLNHP------HIIAIHEVF 123
Cdd:cd14213  10 LRARYEIVDTLGEGAFGKVVECidHKMGGMHVAVKIVKNvDRYREAA-----RSEIQVLEHLNTTdpnstfRCVQMLEWF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 124 ENSSKIVIVMEYASRGDlYDYISERPRLSER--DARHFFRQIVSALHYCHQNGIVHRDLKLENILLD------------- 188
Cdd:cd14213  85 DHHGHVCIVFELLGLST-YDFIKENSFLPFPidHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVqsdyvvkynpkmk 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27229182 189 ------ANGNIKIADFGLSNLYHkgKFLQTFCGSPLYASPEIVNGKPYVGPeVDSWSLGVLLYILVHGTMPFDGQDHK 260
Cdd:cd14213 164 rdertlKNPDIKVVDFGSATYDD--EHHSTLVSTRHYRAPEVILALGWSQP-CDVWSIGCILIEYYLGFTVFQTHDSK 238
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
61-299 1.12e-13

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: 71.58  E-value: 1.12e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKA---RESSGRLVAIKSIrKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEV-FENSSK-----IVI 131
Cdd:cd05075   6 KTLGEGEFGSVMEGqlnQDDSVLKVAVKTM-KIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVcLQNTESegypsPVV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 132 VMEYASRGDLYDYI-----SERP-RLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYH 205
Cdd:cd05075  85 ILPFMKHGDLHSFLlysrlGDCPvYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKIY 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 206 KGKFLQT--FCGSPL-YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNG-AYREPPKPSDa 280
Cdd:cd05075 165 NGDYYRQgrISKMPVkWIAIESLADRVYT-TKSDVWSFGVTMWeIATRGQTPYPGVENSEIYDYLRQGnRLKQPPDCLD- 242
                       250       260
                ....*....|....*....|....
gi 27229182 281 cGLIR-----WLLmvNPTRRATLE 299
Cdd:cd05075 243 -GLYElmsscWLL--NPKDRPSFE 263
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
61-274 1.27e-13

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: 71.63  E-value: 1.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARESSGrlVAIKSIRKDKIKDEQdLLHIRREIEIMSSLNHPHIIaIHEVFENSSKIVIVMEYASRGD 140
Cdd:cd14151  14 QRIGSGSFGTVYKGKWHGD--VAVKMLNVTAPTPQQ-LQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 141 LYDYI-SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNL---YHKGKFLQTFCGS 216
Cdd:cd14151  90 LYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVksrWSGSHQFEQLSGS 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27229182 217 PLYASPEIV---NGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREP 274
Cdd:cd14151 170 ILWMAPEVIrmqDKNPY-SFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSP 229
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
101-304 1.45e-13

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: 71.58  E-value: 1.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 101 IRREIEIMSSLNHPHIIAI-HEVFENSSKIVIVME--YAS--------------RGDLYDYiserpRLSERDARHFFRQI 163
Cdd:cd14011  49 LKRGVKQLTRLRHPRILTVqHPLEESRESLAFATEpvFASlanvlgerdnmpspPPELQDY-----KLYDVEIKYGLLQI 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 164 VSALHYCHQN-GIVHRDLKLENILLDANGNIKIADFGLS--------NLYHKGKFLQT---FCGSPL-YASPEIVNGKPY 230
Cdd:cd14011 124 SEALSFLHNDvKLVHGNICPESVVINSNGEWKLAGFDFCisseqatdQFPYFREYDPNlppLAQPNLnYLAPEYILSKTC 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 231 vGPEVDSWSLGVLLY-ILVHGTMPFDGQDHKT-------LVKQISNGAYREPPKPSDACglIRWLLMVNPTRRATLEDVA 302
Cdd:cd14011 204 -DPASDMFSLGVLIYaIYNKGKPLFDCVNNLLsykknsnQLRQLSLSLLEKVPEELRDH--VKTLLNVTPEVRPDAEQLS 280

                ..
gi 27229182 303 SH 304
Cdd:cd14011 281 KI 282
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
61-254 1.57e-13

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: 70.97  E-value: 1.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKA----RESSGRLVAIKSIrkDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEV-FENSSKIVIVMEY 135
Cdd:cd05058   1 EVIGKGHFGCVYHGtlidSDGQKIHCAVKSL--NRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGIcLPSEGSPLVVLPY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYI-SERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLS-NLYHKGKF-LQT 212
Cdd:cd05058  79 MKHGDLRNFIrSETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLArDIYDKEYYsVHN 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 27229182 213 FCGSPL---YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPF 254
Cdd:cd05058 159 HTGAKLpvkWMALESLQTQKFT-TKSDVWSFGVLLWeLMTRGAPPY 203
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
54-272 1.78e-13

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: 71.33  E-value: 1.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKA----RESSGRLVAIKSIrkdkiKDEQDLLHIRR---EIEIMSSLNHPHIIAI-HEVFEN 125
Cdd:cd05043   5 RERVTLSDLLQEGTFGRIFHGilrdEKGKEEEVLVKTV-----KDHASEIQVTMllqESSLLYGLSHQNLLPIlHVCIED 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 126 SSKIVIVMEYASRGDLYDYIsERPRLSE---------RDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIA 196
Cdd:cd05043  80 GEKPMVLYPYMNWGNLKLFL-QQCRLSEannpqalstQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKIT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 197 DFGLS-----NLYHkgkflqtfC-----GSPL-YASPEIVNGKPYvGPEVDSWSLGVLLYILVH-GTMPFDGQDHKTLVK 264
Cdd:cd05043 159 DNALSrdlfpMDYH--------ClgdneNRPIkWMSLESLVNKEY-SSASDVWSFGVLLWELMTlGQTPYVEIDPFEMAA 229

                ....*...
gi 27229182 265 QISNGaYR 272
Cdd:cd05043 230 YLKDG-YR 236
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
114-304 2.10e-13

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-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: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 70.65  E-value: 2.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 114 PHIIAIHEVFENSSKIVIVMEYASRGDLYDYISERprLSERDARHFFRQ------------------------IVSALHY 169
Cdd:cd05576  51 PNMVCLRKYIISEESVFLVLQHAEGGKLWSYLSKF--LNDKEIHQLFADlderlaaasrfyipeeciqrwaaeMVVALDA 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 170 CHQNGIVHRDLKLENILLDANGNIKIADFGlsnlyhKGKFLQTFCGSP----LYASPEiVNGKPYVGPEVDSWSLGVLLY 245
Cdd:cd05576 129 LHREGIVCRDLNPNNILLNDRGHIQLTYFS------RWSEVEDSCDSDaienMYCAPE-VGGISEETEACDWWSLGALLF 201
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27229182 246 ILVHGTM-----PFDGQDHKTLvkQISNGAYREppkpsdACGLIRWLLMVNPTRR-----ATLEDVASH 304
Cdd:cd05576 202 ELLTGKAlvechPAGINTHTTL--NIPEWVSEE------ARSLLQQLLQFNPTERlgagvAGVEDIKSH 262
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
61-303 2.60e-13

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: 70.60  E-value: 2.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  61 ETLGKGTYGKVKKARESSGRL-VAIKSIRKDKIkDEQDLLHIRREIEIMSSLNHPHIIAIHEVFenSSKIVIVMEYASRG 139
Cdd:cd14025   2 EKVGSGGFGQVYKVRHKHWKTwLAIKCPPSLHV-DDSERMELLEEAKKMEMAKFRHILPVYGIC--SEPVGLVMEYMETG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYISERPRLSERDARHFFRQIVSA--LHyCHQNGIVHRDLKLENILLDANGNIKIADFGLSN---LYHKGKF-LQTF 213
Cdd:cd14025  79 SLEKLLASEPLPWELRFRIIHETAVGMnfLH-CMKPPLLHLDLKPANILLDAHYHVKISDFGLAKwngLSHSHDLsRDGL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 214 CGSPLYASPEIVNGKPYV-GPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVK-QISNGAYREPP-----KPSDACGLIRw 286
Cdd:cd14025 158 RGTIAYLPPERFKEKNRCpDTKHDVYSFAIVIWGILTQKKPFAGENNILHIMvKVVKGHRPSLSpiprqRPSECQQMIC- 236
                       250       260
                ....*....|....*....|..
gi 27229182 287 lLMV-----NPTRRATLEDVAS 303
Cdd:cd14025 237 -LMKrcwdqDPRKRPTFQDITS 257
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
59-262 3.36e-13

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 70.37  E-value: 3.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  59 FLETLGKGTYGKVKKAR---ESSGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd14206   1 YLQEIGNGWFGKVILGEifsDYTPAQVVVKELRVSAGPLEQR--KFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISER-------PRLSERDARHFFR---QIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYH 205
Cdd:cd14206  79 CQLGDLKRYLRAQrkadgmtPDLPTRDLRTLQRmayEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSHNNY 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27229182 206 KGKFLQT--FCGSPL-YASPEI---VNGKPYV---GPEVDSWSLGVLLYILVHgtmpFDGQDHKTL 262
Cdd:cd14206 159 KEDYYLTpdRLWIPLrWVAPELldeLHGNLIVvdqSKESNVWSLGVTIWELFE----FGAQPYRHL 220
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
57-306 4.92e-13

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: 69.97  E-value: 4.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  57 YEFLETLGKGTYGKVKKARESSGrLVAIKS-IRKDkikDEQDLLHIRREIE-IMSSLN-HPHIIAIHEVFENSSKIVIVM 133
Cdd:cd13980   2 YLYDKSLGSTRFLKVARARHDEG-LVVVKVfVKPD---PALPLRSYKQRLEeIRDRLLeLPNVLPFQKVIETDKAAYLIR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYAsRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFG--------LSNLYH 205
Cdd:cd13980  78 QYV-KYNLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFAsfkptylpEDNPAD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 206 KGKFLQT------------FCGSPLYASPEIVNGKPyVGPEVDSWSLG-VLLYILVHGTMPFD---------GQDHKTLV 263
Cdd:cd13980 157 FSYFFDTsrrrtcyiaperFVDALTLDAESERRDGE-LTPAMDIFSLGcVIAELFTEGRPLFDlsqllayrkGEFSPEQV 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 27229182 264 -KQISNGAYREppkpsdacgLIRWLLMVNPTRRATLEDVASHWW 306
Cdd:cd13980 236 lEKIEDPNIRE---------LILHMIQRDPSKRLSAEDYLKKYR 270
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
60-245 6.35e-13

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 69.78  E-value: 6.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  60 LETLGKGTYGKVKKAReSSGRLVAIKSIRKdkiKDEQDLLhirREIEIMSS--LNHPHI---IAIHEVFENSS-KIVIVM 133
Cdd:cd14142  10 VECIGKGRYGEVWRGQ-WQGESVAVKIFSS---RDEKSWF---RETEIYNTvlLRHENIlgfIASDMTSRNSCtQLWLIT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 134 EYASRGDLYDYISeRPRLSERDARHFFRQIVSALHYCH--------QNGIVHRDLKLENILLDANGNIKIADFGLSNLYH 205
Cdd:cd14142  83 HYHENGSLYDYLQ-RTTLDHQEMLRLALSAASGLVHLHteifgtqgKPAIAHRDLKSKNILVKSNGQCCIADLGLAVTHS 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 27229182 206 KG-KFLQTFC----GSPLYASPEIVNGKPYVG-----PEVDSWSLGVLLY 245
Cdd:cd14142 162 QEtNQLDVGNnprvGTKRYMAPEVLDETINTDcfesyKRVDIYAFGLVLW 211
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
81-275 1.18e-12

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 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: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 68.41  E-value: 1.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  81 LVAIKSIRkDKIKDEQDLLHIRrEIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRGDLYDYISERP-RLSERDARHF 159
Cdd:cd05064  35 PVAIHTLR-AGCSDKQRRGFLA-EALTLGQFDHSNIVRLEGVITRGNTMMIVTEYMSNGALDSFLRKHEgQLVAGQLMGM 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 160 FRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCG-SP-LYASPEIVNGKPYvGPEVDS 237
Cdd:cd05064 113 LPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFRRLQEDKSEAIYTTMSGkSPvLWAAPEAIQYHHF-SSASDV 191
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 27229182 238 WSLGVLLY-ILVHGTMPFDGQDHKTLVKQISNGaYREPP 275
Cdd:cd05064 192 WSFGIVMWeVMSYGERPYWDMSGQDVIKAVEDG-FRLPA 229
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
63-244 1.60e-12

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: 67.89  E-value: 1.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  63 LGKGTYGKVKKARE-SSGRLVAIK--SIRKDKIkdeqdllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYASRG 139
Cdd:cd14155   1 IGSGFFSEVYKVRHrTSGQVMALKmnTLSSNRA-------NMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 140 DLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILL--DANGNIKI-ADFGLSN---LYHKGKFLQTF 213
Cdd:cd14155  74 NLEQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrDENGYTAVvGDFGLAEkipDYSDGKEKLAV 153
                       170       180       190
                ....*....|....*....|....*....|.
gi 27229182 214 CGSPLYASPEIVNGKPYvGPEVDSWSLGVLL 244
Cdd:cd14155 154 VGSPYWMAPEVLRGEPY-NEKADVFSYGIIL 183
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
54-303 1.89e-12

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R 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: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 68.14  E-value: 1.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  54 RHRYEFLETLGKGTYGKVKKA------RESSGRLVAIKSIRKDKIKDEQdlLHIRREIEIMSSLNHPHIIAIHEVFENSS 127
Cdd:cd05062   5 REKITMSRELGQGSFGMVYEGiakgvvKDEPETRVAIKTVNEAASMRER--IEFLNEASVMKEFNCHHVVRLLGVVSQGQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 128 KIVIVMEYASRGDLYDYI-SERPRLSERDAR---------HFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIAD 197
Cdd:cd05062  83 PTLVIMELMTRGDLKSYLrSLRPEMENNPVQappslkkmiQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGD 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 198 FGL------SNLYHKGkflqtfcGSPL----YASPEIVNGKPYVgPEVDSWSLGVLLY-ILVHGTMPFDGQDHKTLVKQI 266
Cdd:cd05062 163 FGMtrdiyeTDYYRKG-------GKGLlpvrWMSPESLKDGVFT-TYSDVWSFGVVLWeIATLAEQPYQGMSNEQVLRFV 234
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 27229182 267 SNGAYREPPK--PSDACGLIRWLLMVNPTRRATLEDVAS 303
Cdd:cd05062 235 MEGGLLDKPDncPDMLFELMRMCWQYNPKMRPSFLEIIS 273
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
58-269 2.27e-12

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: 67.73  E-value: 2.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  58 EFLETLGKGTYGKVKKARESSGRLVAIKSIRKDkikDEQDLLHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEYAS 137
Cdd:cd14153   3 EIGELIGKGRFGQVYHGRWHGEVAIRLIDIERD---NEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 138 RGDLYDYISE-RPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDaNGNIKIADFGL---SNLYHKGKF---L 210
Cdd:cd14153  80 GRTLYSVVRDaKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGLftiSGVLQAGRRedkL 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27229182 211 QTFCGSPLYASPEIV---------NGKPYvGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNG 269
Cdd:cd14153 159 RIQSGWLCHLAPEIIrqlspeteeDKLPF-SKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVGSG 225
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
53-266 2.39e-12

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: 68.50  E-value: 2.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  53 LRHRYEFLETLGKGTYGKVKK----ARESSGrlVAIKSIRK-DKIKDEQDL-LHIRREIEIMSSLNHPHIIAIHEVFENS 126
Cdd:cd14214  11 LQERYEIVGDLGEGTFGKVVEcldhARGKSQ--VALKIIRNvGKYREAARLeINVLKKIKEKDKENKFLCVLMSDWFNFH 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 127 SKIVIVMEYASRgDLYDYISERPRLSE--RDARHFFRQIVSALHYCHQNGIVHRDLKLENILL----------------- 187
Cdd:cd14214  89 GHMCIAFELLGK-NTFEFLKENNFQPYplPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFvnsefdtlyneskscee 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 188 --DANGNIKIADFGLSNLYHkgKFLQTFCGSPLYASPEIVNGKPYVGPeVDSWSLGVLLYILVHGTMPF---DGQDHKTL 262
Cdd:cd14214 168 ksVKNTSIRVADFGSATFDH--EHHTTIVATRHYRPPEVILELGWAQP-CDVWSLGCILFEYYRGFTLFqthENREHLVM 244

                ....
gi 27229182 263 VKQI 266
Cdd:cd14214 245 MEKI 248
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
59-301 2.65e-12

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 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: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 67.58  E-value: 2.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182  59 FLETLGKGTYGKV---KKARESSGRLVAIKSIRKDKIKDEQDllHIRREIEIMSSLNHPHIIAIHEVFENSSKIVIVMEY 135
Cdd:cd05086   1 YIQEIGNGWFGKVllgEIYTGTSVARVVVKELKASANPKEQD--DFLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 136 ASRGDLYDYISERPRLSERDARHFFRQ-----IVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFL 210
Cdd:cd05086  79 CDLGDLKTYLANQQEKLRGDSQIMLLQrmaceIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIGFSRYKEDYI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229182 211 QTFCGS--PL-YASPEIV---NGKPYVGPEVDS---WSLGVLLYILV-HGTMPFDGQDHKTLVKQISNGAYREPPKP--- 277
Cdd:cd05086 159 ETDDKKyaPLrWTAPELVtsfQDGLLAAEQTKYsniWSLGVTLWELFeNAAQPYSDLSDREVLNHVIKERQVKLFKPhle 238
                       250       260       270
                ....*....|....*....|....*....|..
gi 27229182 278 ---SDacgliRW-----LLMVNPTRRATLEDV 301
Cdd:cd05086 239 qpySD-----RWyevlqFCWLSPEKRPTAEEV 265
 
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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