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Conserved domains on  [gi|75570321|sp|Q90ZY4|]
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RecName: Full=Serine/threonine-protein kinase SBK1; AltName: Full=Brain-specific protein kinase BSK146; AltName: Full=SH3 domain-binding kinase 1

Protein Classification

SBK1 family serine/threonine-protein kinase( domain architecture ID 10195655)

SBK1 (SH3 domain binding kinase 1) family serine/threonine-protein kinase 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_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
38-296 5.49e-171

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: 477.20  E-value: 5.49e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIAFETDEYYVFAQEYAPSGDLFD 117
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLREYNISLELSVHPHIIKTYDVAFETEDYYVFAQEYAPYGDLFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 118 IIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTRRAGSPVKRVSGTIPYTAPE 197
Cdd:cd13987  81 IIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRVKLCDFGLTRRVGSTVKRVSGTIPYTAPE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 198 LCDTSKHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEEFVRWQKRRTGAVPSQWRRFTDESLRMFRKLLAL 277
Cdd:cd13987 161 VCEAKKNEGFVVDPSIDVWAFGVLLFCCLTGNFPWEKADSDDQFYEEFVRWQKRKNTAVPSQWRRFTPKALRMFKKLLAP 240
                       250
                ....*....|....*....
gi 75570321 278 EQERRCSVKEVFAHLGHRW 296
Cdd:cd13987 241 EPERRCSIKEVFKYLGDRW 259
 
Name Accession Description Interval E-value
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
38-296 5.49e-171

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: 477.20  E-value: 5.49e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIAFETDEYYVFAQEYAPSGDLFD 117
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLREYNISLELSVHPHIIKTYDVAFETEDYYVFAQEYAPYGDLFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 118 IIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTRRAGSPVKRVSGTIPYTAPE 197
Cdd:cd13987  81 IIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRVKLCDFGLTRRVGSTVKRVSGTIPYTAPE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 198 LCDTSKHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEEFVRWQKRRTGAVPSQWRRFTDESLRMFRKLLAL 277
Cdd:cd13987 161 VCEAKKNEGFVVDPSIDVWAFGVLLFCCLTGNFPWEKADSDDQFYEEFVRWQKRKNTAVPSQWRRFTPKALRMFKKLLAP 240
                       250
                ....*....|....*....
gi 75570321 278 EQERRCSVKEVFAHLGHRW 296
Cdd:cd13987 241 EPERRCSIKEVFKYLGDRW 259
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
32-291 1.95e-65

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 208.54  E-value: 1.95e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321     32 YEVIRELGKGTYGKVDLVIHKIRGSKMA--LKFLKKKSTKLKSFLREYSISLYLSpCPFIINMFGIaFETDEYYVFAQEY 109
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAikVIKKKKIKKDRERILREIKILKKLK-HPNIVRLYDV-FEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321    110 APSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAGSPVKRVS- 188
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL-DEDGH-VKLADFGLARQLDPGEKLTTf 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321    189 -GTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWekamPSDTFYEEFVRWQKRRTGAVPSQWRRFTDES 267
Cdd:smart00220 157 vGTPEYMAPEVLLGKGY-----GKAVDIWSLGVILYELLTGKPPF----PGDDQLLELFKKIGKPKPPFPPPEWDISPEA 227
                          250       260
                   ....*....|....*....|....
gi 75570321    268 LRMFRKLLALEQERRCSVKEVFAH 291
Cdd:smart00220 228 KDLIRKLLVKDPEKRLTAEEALQH 251
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
32-292 1.42e-42

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 155.17  E-value: 1.42e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGS----KMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGiAFETDEYYVFAQ 107
Cdd:COG0515   9 YRILRLLGRGGMGVVYLARDLRLGRpvalKVLRPELAADPEARERFRREARALARLNH-PNIVRVYD-VGEEDGRPYLVM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAGSPVK-- 185
Cdd:COG0515  87 EYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL-TPDGR-VKLIDFGIARALGGATLtq 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 186 --RVSGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEEFvrwqkRRTGAVPSQWRRF 263
Cdd:COG0515 165 tgTVVGTPGYMAPEQARGEP-----VDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHL-----REPPPPPSELRPD 234
                       250       260       270
                ....*....|....*....|....*....|.
gi 75570321 264 TDESL-RMFRKLLALEQERRC-SVKEVFAHL 292
Cdd:COG0515 235 LPPALdAIVLRALAKDPEERYqSAAELAAAL 265
Pkinase pfam00069
Protein kinase domain;
32-297 9.78e-31

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 116.57  E-value: 9.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321    32 YEVIRELGKGTYGKVDLVIHKIRGSKMAL---KFLKKKSTKLKSFLREYSISLYLSpCPFIINMFGiAFETDEYYVFAQE 108
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIkkiKKEKIKKKKDKNILREIKILKKLN-HPNIVRLYD-AFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   109 YAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYlhskklvhrdikpenilifdkecrkvklsdfgmtrraGSPVKRVS 188
Cdd:pfam00069  79 YVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLES-------------------------------------GSSLTTFV 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   189 GTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEEFvrwqkRRTGAVPSQWRRFTDESL 268
Cdd:pfam00069 122 GTPWYMAPEVLGGNPY-----GPKVDVWSLGCILYELLTGKPPFPGINGNEIYELII-----DQPYAFPELPSNLSEEAK 191
                         250       260
                  ....*....|....*....|....*....
gi 75570321   269 RMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:pfam00069 192 DLLKKLLKKDPSKRLTATQA---LQHPWF 217
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
20-282 9.73e-28

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 111.45  E-value: 9.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   20 AQNLEKLEVNKY----YEVIRELGKGTYGKVDLVIHKIRGSKMA----LKFLKKKSTKLKSFLREYSISLYLSPcPFIIN 91
Cdd:PTZ00263   4 AYMFTKPDTSSWklsdFEMGETLGTGSFGRVRIAKHKGTGEYYAikclKKREILKMKQVQHVAQEKSILMELSH-PFIVN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   92 MFgIAFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKL 171
Cdd:PTZ00263  83 MM-CSFQDENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKG--HVKV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  172 SDFGMTRRAGSPVKRVSGTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPwekampsdtFYEE--FVRWQ 249
Cdd:PTZ00263 160 TDFGFAKKVPDRTFTLCGTPEYLAPEVIQSKGHGK-----AVDWWTMGVLLYEFIAGYPP---------FFDDtpFRIYE 225
                        250       260       270
                 ....*....|....*....|....*....|....
gi 75570321  250 KRRTGAVpsQWRRFTDESLRMFRK-LLALEQERR 282
Cdd:PTZ00263 226 KILAGRL--KFPNWFDGRARDLVKgLLQTDHTKR 257
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
87-233 4.38e-16

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 79.84  E-value: 4.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   87 PFIINMF--GiafETDEYYVFAQEYAPSGDLFDIIppQVGLPEPVaKRCVH---QVAIALEYLHSKKLVHRDIKPENILI 161
Cdd:NF033483  67 PNIVSVYdvG---EDGGIPYIVMEYVDGRTLKDYI--REHGPLSP-EEAVEimiQILSALEHAHRNGIVHRDIKPQNILI 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  162 fDKEcRKVKLSDFG---------MTRRAGspvkrVSGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:NF033483 141 -TKD-GRVKVTDFGiaralssttMTQTNS-----VLGTVHYLSPEQARGGT-----VDARSDIYSLGIVLYEMLTGRPPF 208

                 .
gi 75570321  233 E 233
Cdd:NF033483 209 D 209
 
Name Accession Description Interval E-value
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
38-296 5.49e-171

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: 477.20  E-value: 5.49e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIAFETDEYYVFAQEYAPSGDLFD 117
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLREYNISLELSVHPHIIKTYDVAFETEDYYVFAQEYAPYGDLFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 118 IIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTRRAGSPVKRVSGTIPYTAPE 197
Cdd:cd13987  81 IIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRVKLCDFGLTRRVGSTVKRVSGTIPYTAPE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 198 LCDTSKHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEEFVRWQKRRTGAVPSQWRRFTDESLRMFRKLLAL 277
Cdd:cd13987 161 VCEAKKNEGFVVDPSIDVWAFGVLLFCCLTGNFPWEKADSDDQFYEEFVRWQKRKNTAVPSQWRRFTPKALRMFKKLLAP 240
                       250
                ....*....|....*....
gi 75570321 278 EQERRCSVKEVFAHLGHRW 296
Cdd:cd13987 241 EPERRCSIKEVFKYLGDRW 259
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
32-291 1.95e-65

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 208.54  E-value: 1.95e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321     32 YEVIRELGKGTYGKVDLVIHKIRGSKMA--LKFLKKKSTKLKSFLREYSISLYLSpCPFIINMFGIaFETDEYYVFAQEY 109
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAikVIKKKKIKKDRERILREIKILKKLK-HPNIVRLYDV-FEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321    110 APSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAGSPVKRVS- 188
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL-DEDGH-VKLADFGLARQLDPGEKLTTf 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321    189 -GTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWekamPSDTFYEEFVRWQKRRTGAVPSQWRRFTDES 267
Cdd:smart00220 157 vGTPEYMAPEVLLGKGY-----GKAVDIWSLGVILYELLTGKPPF----PGDDQLLELFKKIGKPKPPFPPPEWDISPEA 227
                          250       260
                   ....*....|....*....|....
gi 75570321    268 LRMFRKLLALEQERRCSVKEVFAH 291
Cdd:smart00220 228 KDLIRKLLVKDPEKRLTAEEALQH 251
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
32-296 4.62e-55

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


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 182.15  E-value: 4.62e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLR---EYSISLYLSPcPFIINMFGIAFETDEYYVFaQE 108
Cdd:cd14069   3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENikkEVCIQKMLSH-KNVVRFYGHRREGEFQYLF-LE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMT---RRAGSpvK 185
Cdd:cd14069  81 YASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDEND--NLKISDFGLAtvfRYKGK--E 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 186 RVS----GTIPYTAPELCDTSKHDGFCVdystDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEEFVrwQKRRTGAVPsqWR 261
Cdd:cd14069 157 RLLnkmcGTLPYVAPELLAKKKYRAEPV----DVWSCGIVLFAMLAGELPWDQPSDSCQEYSDWK--ENKKTYLTP--WK 228
                       250       260       270
                ....*....|....*....|....*....|....*
gi 75570321 262 RFTDESLRMFRKLLALEQERRCSVKEVfahLGHRW 296
Cdd:cd14069 229 KIDTAALSLLRKILTENPNKRITIEDI---KKHPW 260
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
32-296 7.81e-55

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: 181.18  E-value: 7.81e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMA---LKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFGIaFETDEYYVFAQE 108
Cdd:cd14003   2 YELGKTLGEGSFGKVKLARHKLTGEKVAikiIDKSKLKEEIEEKIKREIEI-MKLLNHPNIIKLYEV-IETENKIYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTR--RAGSPVKR 186
Cdd:cd14003  80 YASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILL-DKNGN-LKIIDFGLSNefRGGSLLKT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 187 VSGTIPYTAPELCDTSKHDGFCVdystDVWAFGVLLFCMLTGNFPWEkampsDTFYEEFVRWQKRRTgavPSQWRRFTDE 266
Cdd:cd14003 158 FCGTPAYAAPEVLLGRKYDGPKA----DVWSLGVILYAMLTGYLPFD-----DDNDSKLFRKILKGK---YPIPSHLSPD 225
                       250       260       270
                ....*....|....*....|....*....|
gi 75570321 267 SLRMFRKLLALEQERRCSVKEVfahLGHRW 296
Cdd:cd14003 226 ARDLIRRMLVVDPSKRITIEEI---LNHPW 252
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
38-292 1.39e-47

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: 160.90  E-value: 1.39e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMA--LKFLKKKSTKLKSFLREYSISLYLSpCPFIINMFGIaFETDEYYVFAQEYAPSGDL 115
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAvkVIPKEKLKKLLEELLREIEILKKLN-HPNIVKLYDV-FETENFLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 116 FDIIPPQVG-LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAGSPVKRVSGTIPYT 194
Cdd:cd00180  79 KDLLKENKGpLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILL--DSDGTVKLADFGLAKDLDSDDSLLKTTGGTT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 195 APELCDTSKHDGFCVDYSTDVWAFGVLLFCMltgnfpwekampsdtfyEEFVrwqkrrtgavpsqwrrftdeslRMFRKL 274
Cdd:cd00180 157 PPYYAPPELLGGRYYGPKVDIWSLGVILYEL-----------------EELK----------------------DLIRRM 197
                       250
                ....*....|....*...
gi 75570321 275 LALEQERRCSVKEVFAHL 292
Cdd:cd00180 198 LQYDPKKRPSAKELLEHL 215
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
32-298 1.44e-44

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: 154.55  E-value: 1.44e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMA----LKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGiAFETDEYYVFAQ 107
Cdd:cd14007   2 FEIGKPLGKGKFGNVYLAREKKSGFIVAlkviSKSQLQKSGLEHQLRREIEIQSHLRH-PNILRLYG-YFEDKKRIYLIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRAGSPVKR- 186
Cdd:cd14007  80 EYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNG--ELKLADFGWSVHAPSNRRKt 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 187 VSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFyeefvrwQKRRTGAV--PSQwrrFT 264
Cdd:cd14007 158 FCGTLDYLPPEMVEGKEY-----DYKVDIWSLGVLCYELLVGKPPFESKSHQETY-------KRIQNVDIkfPSS---VS 222
                       250       260       270
                ....*....|....*....|....*....|....
gi 75570321 265 DESLRMFRKLLALEQERRCSVKEVFAhlgHRWML 298
Cdd:cd14007 223 PEAKDLISKLLQKDPSKRLSLEQVLN---HPWIK 253
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
32-296 1.18e-43

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: 152.25  E-value: 1.18e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMAL---KFLKKKSTKLKSFLREYSISLYLSpCPFIINMFGIaFETDEYYVFAQE 108
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVkiiDKKKLKSEDEEMLRREIEILKRLD-HPNIVKLYEV-FEDDKNLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKE-CRKVKLSDFGMTRR--AGSPVK 185
Cdd:cd05117  80 LCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDpDSPIKIIDFGLAKIfeEGEKLK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 186 RVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWEkampSDTFYEEFvrwQKRRTGAV---PSQWRR 262
Cdd:cd05117 160 TVCGTPYYVAPEVLKGKGY-----GKKCDIWSLGVILYILLCGYPPFY----GETEQELF---EKILKGKYsfdSPEWKN 227
                       250       260       270
                ....*....|....*....|....*....|....
gi 75570321 263 FTDESLRMFRKLLALEQERRCSVKEVfahLGHRW 296
Cdd:cd05117 228 VSEEAKDLIKRLLVVDPKKRLTAAEA---LNHPW 258
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
27-297 1.25e-42

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: 149.85  E-value: 1.25e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  27 EVNKYYEVIRELGKGTYGKVDLVIHKIRGSKMA---------LKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIaF 97
Cdd:cd14084   3 ELRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAikiinkrkfTIGSRREINKPRNIETEIEILKKLSH-PCIIKIEDF-F 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  98 ETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDK--ECRkVKLSDFG 175
Cdd:cd14084  81 DAEDDYYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQeeECL-IKITDFG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 176 MTRRAG--SPVKRVSGTIPYTAPELCDTSKHDGfcvdYS--TDVWAFGVLLFCMLTGNFPWekampSDTFYEEFVRWQ-- 249
Cdd:cd14084 160 LSKILGetSLMKTLCGTPTYLAPEVLRSFGTEG----YTraVDCWSLGVILFICLSGYPPF-----SEEYTQMSLKEQil 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 75570321 250 KRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14084 231 SGKYTFIPKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEA---LEHPWL 275
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
32-292 1.42e-42

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 155.17  E-value: 1.42e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGS----KMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGiAFETDEYYVFAQ 107
Cdd:COG0515   9 YRILRLLGRGGMGVVYLARDLRLGRpvalKVLRPELAADPEARERFRREARALARLNH-PNIVRVYD-VGEEDGRPYLVM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAGSPVK-- 185
Cdd:COG0515  87 EYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL-TPDGR-VKLIDFGIARALGGATLtq 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 186 --RVSGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEEFvrwqkRRTGAVPSQWRRF 263
Cdd:COG0515 165 tgTVVGTPGYMAPEQARGEP-----VDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHL-----REPPPPPSELRPD 234
                       250       260       270
                ....*....|....*....|....*....|.
gi 75570321 264 TDESL-RMFRKLLALEQERRC-SVKEVFAHL 292
Cdd:COG0515 235 LPPALdAIVLRALAKDPEERYqSAAELAAAL 265
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
32-292 6.56e-42

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: 147.73  E-value: 6.56e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGS----KMALKFLKKKSTKLKSFLREYSISLYLSpCPFIINMFGIaFETDEYYVFAQ 107
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLLGRpvaiKVLRPELAEDEEFRERFLREARALARLS-HPNIVRVYDV-GEDDGRPYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRAGSPVK-- 185
Cdd:cd14014  80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG--RVKLTDFGIARALGDSGLtq 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 186 --RVSGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEefvrwQKRRTGAVPSQWRRF 263
Cdd:cd14014 158 tgSVLGTPAYMAPEQARGGP-----VDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAK-----HLQEAPPPPSPLNPD 227
                       250       260       270
                ....*....|....*....|....*....|.
gi 75570321 264 TDESL-RMFRKLLALEQERR-CSVKEVFAHL 292
Cdd:cd14014 228 VPPALdAIILRALAKDPEERpQSAAELLAAL 258
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
38-291 8.00e-41

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: 145.00  E-value: 8.00e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDL-------------VIHKIRGSKMALKFLKKKSTKLKSFL--REYSIslyLSPC--PFIINMFGI---AF 97
Cdd:cd14008   1 LGRGSFGKVKLaldtetgqlyaikIFNKSRLRKRREGKNDRGKIKNALDDvrREIAI---MKKLdhPNIVRLYEViddPE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  98 ETDEYYVFaqEYAPSGDLFDIIPPQVG--LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFG 175
Cdd:cd14008  78 SDKLYLVL--EYCEGGPVMELDSGDRVppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLL--TADGTVKISDFG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 176 ---MTRRAGSPVKRVSGTIPYTAPELCDTSkHDGFCVdYSTDVWAFGVLLFCMLTGNFPWEkampSDTFYEEFvrwQKRR 252
Cdd:cd14008 154 vseMFEDGNDTLQKTAGTPAFLAPELCDGD-SKTYSG-KAADIWALGVTLYCLVFGRLPFN----GDNILELY---EAIQ 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 75570321 253 TGAVPSQWRRFTDESLR-MFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14008 225 NQNDEFPIPPELSPELKdLLRRMLEKDPEKRITLKEIKEH 264
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
36-233 1.30e-40

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: 144.20  E-value: 1.30e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  36 RELGKGTYGKVDLVIHKIRGSKMA---LKFLKKKSTKLKSFLREYSISLYLSpCPFIINMFGIAFETDEYYVFaQEYAPS 112
Cdd:cd06606   6 ELLGKGSFGSVYLALNLDTGELMAvkeVELSGDSEEELEALEREIRILSSLK-HPNIVRYLGTERTENTLNIF-LEYVPG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 113 GDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTRR-----AGSPVKRV 187
Cdd:cd06606  84 GSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGV--VKLADFGCAKRlaeiaTGEGTKSL 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75570321 188 SGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd06606 162 RGTPYWMAPEVIRGEGY-----GRAADIWSLGCTVIEMATGKPPWS 202
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
38-231 1.83e-40

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: 143.43  E-value: 1.83e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGS----KMALKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFgIAFETDEYYVFAQEYAPSG 113
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKlyamKVLRKKEIIKRKEVEHTLNERNI-LERVNHPFIVKLH-YAFQTEEKLYLVLDYVPGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAGSPVKR---VSGT 190
Cdd:cd05123  79 ELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILL-DSDGH-IKLTDFGLAKELSSDGDRtytFCGT 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 75570321 191 IPYTAPELCDTSKHdGFCVDYstdvWAFGVLLFCMLTGNFP 231
Cdd:cd05123 157 PEYLAPEVLLGKGY-GKAVDW----WSLGVLLYEMLTGKPP 192
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
38-289 4.66e-38

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


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 137.82  E-value: 4.66e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKM--------ALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIAFETDEYYVFAQEY 109
Cdd:cd13994   1 IGKGATSVVRIVTKKNPRSGVlyavkeyrRRDDESKRKDYVKRLTSEYIISSKLHH-PNIVKVLDLCQDLHGKWCLVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 110 APSGDLFDIIPPQvGLPEPVAKRC-VHQVAIALEYLHSKKLVHRDIKPENILIfDKECrKVKLSDFGMTRRAGSPV---- 184
Cdd:cd13994  80 CPGGDLFTLIEKA-DSLSLEEKDCfFKQILRGVAYLHSHGIAHRDLKPENILL-DEDG-VLKLTDFGTAEVFGMPAekes 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 ---KRVSGTIPYTAPELCDTSKHDGFCVDystdVWAFGVLLFCMLTGNFPWEKAMPSDTFYEEFVRwQKRRTGAVPSQWR 261
Cdd:cd13994 157 pmsAGLCGSEPYMAPEVFTSGSYDGRAVD----VWSCGIVLFALFTGRFPWRSAKKSDSAYKAYEK-SGDFTNGPYEPIE 231
                       250       260
                ....*....|....*....|....*....
gi 75570321 262 RFTD-ESLRMFRKLLALEQERRCSVKEVF 289
Cdd:cd13994 232 NLLPsECRRLIYRMLHPDPEKRITIDEAL 260
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
32-297 2.14e-37

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: 135.77  E-value: 2.14e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDL---------------VIHKIRGSKmalkflkkksTKLKSFL-REYSISLYLSPcPFIINMFGI 95
Cdd:cd14080   2 YRLGKTIGEGSYSKVKLaeytksglkekvackIIDKKKAPK----------DFLEKFLpRELEILRKLRH-PNIIQVYSI 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  96 aFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFG 175
Cdd:cd14080  71 -FERGSKVFIFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILL--DSNNNVKLSDFG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 176 MTRRAGSPVKRVS-----GTIPYTAPELCDTSKHDGFcvdySTDVWAFGVLLFCMLTGnfpwekAMP-SDTFYEEFVRWQ 249
Cdd:cd14080 148 FARLCPDDDGDVLsktfcGSAAYAAPEILQGIPYDPK----KYDIWSLGVILYIMLCG------SMPfDDSNIKKMLKDQ 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 75570321 250 KRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAhlgHRWM 297
Cdd:cd14080 218 QNRKVRFPSSVKKLSPECKDLIDQLLEPDPTKRATIEEILN---HPWL 262
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
32-296 1.61e-33

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: 125.52  E-value: 1.61e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPC-PFIINMFGiAFETDEYYVFAQEYA 110
Cdd:cd14095   2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHMIENEVAILRRVKhPNIVQLIE-EYDTDTELYLVMELV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKE--CRKVKLSDFGMTRRAGSPVKRVS 188
Cdd:cd14095  81 KGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEdgSKSLKLADFGLATEVKEPLFTVC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 189 GTIPYTAPE-LCDTSKhdGFCVdystDVWAFGVLLFCMLTGnFPWEKAmPSDTFYEEFVRWQKRRTGAVPSQWRRFTDES 267
Cdd:cd14095 161 GTPTYVAPEiLAETGY--GLKV----DIWAAGVITYILLCG-FPPFRS-PDRDQEELFDLILAGEFEFLSPYWDNISDSA 232
                       250       260
                ....*....|....*....|....*....
gi 75570321 268 LRMFRKLLALEQERRCSVKEVfahLGHRW 296
Cdd:cd14095 233 KDLISRMLVVDPEKRYSAGQV---LDHPW 258
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
32-296 2.51e-33

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: 125.77  E-value: 2.51e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGS----KMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGiAFETDEYYVFAQ 107
Cdd:cd05580   3 FEFLKTLGTGSFGRVRLVKHKDSGKyyalKILKKAKIIKLKQVEHVLNEKRILSEVRH-PFIVNLLG-SFQDDRNLYMVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKeCRKVKLSDFGMTRRAGSPVKRV 187
Cdd:cd05580  81 EYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLL-DS-DGHIKITDFGFAKRVKDRTYTL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 188 SGTIPYTAPELCDTSKHdGFCVDYstdvWAFGVLLFCMLTGNFPwekampsdtFYEE--FVRWQKRRTGAVpsQWRRFTD 265
Cdd:cd05580 159 CGTPEYLAPEIILSKGH-GKAVDW----WALGILIYEMLAGYPP---------FFDEnpMKIYEKILEGKI--RFPSFFD 222
                       250       260       270
                ....*....|....*....|....*....|....
gi 75570321 266 ESLR-MFRKLLALEQERR--CSVKEVFAHLGHRW 296
Cdd:cd05580 223 PDAKdLIKRLLVVDLTKRlgNLKNGVEDIKNHPW 256
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
33-235 6.52e-33

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: 123.86  E-value: 6.52e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  33 EVIRELGKGTYGKVDLVIHKIRGSKMA--LKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFGiAFETDEYYVFAQEYA 110
Cdd:cd06623   4 ERVKVLGQGSSGVVYKVRHKPTGKIYAlkKIHVDGDEEFRKQLLRELKT-LRSCESPYVVKCYG-AFYKEGEISIVLEYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSK-KLVHRDIKPENILIFDKECrkVKLSDFGMTRR-AGSPVKRVS 188
Cdd:cd06623  82 DGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGE--VKIADFGISKVlENTLDQCNT 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 75570321 189 --GTIPYTAPELCDtSKHDGfcvdYSTDVWAFGVLLFCMLTGNFPWEKA 235
Cdd:cd06623 160 fvGTVTYMSPERIQ-GESYS----YAADIWSLGLTLLECALGKFPFLPP 203
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
32-291 1.20e-32

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: 122.96  E-value: 1.20e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMAL---KFLKKKSTKLKSFLREYSIslyLSPC--PFIINMFGiAFETDEYYVFA 106
Cdd:cd08215   2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLkeiDLSNMSEKEREEALNEVKL---LSKLkhPNIVKYYE-SFEENGKLCIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 107 QEYAPSGDLFDII----PPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKecRKVKLSDFGMTRRAGS 182
Cdd:cd08215  78 MEYADGGDLAQKIkkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKD--GVVKLGDFGISKVLES 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 183 PV---KRVSGTIPYTAPELCdtsKHDGFcvDYSTDVWAFGVLLFCMLTGNFPWEkampSDTFYEEFVRWQKRRTGAVPSQ 259
Cdd:cd08215 156 TTdlaKTVVGTPYYLSPELC---ENKPY--NYKSDIWALGCVLYELCTLKHPFE----ANNLPALVYKIVKGQYPPIPSQ 226
                       250       260       270
                ....*....|....*....|....*....|..
gi 75570321 260 wrrFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd08215 227 ---YSSELRDLVNSMLQKDPEKRPSANEILSS 255
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
31-291 1.82e-32

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: 122.75  E-value: 1.82e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  31 YYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPC-PFIINMFGIaFETDEYYVFAQEY 109
Cdd:cd14185   1 HYEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMIESEILIIKSLShPNIVKLFEV-YETEKEIYLILEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 110 APSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKE--CRKVKLSDFGMTRRAGSPVKRV 187
Cdd:cd14185  80 VRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPdkSTTLKLADFGLAKYVTGPIFTV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 188 SGTIPYTAPELCdTSKHDGFCVdystDVWAFGVLLFCMLTGNFPWEKamPSDTFYEEFVRWQKRRTGAVPSQWRRFTDES 267
Cdd:cd14185 160 CGTPTYVAPEIL-SEKGYGLEV----DMWAAGVILYILLCGFPPFRS--PERDQEELFQIIQLGHYEFLPPYWDNISEAA 232
                       250       260
                ....*....|....*....|....
gi 75570321 268 LRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14185 233 KDLISRLLVVDPEKRYTAKQVLQH 256
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
40-291 4.38e-32

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: 121.94  E-value: 4.38e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  40 KGTYGKVDLVIHKIRGSKMA----LKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFgIAFETDEYYVFAQEYAPSGDL 115
Cdd:cd05579   3 RGAYGRVYLAKKKSTGDLYAikviKKRDMIRKNQVDSVLAERNI-LSQAQNPFVVKLY-YSFQGKKNLYLVMEYLPGGDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 116 FDIIPpQVG-LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTR---------------- 178
Cdd:cd05579  81 YSLLE-NVGaLDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILI-DANGH-LKLTDFGLSKvglvrrqiklsiqkks 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 179 --RAGSPVKRVSGTIPYTAPELCDTSKHdGFCVDYstdvWAFGVLLFCMLTGNFPWEKAMPSDTFyeefvrwQKRRTGAV 256
Cdd:cd05579 158 ngAPEKEDRRIVGTPDYLAPEILLGQGH-GKTVDW----WSLGVILYEFLVGIPPFHAETPEEIF-------QNILNGKI 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 75570321 257 PsqWRRF---TDESLRMFRKLLALEQERR---CSVKEVFAH 291
Cdd:cd05579 226 E--WPEDpevSDEAKDLISKLLTPDPEKRlgaKGIEEIKNH 264
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
32-296 5.49e-32

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: 121.43  E-value: 5.49e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIH----KIRGSKMALKFLKKKSTKLKSFL-REYSISLYLSPcPFIINMFGIaFETDEYYVFA 106
Cdd:cd14098   2 YQIIDRLGSGTFAEVKKAVEvetgKMRAIKQIVKRKVAGNDKNLQLFqREINILKSLEH-PGIVRLIDW-YEDDQHIYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 107 QEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTR--RAGSPV 184
Cdd:cd14098  80 MEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVIVKISDFGLAKviHTGTFL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 KRVSGTIPYTAPE-LCDTSKHDGFCVDYSTDVWAFGVLLFCMLTGNFPW--------EKAMPSDTFYEEfvrwqkrrtga 255
Cdd:cd14098 160 VTFCGTMAYLAPEiLMSKEQNLQGGYSNLVDMWSVGCLVYVMLTGALPFdgssqlpvEKRIRKGRYTQP----------- 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 75570321 256 vPSQWRRFTDESLRMFRKLLALEQERRCSVKEVfahLGHRW 296
Cdd:cd14098 229 -PLVDFNISEEAIDFILRLLDVDPEKRMTAAQA---LDHPW 265
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
38-231 9.30e-32

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: 120.79  E-value: 9.30e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSF----LREYSISLYLSpCPFIINMFGiAFEtDEYYV-FAQEYAPS 112
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQqehiFSEKEILEECN-SPFIVKLYR-TFK-DKKYLyMLMEYCLG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 113 GDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAGSPVKRVS--GT 190
Cdd:cd05572  78 GELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLL-DSNGY-VKLVDFGFAKKLGSGRKTWTfcGT 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 75570321 191 IPYTAPELCdTSKHDGFCVDYstdvWAFGVLLFCMLTGNFP 231
Cdd:cd05572 156 PEYVAPEII-LNKGYDFSVDY----WSLGILLYELLTGRPP 191
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
38-296 1.03e-31

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: 120.07  E-value: 1.03e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSpCPFIINMFGiAFETDEYYVFAQEYAPSGDLFD 117
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKKEAVLREISILNQLQ-HPRIIQLHE-AYESPTELVLILELCSGGELLD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 118 IIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTRR--AGSPVKRVSGTIPYTA 195
Cdd:cd14006  79 RLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQIKIIDFGLARKlnPGEELKEIFGTPEFVA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 196 PELcdtskHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYE-EFVRWQKRRTGavpsqWRRFTDESLRMFRKL 274
Cdd:cd14006 159 PEI-----VNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANiSACRVDFSEEY-----FSSVSQEAKDFIRKL 228
                       250       260
                ....*....|....*....|..
gi 75570321 275 LALEQERRCSVKEVfahLGHRW 296
Cdd:cd14006 229 LVKEPRKRPTAQEA---LQHPW 247
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
32-296 3.01e-31

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: 119.03  E-value: 3.01e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFL----REYSISLYLSPcPFIINMFGIaFETDEYYVFAQ 107
Cdd:cd14073   3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMvrirREIEIMSSLNH-PHIIRIYEV-FENKDKIVIVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRR-------- 179
Cdd:cd14073  81 EYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILL-DQNGN-AKIADFGLSNLyskdkllq 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 180 --AGSPV----KRVSGTiPYTAPELcdtskhdgfcvdystDVWAFGVLLFCMLTGnfpwekAMPSDTF-YEEFVRWQKRR 252
Cdd:cd14073 159 tfCGSPLyaspEIVNGT-PYQGPEV---------------DCWSLGVLLYTLVYG------TMPFDGSdFKRLVKQISSG 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 75570321 253 TGAVPSQwrrfTDESLRMFRKLLALEQERRCSVKEVfAHlgHRW 296
Cdd:cd14073 217 DYREPTQ----PSDASGLIRWMLTVNPKRRATIEDI-AN--HWW 253
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
31-297 3.53e-31

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: 119.03  E-value: 3.53e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  31 YYEVIRELGKGTYGKVDLVIHKIRGSKMALK---FLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIaFETDEYYVFAQ 107
Cdd:cd14071   1 FYDIERTIGKGNFAVVKLARHRITKTEVAIKiidKSQLDEENLKKIYREVQIMKMLNH-PHIIKLYQV-METKDMLYLVT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR--RAGSPVK 185
Cdd:cd14071  79 EYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLL--DANMNIKIADFGFSNffKPGELLK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 186 RVSGTIPYTAPELCDTSKHDGFCVdystDVWAFGVLLFCMLTGNFPWEkampSDTFyeefvrwQKRRTGAVPSQWR---R 262
Cdd:cd14071 157 TWCGSPPYAAPEVFEGKEYEGPQL----DIWSLGVVLYVLVCGALPFD----GSTL-------QTLRDRVLSGRFRipfF 221
                       250       260       270
                ....*....|....*....|....*....|....*
gi 75570321 263 FTDESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14071 222 MSTDCEHLIRRMLVLDPSKRLTIEQI---KKHKWM 253
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
32-291 6.22e-31

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: 118.51  E-value: 6.22e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFL----REYSIsLYLSPCPFIINMFGIaFETDEYYVFAQ 107
Cdd:cd14081   3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLmkveREIAI-MKLIEHPNVLKLYDV-YENKKYLYLVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKecRKVKLSDFGMTR--RAGSPVK 185
Cdd:cd14081  81 EYVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEK--NNIKIADFGMASlqPEGSLLE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 186 RVSGTIPYTAPELCDTSKHDGfcvdYSTDVWAFGVLLFCMLTGNFPwekampsdtFYEEFVR--WQKRRTGA--VPSQwr 261
Cdd:cd14081 159 TSCGSPHYACPEVIKGEKYDG----RKADIWSCGVILYALLVGALP---------FDDDNLRqlLEKVKRGVfhIPHF-- 223
                       250       260       270
                ....*....|....*....|....*....|
gi 75570321 262 rFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14081 224 -ISPDAQDLLRRMLEVNPEKRITIEEIKKH 252
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
32-228 7.08e-31

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: 118.11  E-value: 7.08e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPC---PFIINMFGIAF---ETDEYYVF 105
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALREIKLLKHLNDVeghPNIVKLLDVFEhrgGNHLCLVF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 106 aqEYAPSgDLFDIIP-PQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRKVKLSDFGMTRRAGSPV 184
Cdd:cd05118  81 --ELMGM-NLYELIKdYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILI-NLELGQLKLADFGLARSFTSPP 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 75570321 185 KRVS-GTIPYTAPELCDTSKHdgfcVDYSTDVWAFGVLLFCMLTG 228
Cdd:cd05118 157 YTPYvATRWYRAPEVLLGAKP----YGSSIDIWSLGCILAELLTG 197
Pkinase pfam00069
Protein kinase domain;
32-297 9.78e-31

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 116.57  E-value: 9.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321    32 YEVIRELGKGTYGKVDLVIHKIRGSKMAL---KFLKKKSTKLKSFLREYSISLYLSpCPFIINMFGiAFETDEYYVFAQE 108
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIkkiKKEKIKKKKDKNILREIKILKKLN-HPNIVRLYD-AFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   109 YAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYlhskklvhrdikpenilifdkecrkvklsdfgmtrraGSPVKRVS 188
Cdd:pfam00069  79 YVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLES-------------------------------------GSSLTTFV 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   189 GTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEEFvrwqkRRTGAVPSQWRRFTDESL 268
Cdd:pfam00069 122 GTPWYMAPEVLGGNPY-----GPKVDVWSLGCILYELLTGKPPFPGINGNEIYELII-----DQPYAFPELPSNLSEEAK 191
                         250       260
                  ....*....|....*....|....*....
gi 75570321   269 RMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:pfam00069 192 DLLKKLLKKDPSKRLTATQA---LQHPWF 217
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
32-297 1.15e-30

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: 117.62  E-value: 1.15e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALK---FLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIaFETDEYYVFAQE 108
Cdd:cd14072   2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKiidKTQLNPSSLQKLFREVRIMKILNH-PNIVKLFEV-IETEKTLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECrKVKLSDFGMTR--RAGSPVKR 186
Cdd:cd14072  80 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLL-DADM-NIKIADFGFSNefTPGNKLDT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 187 VSGTIPYTAPELCDTSKHDGFCVdystDVWAFGVLLFCMLTGNFPWEKAMPSDtFYEEFVRWQKRrtgaVPsqWRRFTD- 265
Cdd:cd14072 158 FCGSPPYAAPELFQGKKYDGPEV----DVWSLGVILYTLVSGSLPFDGQNLKE-LRERVLRGKYR----IP--FYMSTDc 226
                       250       260       270
                ....*....|....*....|....*....|..
gi 75570321 266 ESLrmFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14072 227 ENL--LKKFLVLNPSKRGTLEQI---MKDRWM 253
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
32-291 1.21e-30

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: 117.75  E-value: 1.21e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMA----LKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFGIAFETDEYYVfAQ 107
Cdd:cd14079   4 YILGKTLGVGSFGKVKLAEHELTGHKVAvkilNRQKIKSLDMEEKIRREIQI-LKLFRHPHIIRLYEVIETPTDIFM-VM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR--RAGSPVK 185
Cdd:cd14079  82 EYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLL--DSNMNVKIADFGLSNimRDGEFLK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 186 RVSGTIPYTAPELCDTSKHDGFCVdystDVWAFGVLLFCMLTGNFPwekampsdtFYEEFVR--WQKRRTG--AVPSQwr 261
Cdd:cd14079 160 TSCGSPNYAAPEVISGKLYAGPEV----DVWSCGVILYALLCGSLP---------FDDEHIPnlFKKIKSGiyTIPSH-- 224
                       250       260       270
                ....*....|....*....|....*....|
gi 75570321 262 rFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14079 225 -LSPGARDLIKRMLVVDPLKRITIPEIRQH 253
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
74-291 1.49e-30

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: 117.84  E-value: 1.49e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  74 LREYSISLYLSPCPFIINMFGIaFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRD 153
Cdd:cd14093  56 RREIEILRQVSGHPNIIELHDV-FESPTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRD 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 154 IKPENILIFDKEcrKVKLSDFGMTRR--AGSPVKRVSGTIPYTAPELCDTSKHDGFcVDYS--TDVWAFGVLLFCMLTGN 229
Cdd:cd14093 135 LKPENILLDDNL--NVKISDFGFATRldEGEKLRELCGTPGYLAPEVLKCSMYDNA-PGYGkeVDMWACGVIMYTLLAGC 211
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75570321 230 FPWekampsdtfyeefvrWQKR-----------RTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14093 212 PPF---------------WHRKqmvmlrnimegKYEFGSPEWDDISDTAKDLISKLLVVDPKKRLTAEEALEH 269
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
32-289 2.23e-30

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: 117.32  E-value: 2.23e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLV----------------IHKIRGSKMALKflkkkstklksfLREYSISLYLSPcPFIINMFGI 95
Cdd:cd05581   3 FKFGKPLGEGSYSTVVLAkeketgkeyaikvldkRHIIKEKKVKYV------------TIEKEVLSRLAH-PGIVKLYYT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  96 AFETDEYYvFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILiFDKECRkVKLSDFG 175
Cdd:cd05581  70 FQDESKLY-FVLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENIL-LDEDMH-IKITDFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 176 ------------------------MTRRAGSPVkrvsGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:cd05581 147 takvlgpdsspestkgdadsqiayNQARAASFV----GTAEYVSPELLNEKP-----AGKSSDLWALGCIIYQMLTGKPP 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 232 WEkampSDTFYEEFVRWQKRRtgavPSQWRRFTDESLRMFRKLLALEQERRCSVKEVF 289
Cdd:cd05581 218 FR----GSNEYLTFQKIVKLE----YEFPENFPPDAKDLIQKLLVLDPSKRLGVNENG 267
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
31-246 2.58e-30

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: 117.07  E-value: 2.58e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  31 YYEVIRELGKGTYGKVDLVIHKIRGSKMA--------LKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIaFETDEY 102
Cdd:cd13993   1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAikclyksgPNSKDGNDFQKLPQLREIDLHRRVSRHPNIITLHDV-FETEVA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 103 YVFAQEYAPSGDLFDIIPPQ---VGLPEPVaKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRkVKLSDFGM-TR 178
Cdd:cd13993  80 IYIVLEYCPNGDLFEAITENriyVGKTELI-KNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGT-VKLCDFGLaTT 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 179 RAGSPVKRVsGTIPYTAPELCDTSKHDG-FCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSD-TFYEEFV 246
Cdd:cd13993 158 EKISMDFGV-GSEFYMAPECFDEVGRSLkGYPCAAGDIWSLGIILLNLTFGRNPWKIASESDpIFYDYYL 226
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
32-296 9.41e-30

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: 115.19  E-value: 9.41e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMAL----KFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFGIAFETDEYYvFAQ 107
Cdd:cd14663   2 YELGRTLGEGTFAKVKFARNTKTGESVAIkiidKEQVAREGMVEQIKREIAI-MKLLRHPNIVELHEVMATKTKIF-FVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMT-----RRAGS 182
Cdd:cd14663  80 ELVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDG--NLKISDFGLSalseqFRQDG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 183 PVKRVSGTIPYTAPELCDTSKHDGFcvdySTDVWAFGVLLFCMLTGNFPWE---------KAMPSDTfyeEFVRWqkrrt 253
Cdd:cd14663 158 LLHTTCGTPNYVAPEVLARRGYDGA----KADIWSCGVILFVLLAGYLPFDdenlmalyrKIMKGEF---EYPRW----- 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 75570321 254 gavpsqwrrFTDESLRMFRKLLALEQERRCSVKEVFAhlgHRW 296
Cdd:cd14663 226 ---------FSPGAKSLIKRILDPNPSTRITVEQIMA---SPW 256
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
28-297 1.65e-29

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: 114.76  E-value: 1.65e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  28 VNKYYEVI-RELGKGTYGKVDLVIHKIRGSKMALK---FLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIaFETDEYY 103
Cdd:cd14106   5 INEVYTVEsTPLGRGKFAVVRKCIHKETGKEYAAKflrKRRRGQDCRNEILHEIAVLELCKDCPRVVNLHEV-YETRSEL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 104 VFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI-FDKECRKVKLSDFGMTR--RA 180
Cdd:cd14106  84 ILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtSEFPLGDIKLCDFGISRviGE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 181 GSPVKRVSGTIPYTAPELCdtsKHDGFCVdySTDVWAFGVLLFCMLTGNFPWekamPSDTFYEEFVRWQKRRTGAVPSQW 260
Cdd:cd14106 164 GEEIREILGTPDYVAPEIL---SYEPISL--ATDMWSIGVLTYVLLTGHSPF----GGDDKQETFLNISQCNLDFPEELF 234
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 75570321 261 RRFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14106 235 KDVSPLAIDFIKRLLVKDPEKRLTAKEC---LEHPWL 268
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
28-297 6.51e-29

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: 112.86  E-value: 6.51e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  28 VNKYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKS--------TKLKSFLREYSislylspCPFIINMFGIaFET 99
Cdd:cd14078   1 LLKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKAlgddlprvKTEIEALKNLS-------HQHICRLYHV-IET 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 100 DEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKEcRKVKLSDFGMTRR 179
Cdd:cd14078  73 DNKIFMVLEYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLL-DED-QNLKLIDFGLCAK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 180 ----AGSPVKRVSGTIPYTAPELCDTSKHDGfcvdYSTDVWAFGVLLFCMLTGNFPWEkampsDTFYEEFVRWQKRRTGA 255
Cdd:cd14078 151 pkggMDHHLETCCGSPAYAAPELIQGKPYIG----SEADVWSMGVLLYALLCGFLPFD-----DDNVMALYRKIQSGKYE 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 75570321 256 VPSqWrrFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14078 222 EPE-W--LSPSSKLLLDQMLQVDPKKRITVKEL---LNHPWV 257
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
32-291 8.37e-29

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: 112.73  E-value: 8.37e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGS----KMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFgIAFETDEYYVFAQ 107
Cdd:cd05578   2 FQILRVIGKGSFGKVCIVQKKDTKKmfamKYMNKQKCIEKDSVRNVLNELEILQELEH-PFLVNLW-YSFQDEEDMYMVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILiFDKECRkVKLSDFGMTR--RAGSPVK 185
Cdd:cd05578  80 DLLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNIL-LDEQGH-VHITDFNIATklTDGTLAT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 186 RVSGTIPYTAPELCDTSKHdGFCVDYstdvWAFGVLLFCMLTGNFPWEkaMPSDTFYEEFVRWQKRRTGAVPSQWrrftD 265
Cdd:cd05578 158 STSGTKPYMAPEVFMRAGY-SFAVDW----WSLGVTAYEMLRGKRPYE--IHSRTSIEEIRAKFETASVLYPAGW----S 226
                       250       260
                ....*....|....*....|....*...
gi 75570321 266 ESLRMF-RKLLALE-QERRCSVKEVFAH 291
Cdd:cd05578 227 EEAIDLiNKLLERDpQKRLGDLSDLKNH 254
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
32-297 1.24e-28

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: 112.54  E-value: 1.24e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMA----------------LKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGI 95
Cdd:cd14077   3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAikiiprasnaglkkerEKRLEKEISRDIRTIREAALSSLLNH-PHICRLRDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  96 AFETDEYY-VFaqEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDF 174
Cdd:cd14077  82 LRTPNHYYmLF--EYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILI--SKSGNIKIIDF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 175 GMTR--RAGSPVKRVSGTIPYTAPELCDTSKHDGFCVdystDVWAFGVLLFCMLTGNFPW-EKAMPsdtfyeefVRWQKR 251
Cdd:cd14077 158 GLSNlyDPRRLLRTFCGSLYFAAPELLQAQPYTGPEV----DVWSFGVVLYVLVCGKVPFdDENMP--------ALHAKI 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 75570321 252 RTGAV--PSQwrrFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14077 226 KKGKVeyPSY---LSSECKSLISRMLVVDPKKRATLEQV---LNHPWM 267
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
31-297 1.53e-28

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: 112.09  E-value: 1.53e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  31 YYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLR---------EYSI--SLYLSPCPFIINMFGIaFET 99
Cdd:cd14004   1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDTWVRdrklgtvplEIHIldTLNKRSHPNIVKLLDF-FED 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 100 DEYYVFAQEYAPSG-DLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTR 178
Cdd:cd14004  80 DEFYYLVMEKHGSGmDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGT--IKLIDFGSAA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 179 --RAGsPVKRVSGTIPYTAPELCDTSKHDGfcvdYSTDVWAFGVLLFCMLTGNFPwekampsdtFY--EEFVRWQKRRTG 254
Cdd:cd14004 158 yiKSG-PFDTFVGTIDYAAPEVLRGNPYGG----KEQDIWALGVLLYTLVFKENP---------FYniEEILEADLRIPY 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 75570321 255 AVpsqwrrfTDESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14004 224 AV-------SEDLIDLISRMLNRDVGDRPTIEEL---LTDPWL 256
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
33-246 1.86e-28

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: 112.52  E-value: 1.86e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  33 EVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKK--STKLKSFLREYSISLYLSPCPFIINMFGIAFETDEYYVFAQEYA 110
Cdd:cd06617   4 EVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATvnSQEQKRLLMDLDISMRSVDCPYTVTFYGALFREGDVWICMEVMD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGDLF--DIIPPQVGLPEPVAKRCVHQVAIALEYLHSK-KLVHRDIKPENILIfdKECRKVKLSDFGMTrraGSPVKRV 187
Cdd:cd06617  84 TSLDKFykKVYDKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLI--NRNGQVKLCDFGIS---GYLVDSV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 188 SGTI-----PYTAPELCD-TSKHDGFcvDYSTDVWAFGVLLFCMLTGNFPWEK-----------------AMPSDTFYEE 244
Cdd:cd06617 159 AKTIdagckPYMAPERINpELNQKGY--DVKSDVWSLGITMIELATGRFPYDSwktpfqqlkqvveepspQLPAEKFSPE 236

                ..
gi 75570321 245 FV 246
Cdd:cd06617 237 FQ 238
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
20-282 9.73e-28

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 111.45  E-value: 9.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   20 AQNLEKLEVNKY----YEVIRELGKGTYGKVDLVIHKIRGSKMA----LKFLKKKSTKLKSFLREYSISLYLSPcPFIIN 91
Cdd:PTZ00263   4 AYMFTKPDTSSWklsdFEMGETLGTGSFGRVRIAKHKGTGEYYAikclKKREILKMKQVQHVAQEKSILMELSH-PFIVN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   92 MFgIAFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKL 171
Cdd:PTZ00263  83 MM-CSFQDENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKG--HVKV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  172 SDFGMTRRAGSPVKRVSGTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPwekampsdtFYEE--FVRWQ 249
Cdd:PTZ00263 160 TDFGFAKKVPDRTFTLCGTPEYLAPEVIQSKGHGK-----AVDWWTMGVLLYEFIAGYPP---------FFDDtpFRIYE 225
                        250       260       270
                 ....*....|....*....|....*....|....
gi 75570321  250 KRRTGAVpsQWRRFTDESLRMFRK-LLALEQERR 282
Cdd:PTZ00263 226 KILAGRL--KFPNWFDGRARDLVKgLLQTDHTKR 257
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
33-243 2.08e-27

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: 108.97  E-value: 2.08e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  33 EVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSF--LREYSIsLYLSPCPFIINMFGiAFETDEYYVFAQEYA 110
Cdd:cd06605   4 EYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQKqiLRELDV-LHKCNSPYIVGFYG-AFYSEGDISICMEYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSK-KLVHRDIKPENILIFDKEcrKVKLSDFGM-TRRAGSPVKRVS 188
Cdd:cd06605  82 DGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRG--QVKLCDFGVsGQLVDSLAKTFV 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75570321 189 GTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPW--EKAMPSDTFYE 243
Cdd:cd06605 160 GTRSYMAPERISGGKY-----TVKSDIWSLGLSLVELATGRFPYppPNAKPSMMIFE 211
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
32-291 4.76e-27

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: 108.68  E-value: 4.76e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIH-KIRGSKMA--------LKFLKKKSTKLKSFLREYSISLYLSpCPFIINMFGIaFETDEY 102
Cdd:cd14096   3 YRLINKIGEGAFSNVYKAVPlRNTGKPVAikvvrkadLSSDNLKGSSRANILKEVQIMKRLS-HPNIVKLLDF-QESDEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 103 YVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENIL----IF--------------DK 164
Cdd:cd14096  81 YYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLfepiPFipsivklrkadddeTK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 165 E-------------CRKVKLSDFGMTRRA-GSPVKRVSGTIPYTAPELCdTSKHdgfcVDYSTDVWAFGVLLFCMLTGnF 230
Cdd:cd14096 161 VdegefipgvggggIGIVKLADFGLSKQVwDSNTKTPCGTVGYTAPEVV-KDER----YSKKVDMWALGCVLYTLLCG-F 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 231 PwekampsdTFYEEFVR--WQKRRTGA---VPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14096 235 P--------PFYDESIEtlTEKISRGDytfLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAH 292
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
86-297 6.27e-27

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: 107.71  E-value: 6.27e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  86 CPFIINMFGiAFETDEYYVFAQEY-APSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDK 164
Cdd:cd14005  65 VPGVIRLLD-WYERPDGFLLIMERpEPCQDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLI-NL 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 165 ECRKVKLSDFGmtrrAGSPVKR-----VSGTIPYTAPELCDTSKHDGfcvdYSTDVWAFGVLLFCMLTGNFPWEkampSD 239
Cdd:cd14005 143 RTGEVKLIDFG----CGALLKDsvytdFDGTRVYSPPEWIRHGRYHG----RPATVWSLGILLYDMLCGDIPFE----ND 210
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 240 tfyEEFVRWQkrrtgavPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAhlgHRWM 297
Cdd:cd14005 211 ---EQILRGN-------VLFRPRLSKECCDLISRCLQFDPSKRPSLEQILS---HPWF 255
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
38-233 7.17e-27

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: 107.24  E-value: 7.17e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHkiRGSKMA---LKFLKKKSTKLKSFLREYSIslyLSPC--PFIINMFGIAFETDEYYVFAqEYAPS 112
Cdd:cd13999   1 IGSGSFGEVYKGKW--RGTDVAikkLKVEDDNDELLKEFRREVSI---LSKLrhPNIVQFIGACLSPPPLCIVT-EYMPG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 113 GDLFDII-PPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTRRAGSP---VKRVS 188
Cdd:cd13999  75 GSLYDLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFT--VKIADFGLSRIKNSTtekMTGVV 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 75570321 189 GTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd13999 153 GTPRWMAPEVLRGEP-----YTEKADVYSFGIVLWELLTGEVPFK 192
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
87-231 9.11e-27

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: 106.95  E-value: 9.11e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGiAFETDEYYVFAQEYApSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKec 166
Cdd:cd14002  60 PNIIEMLD-SFETKKEFVVVTEYA-QGELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKG-- 135
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 167 RKVKLSDFGMTRRAGSP---VKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:cd14002 136 GVVKLCDFGFARAMSCNtlvLTSIKGTPLYMAPELVQEQPY-----DHTADLWSLGCILYELFVGQPP 198
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
38-233 1.35e-26

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: 108.07  E-value: 1.35e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHK----IRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGiAFETDEYYVFAQEYAPSG 113
Cdd:cd05570   3 LGKGSFGKVMLAERKktdeLYAIKVLKKEVIIEDDDVECTMTEKRVLALANRHPFLTGLHA-CFQTEDRLYFVMEYVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAGSPVKRVS---GT 190
Cdd:cd05570  82 DLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLL-DAEGH-IKIADFGMCKEGIWGGNTTStfcGT 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 75570321 191 IPYTAPE-LCDTSKhdGFCVDYstdvWAFGVLLFCMLTGNFPWE 233
Cdd:cd05570 160 PDYIAPEiLREQDY--GFSVDW----WALGVLLYEMLAGQSPFE 197
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
31-236 1.96e-26

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: 106.13  E-value: 1.96e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  31 YYEVIRELGKGTYGKVDLVIHKIRGSKMAL-KFLKKKSTKLKSFLREYSIslyLSPC--PFIINMFGiAFETDEYYVFAQ 107
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIkKINLESKEKKESILNEIAI---LKKCkhPNIVKYYG-SYLKKDELWIVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVG-LPEP-VAKRCvHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRR--AGSP 183
Cdd:cd05122  77 EFCSGGSLKDLLKNTNKtLTEQqIAYVC-KEVLKGLEYLHSHGIIHRDIKAANILLTSDG--EVKLIDFGLSAQlsDGKT 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 184 VKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWE-----KAM 236
Cdd:cd05122 154 RNTFVGTPYWMAPEVIQGKPY-----GFKADIWSLGITAIEMAEGKPPYSelppmKAL 206
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
35-241 2.33e-26

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: 106.03  E-value: 2.33e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  35 IRELGKGTYGKVDLVIHKIRGS----KMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFgIAFETDEYYVFAQEYA 110
Cdd:cd05611   1 LKPISKGAFGSVYLAKKRSTGDyfaiKVLKKSDMIAKNQVTNVKAERAIMMIQGESPYVAKLY-YSFQSKDYLYLVMEYL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRA--GSPVKRVS 188
Cdd:cd05611  80 NGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLI--DQTGHLKLTDFGLSRNGleKRHNKKFV 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 75570321 189 GTIPYTAPELCdtskhDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTF 241
Cdd:cd05611 158 GTPDYLAPETI-----LGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVF 205
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
31-297 3.64e-26

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: 105.50  E-value: 3.64e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  31 YYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFL---REYSiSLYLSPCPFIINMFGIAfETDEYYVFAQ 107
Cdd:cd14075   3 FYRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQRllsREIS-SMEKLHHPNIIRLYEVV-ETLSKLHLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGM--TRRAGSPVK 185
Cdd:cd14075  81 EYASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNC--VKVGDFGFstHAKRGETLN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 186 RVSGTIPYTAPELcdtskhdgFCVDY----STDVWAFGVLLFCMLTGNFPwekampsdtFYEEFVRWQKRR----TGAVP 257
Cdd:cd14075 159 TFCGSPPYAAPEL--------FKDEHyigiYVDIWALGVLLYFMVTGVMP---------FRAETVAKLKKCilegTYTIP 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 75570321 258 SQwrrFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14075 222 SY---VSEPCQELIRGILQPVPSDRYSIDEI---KNSEWL 255
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
32-297 4.30e-26

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: 105.63  E-value: 4.30e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKV----------DLVIhKIRGSKMALKFLKKKSTKlksflREYSISLYLSPCPfIINMFGIaFETDE 101
Cdd:cd14165   3 YILGINLGEGSYAKVksayserlkcNVAI-KIIDKKKAPDDFVEKFLP-----RELEILARLNHKS-IIKTYEI-FETSD 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 102 YYVF-AQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECrKVKLSDFGMTRRA 180
Cdd:cd14165  75 GKVYiVMELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLL-DKDF-NIKLTDFGFSKRC 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 181 -----GSPV--KRVSGTIPYTAPEL-----CDTSKHdgfcvdystDVWAFGVLLFCMLTGNFPWEkampsDTFYEEFVRW 248
Cdd:cd14165 153 lrdenGRIVlsKTFCGSAAYAAPEVlqgipYDPRIY---------DIWSLGVILYIMVCGSMPYD-----DSNVKKMLKI 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 75570321 249 QKRRTGAVPSQwRRFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14165 219 QKEHRVRFPRS-KNLTSECKDLIYRLLQPDVSQRLCIDEV---LSHPWL 263
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
108-297 5.75e-26

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: 105.19  E-value: 5.75e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFD-IIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcRKVKLSDFGMTRR--AGSPV 184
Cdd:cd14074  82 ELGDGGDMYDyIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQ-GLVKLTDFGFSNKfqPGEKL 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 KRVSGTIPYTAPELCDTSKHDGFCVdystDVWAFGVLLFCMLTGNFPWEKAMPSDTF-------YEefvrwqkrrtgaVP 257
Cdd:cd14074 161 ETSCGSLAYSAPEILLGDEYDAPAV----DIWSLGVILYMLVCGQPPFQEANDSETLtmimdckYT------------VP 224
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 75570321 258 SQwrrFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14074 225 AH---VSPECKDLIRRMLIRDPKKRASLEEI---ENHPWL 258
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
32-291 9.14e-26

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: 104.27  E-value: 9.14e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVD---------LVIHKIRGSKMALKFLKKKSTklksflREYSISLYLSPcPFIINMFGIaFETDEY 102
Cdd:cd14161   5 YEFLETLGKGTYGRVKkardssgrlVAIKSIRKDRIKDEQDLLHIR------REIEIMSSLNH-PHIISVYEV-FENSSK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 103 YVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR--RA 180
Cdd:cd14161  77 IVIVMEYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILL--DANGNIKIADFGLSNlyNQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 181 GSPVKRVSGTIPYTAPELCDTSKHDGFCVdystDVWAFGVLLFCMLTGnfpwekAMPSDTF-YEEFVrwQKRRTGAV--P 257
Cdd:cd14161 155 DKFLQTYCGSPLYASPEIVNGRPYIGPEV----DSWSLGVLLYILVHG------TMPFDGHdYKILV--KQISSGAYreP 222
                       250       260       270
                ....*....|....*....|....*....|....
gi 75570321 258 SQwrrfTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14161 223 TK----PSDACGLIRWLLMVNPERRATLEDVASH 252
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
32-302 1.66e-25

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: 104.64  E-value: 1.66e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKsflREYSISLYLSPCPFIINMFGIaFETDEYYVFAQEYAP 111
Cdd:cd14091   2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPS---EEIEILLRYGQHPNIITLRDV-YDDGNSVYLVTELLR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 112 SGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECR--KVKLSDFGMTR--RAGspvkrv 187
Cdd:cd14091  78 GGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDpeSLRICDFGFAKqlRAE------ 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 188 SG---TIPYT----APELCdtsKHDGFcvDYSTDVWAFGVLLFCMLTGNFPWeKAMPSDTFYEEFVRWQKRRTGAVPSQW 260
Cdd:cd14091 152 NGllmTPCYTanfvAPEVL---KKQGY--DAACDIWSLGVLLYTMLAGYTPF-ASGPNDTPEVILARIGSGKIDLSGGNW 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 75570321 261 RRFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWMLDGTS 302
Cdd:cd14091 226 DHVSDSAKDLVRKMLHVDPSQRPTAAQV---LQHPWIRNRDS 264
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
108-281 2.19e-25

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: 103.53  E-value: 2.19e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILiFDKECRkVKLSDFGMTRRAGSPV--- 184
Cdd:cd14162  80 ELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLL-LDKNNN-LKITDFGFARGVMKTKdgk 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 KRVS----GTIPYTAPELCDTSKHDGFCvdysTDVWAFGVLLFCMLTGNFPWekampSDTFYEEFVRwQKRRTGAVPSQw 260
Cdd:cd14162 158 PKLSetycGSYAYASPEILRGIPYDPFL----SDIWSMGVVLYTMVYGRLPF-----DDSNLKVLLK-QVQRRVVFPKN- 226
                       170       180
                ....*....|....*....|.
gi 75570321 261 RRFTDESLRMFRKLLALEQER 281
Cdd:cd14162 227 PTVSEECKDLILRMLSPVKKR 247
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
32-242 2.51e-25

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


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 104.63  E-value: 2.51e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLR----EYSIsLYLSPCPFIINMFGiAFETDEYYVFAQ 107
Cdd:cd05574   3 FKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKrvltEREI-LATLDHPFLPTLYA-SFQTSTHLCFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVG--LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAGSPVK 185
Cdd:cd05574  81 DYCPGGELFRLLQKQPGkrLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILL--HESGHIMLTDFDLSKQSSVTPP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 186 RVS--------------------------------GTIPYTAPELCDTSKHdGFCVDYstdvWAFGVLLFCMLTGNFPWE 233
Cdd:cd05574 159 PVRkslrkgsrrssvksieketfvaepsarsnsfvGTEEYIAPEVIKGDGH-GSAVDW----WTLGILLYEMLYGTTPFK 233

                ....*....
gi 75570321 234 KAMPSDTFY 242
Cdd:cd05574 234 GSNRDETFS 242
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
32-291 4.65e-25

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: 102.42  E-value: 4.65e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSIS-LYLSPCPFIINMFGIAFETDEYYVfAQEYA 110
Cdd:cd14184   3 YKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHLIENEVSiLRRVKHPNIIMLIEEMDTPAELYL-VMELV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI--FDKECRKVKLSDFGMTRRAGSPVKRVS 188
Cdd:cd14184  82 KGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceYPDGTKSLKLGDFGLATVVEGPLYTVC 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 189 GTIPYTAPELCDTSKHdGFCVdystDVWAFGVLLFCMLTGNFPW--EKAMPSDTFYEEFVRWQKrrtgaVPSQ-WRRFTD 265
Cdd:cd14184 162 GTPTYVAPEIIAETGY-GLKV----DIWAAGVITYILLCGFPPFrsENNLQEDLFDQILLGKLE-----FPSPyWDNITD 231
                       250       260
                ....*....|....*....|....*.
gi 75570321 266 ESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14184 232 SAKELISHMLQVNVEARYTAEQILSH 257
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
32-291 6.23e-25

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: 102.34  E-value: 6.23e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHK----IRGSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIAFETDEYYVFAq 107
Cdd:cd14116   7 FEIGRPLGKGKFGNVYLAREKqskfILALKVLFKAQLEKAGVEHQLRREVEIQSHLRH-PNILRLYGYFHDATRVYLIL- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAGSPVKR- 186
Cdd:cd14116  85 EYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLL--GSAGELKIADFGWSVHAPSSRRTt 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 187 VSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWEkampSDTFYEEFvrwqkRRTGAVPSQWRRFTDE 266
Cdd:cd14116 163 LCGTLDYLPPEMIEGRMH-----DEKVDLWSLGVLCYEFLVGKPPFE----ANTYQETY-----KRISRVEFTFPDFVTE 228
                       250       260
                ....*....|....*....|....*.
gi 75570321 267 SLR-MFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14116 229 GARdLISRLLKHNPSQRPMLREVLEH 254
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
32-232 1.24e-24

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: 102.10  E-value: 1.24e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRG----SKMALKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFgIAFETDEYYVFAQ 107
Cdd:cd14209   3 FDRIKTLGTGSFGRVMLVRHKETGnyyaMKILDKQKVVKLKQVEHTLNEKRI-LQAINFPFLVKLE-YSFKDNSNLYMVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKEcRKVKLSDFGMTRRAGSPVKRV 187
Cdd:cd14209  81 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLI-DQQ-GYIKVTDFGFAKRVKGRTWTL 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 75570321 188 SGTIPYTAPELCdTSKHDGFCVDYstdvWAFGVLLFCMLTGNFPW 232
Cdd:cd14209 159 CGTPEYLAPEII-LSKGYNKAVDW----WALGVLIYEMAAGYPPF 198
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
87-282 1.66e-24

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


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 102.38  E-value: 1.66e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGiAFETDEYYVFAQEYAPSGDLFDIIPPQVgLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKEc 166
Cdd:cd05589  62 PFLVNLFA-CFQTPEHVCFVMEYAAGGDLMMHIHEDV-FSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLL-DTE- 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 167 RKVKLSDFGMTRRAGSPVKRVS---GTIPYTAPE-LCDTSkhdgfcVDYSTDVWAFGVLLFCMLTGNFPWekamPSDTFY 242
Cdd:cd05589 138 GYVKIADFGLCKEGMGFGDRTStfcGTPEFLAPEvLTDTS------YTRAVDWWGLGVLIYEMLVGESPF----PGDDEE 207
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75570321 243 EEF-------VRWqkrrtgavPsqwRRFTDESLRMFRKLLALEQERR 282
Cdd:cd05589 208 EVFdsivndeVRY--------P---RFLSTEAISIMRRLLRKNPERR 243
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
87-243 1.71e-24

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: 101.09  E-value: 1.71e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321     87 PFIINMFGIAFETDEYYVfAQEYAPSGDLFDIIPPQVGLPEPVAKRC--VHQVAIALEYLHSKKLVHRDIKPENILIFDK 164
Cdd:smart00221  61 PNIVKLLGVCTEEEPLMI-VMEYMPGGDLLDYLRKNRPKELSLSDLLsfALQIARGMEYLESKNFIHRDLAARNCLVGEN 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321    165 ecRKVKLSDFGMTRRAGS-PVKRVSGT-IPY--TAPE-LCD---TSKhdgfcvdysTDVWAFGVLLFCMLT-GNFPWEkA 235
Cdd:smart00221 140 --LVVKISDFGLSRDLYDdDYYKVKGGkLPIrwMAPEsLKEgkfTSK---------SDVWSFGVLLWEIFTlGEEPYP-G 207

                   ....*...
gi 75570321    236 MPSDTFYE 243
Cdd:smart00221 208 MSNAEVLE 215
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
87-296 4.45e-24

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: 99.79  E-value: 4.45e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIaFETDEYyVFAQEYAPSGDLFDII--PPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIF-D 163
Cdd:cd14082  62 PGVVNLECM-FETPER-VFVVMEKLHGDMLEMIlsSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLAsA 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 164 KECRKVKLSDFGMTRRAG--SPVKRVSGTIPYTAPELCdtsKHDGFcvDYSTDVWAFGVLLFCMLTGNFPWEKampsdtf 241
Cdd:cd14082 140 EPFPQVKLCDFGFARIIGekSFRRSVVGTPAYLAPEVL---RNKGY--NRSLDMWSVGVIIYVSLSGTFPFNE------- 207
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75570321 242 yEEFVRWQKRRTGAV--PSQWRRFTDESLRMFRKLLALEQERRCSVKEVfahLGHRW 296
Cdd:cd14082 208 -DEDINDQIQNAAFMypPNPWKEISPDAIDLINNLLQVKMRKRYSVDKS---LSHPW 260
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
32-282 4.56e-24

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: 100.59  E-value: 4.56e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGS----KMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFgiAFETDEYYVFA- 106
Cdd:cd05612   3 FERIKTIGTGTFGRVHLVRDRISEHyyalKVMAIPEVIRLKQEQHVHNEKRVLKEVSH-PFIIRLF--WTEHDQRFLYMl 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 107 QEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAGSPVKR 186
Cdd:cd05612  80 MEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILL-DKEGH-IKLTDFGFAKKLRDRTWT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 187 VSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFyeefvrwQKRRTGAVpsQWRRFTDE 266
Cdd:cd05612 158 LCGTPEYLAPEVIQSKGH-----NKAVDWWALGILIYEMLVGYPPFFDDNPFGIY-------EKILAGKL--EFPRHLDL 223
                       250
                ....*....|....*..
gi 75570321 267 SLR-MFRKLLALEQERR 282
Cdd:cd05612 224 YAKdLIKKLLVVDRTRR 240
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
87-234 9.06e-24

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 99.16  E-value: 9.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   87 PFIINMFgIAFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILiFDKEC 166
Cdd:PHA03390  69 PNFIKLY-YSVTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVL-YDRAK 146
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321  167 RKVKLSDFGMTRRAGSPVKRvSGTIPYTAPElcdtsKHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEK 234
Cdd:PHA03390 147 DRIYLCDYGLCKIIGTPSCY-DGTLDYFSPE-----KIKGHNYDVSFDWWAVGVLTYELLTGKHPFKE 208
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
98-291 1.07e-23

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: 98.45  E-value: 1.07e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  98 ETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKV-KLSDFGM 176
Cdd:cd14009  62 KTEDFIYLVLEYCAGGDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPVlKIADFGF 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 177 TRR----------AGSPVkrvsgtipYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWEKAMPSdtfyeEFV 246
Cdd:cd14009 142 ARSlqpasmaetlCGSPL--------YMAPEILQFQKYDA-----KADLWSVGAILFEMLVGKPPFRGSNHV-----QLL 203
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75570321 247 RWQKRRTGAVPSQWRRFTDESLR-MFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14009 204 RNIERSDAVIPFPIAAQLSPDCKdLLRRLLRRDPAERISFEEFFAH 249
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
87-232 1.21e-23

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: 98.91  E-value: 1.21e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVFaQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEC 166
Cdd:cd06626  59 PNLVRYYGVEVHREEVYIF-MEYCQEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGL 137
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75570321 167 rkVKLSDFGM--------TRRAGSPVKRVSGTIPYTAPELCDTSKHDGFcvDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd06626 138 --IKLGDFGSavklknntTTMAPGEVNSLVGTPAYMAPEVITGNKGEGH--GRAADIWSLGCVVLEMATGKRPW 207
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
35-232 1.23e-23

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 98.72  E-value: 1.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321    35 IRELGKGTYGKVDLVIHKIRGSKMALK------FLKKKSTKLKSFLREYSISLYLSpCPFIINMFGIAFETDEYYVFaQE 108
Cdd:pfam07714   4 GEKLGEGAFGEVYKGTLKGEGENTKIKvavktlKEGADEEEREDFLEEASIMKKLD-HPNIVKLLGVCTQGEPLYIV-TE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   109 YAPSGDLFDII---PPQVGLPEPVakRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR---RAGS 182
Cdd:pfam07714  82 YMPGGDLLDFLrkhKRKLTLKDLL--SMALQIAKGMEYLESKNFVHRDLAARNCLV--SENLVVKISDFGLSRdiyDDDY 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 75570321   183 PVKRVSGTIP--YTAPELCDTSKhdgfcvdYST--DVWAFGVLLFCMLT-GNFPW 232
Cdd:pfam07714 158 YRKRGGGKLPikWMAPESLKDGK-------FTSksDVWSFGVLLWEIFTlGEQPY 205
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
89-243 1.25e-23

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 98.37  E-value: 1.25e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321     89 IINMFGIAFETDEYYVfAQEYAPSGDLFDII---PPQVGLPEPVAkrCVHQVAIALEYLHSKKLVHRDIKPENILIFDKe 165
Cdd:smart00219  63 VVKLLGVCTEEEPLYI-VMEYMEGGDLLSYLrknRPKLSLSDLLS--FALQIARGMEYLESKNFIHRDLAARNCLVGEN- 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321    166 cRKVKLSDFGMTRRAGS-PVKRVSGT-IPY--TAPE-LCD---TSKhdgfcvdysTDVWAFGVLLFCMLT-GNFPWEkAM 236
Cdd:smart00219 139 -LVVKISDFGLSRDLYDdDYYRKRGGkLPIrwMAPEsLKEgkfTSK---------SDVWSFGVLLWEIFTlGEQPYP-GM 207

                   ....*..
gi 75570321    237 PSDTFYE 243
Cdd:smart00219 208 SNEEVLE 214
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
87-232 1.79e-23

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: 98.24  E-value: 1.79e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVFAqEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKEC 166
Cdd:cd06632  62 PNIVQYYGTEREEDNLYIFL-EYVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILV-DTNG 139
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 167 RkVKLSDFGMTRR--AGSPVKRVSGTIPYTAPELCDtSKHDGFcvDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd06632 140 V-VKLADFGMAKHveAFSFAKSFKGSPYWMAPEVIM-QKNSGY--GLAVDIWSLGCTVLEMATGKPPW 203
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
32-291 1.84e-23

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: 98.76  E-value: 1.84e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMA--LKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIAFETDE-YYVFaqE 108
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAikKMKKKFYSWEECMNLREVKSLRKLNEHPNIVKLKEVFRENDElYFVF--E 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPsGDLFDIIPPQVG--LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTR--RAGSPV 184
Cdd:cd07830  79 YME-GNLYQLMKDRKGkpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEV--VKIADFGLAReiRSRPPY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 KRVSGTIPYTAPELCDTSKHdgfcvdYST--DVWAFGVLLFCMLTGN--FPWEKAMpsDTFY-----------EEFVRWQ 249
Cdd:cd07830 156 TDYVSTRWYRAPEILLRSTS------YSSpvDIWALGCIMAELYTLRplFPGSSEI--DQLYkicsvlgtptkQDWPEGY 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 75570321 250 K--RRTG-----AVPSQWRRF----TDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07830 228 KlaSKLGfrfpqFAPTSLHQLipnaSPEAIDLIKDMLRWDPKKRPTASQALQH 280
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
32-232 2.01e-23

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: 100.85  E-value: 2.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHK----IRGSKMALKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFgIAFETDEYYVFAQ 107
Cdd:cd05622  75 YEVVKVIGRGAFGEVQLVRHKstrkVYAMKLLSKFEMIKRSDSAFFWEERDI-MAFANSPWVVQLF-YAFQDDRYLYMVM 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPpQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFG----MTRRAGSP 183
Cdd:cd05622 153 EYMPGGDLVNLMS-NYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLL-DKSGH-LKLADFGtcmkMNKEGMVR 229
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 75570321 184 VKRVSGTIPYTAPELCDTSKHDGFcVDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd05622 230 CDTAVGTPDYISPEVLKSQGGDGY-YGRECDWWSVGVFLYEMLVGDTPF 277
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
32-298 2.29e-23

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: 99.71  E-value: 2.29e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKsflREYSISLYLSPCPFIINMFGIaFETDEYYVFAQEYAP 111
Cdd:cd14176  21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT---EEIEILLRYGQHPNIITLKDV-YDDGKYVYVVTELMK 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 112 SGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEC--RKVKLSDFGMTR--RAGSPVKRV 187
Cdd:cd14176  97 GGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGnpESIRICDFGFAKqlRAENGLLMT 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 188 SG-TIPYTAPELCDTSKHDGFCvdystDVWAFGVLLFCMLTGNFPWEKAmPSDTFYEEFVRWQKRRTGAVPSQWRRFTDE 266
Cdd:cd14176 177 PCyTANFVAPEVLERQGYDAAC-----DIWSLGVLLYTMLTGYTPFANG-PDDTPEEILARIGSGKFSLSGGYWNSVSDT 250
                       250       260       270
                ....*....|....*....|....*....|..
gi 75570321 267 SLRMFRKLLALEQERRCSVKEVfahLGHRWML 298
Cdd:cd14176 251 AKDLVSKMLHVDPHQRLTAALV---LRHPWIV 279
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
32-291 2.91e-23

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: 98.01  E-value: 2.91e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLV----IHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIAFETDEYYVFAq 107
Cdd:cd14117   8 FDIGRPLGKGKFGNVYLArekqSKFIVALKVLFKSQIEKEGVEHQLRREIEIQSHLRH-PNILRLYNYFHDRKRIYLIL- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRAGSPVKR- 186
Cdd:cd14117  86 EYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKG--ELKIADFGWSVHAPSLRRRt 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 187 VSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFyeefvrwqkRRTGAVPSQWRRFTDE 266
Cdd:cd14117 164 MCGTLDYLPPEMIEGRTH-----DEKVDLWCIGVLCYELLVGMPPFESASHTETY---------RRIVKVDLKFPPFLSD 229
                       250       260
                ....*....|....*....|....*.
gi 75570321 267 SLR-MFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14117 230 GSRdLISKLLRYHPSERLPLKGVMEH 255
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
29-225 3.51e-23

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: 97.89  E-value: 3.51e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  29 NKYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLksfLREYSISL-YLSPC--PFIINMFGIAFETDEYYVF 105
Cdd:cd06611   4 NDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIESEEE---LEDFMVEIdILSECkhPNIVGLYEAYFYENKLWIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 106 AqEYAPSGDLFDIIPP-QVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI-FDKEcrkVKLSDFGMTRRAGSP 183
Cdd:cd06611  81 I-EFCDGGALDSIMLElERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLtLDGD---VKLADFGVSAKNKST 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75570321 184 VKRVS---GTIPYTAPEL--CDTSKHDGFcvDYSTDVWAFGVLLFCM 225
Cdd:cd06611 157 LQKRDtfiGTPYWMAPEVvaCETFKDNPY--DYKADIWSLGITLIEL 201
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
30-233 4.79e-23

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: 96.85  E-value: 4.79e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  30 KYYEVIRELGKGTYGKV----DLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGiAFETDEYYVF 105
Cdd:cd14099   1 KRYRRGKFLGKGGFAKCyevtDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLKH-PNIVKFHD-CFEDEENVYI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 106 AQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKecRKVKLSDFGMTRRAGSPVK 185
Cdd:cd14099  79 LLELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDEN--MNVKIGDFGLAARLEYDGE 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75570321 186 R---VSGTIPYTAPELCDTSKHDGFCVdystDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd14099 157 RkktLCGTPNYIAPEVLEKKKGHSFEV----DIWSLGVILYTLLVGKPPFE 203
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
32-321 5.06e-23

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: 97.78  E-value: 5.06e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKsflREYSISLYLSPCPFIINMFGIaFETDEYYVFAQEYAP 111
Cdd:cd14178   5 YEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPS---EEIEILLRYGQHPNIITLKDV-YDDGKFVYLVMELMR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 112 SGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDK--ECRKVKLSDFGMTR--RAGSPVKRV 187
Cdd:cd14178  81 GGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDEsgNPESIRICDFGFAKqlRAENGLLMT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 188 SG-TIPYTAPELCDTSKHDGFCvdystDVWAFGVLLFCMLTGNFPWEKAmPSDTFYEEFVRWQKRRTGAVPSQWRRFTDE 266
Cdd:cd14178 161 PCyTANFVAPEVLKRQGYDAAC-----DIWSLGILLYTMLAGFTPFANG-PDDTPEEILARIGSGKYALSGGNWDSISDA 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 267 SLRMFRKLLALEQERRCSVKEVfahLGHRWMLdgtsgNHHQSVLNSSSEEDELLV 321
Cdd:cd14178 235 AKDIVSKMLHVDPHQRLTAPQV---LRHPWIV-----NREYLSQNQLSRQDVHLV 281
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
36-241 5.18e-23

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: 97.30  E-value: 5.18e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  36 RELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKL---KSFLREYSISLYLSPCPFIINMFGIaFETDEYYVFAQEYAPS 112
Cdd:cd14198  14 KELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQdcrAEILHEIAVLELAKSNPRVVNLHEV-YETTSEIILILEYAAG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 113 GDLFDIIPPQVG--LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFD-KECRKVKLSDFGMTRRAGSP--VKRV 187
Cdd:cd14198  93 GEIFNLCVPDLAemVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSiYPLGDIKIVDFGMSRKIGHAceLREI 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 75570321 188 SGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTF 241
Cdd:cd14198 173 MGTPEYLAPEILNYDP-----ITTATDMWNIGVIAYMLLTHESPFVGEDNQETF 221
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
38-233 6.08e-23

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: 97.86  E-value: 6.08e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLViHKIRGSKMALKFLKKKSTKLKSFLR-------EYSIsLYLSPCPFIINMFgIAFETDEYYVFAQEYA 110
Cdd:cd05582   3 LGQGSFGKVFLV-RKITGPDAGTLYAMKVLKKATLKVRdrvrtkmERDI-LADVNHPFIVKLH-YAFQTEGKLYLILDFL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAGSPVKRV--- 187
Cdd:cd05582  80 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL--DEDGHIKLTDFGLSKESIDHEKKAysf 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75570321 188 SGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd05582 158 CGTVEYMAPEVVNRRGH-----TQSADWWSFGVLMFEMLTGSLPFQ 198
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
38-291 6.85e-23

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: 96.96  E-value: 6.85e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALK---------FLKKKSTKLKSFLREYSISLYLSPCPFIINMFGiAFETDEYYVFAQE 108
Cdd:cd14181  18 IGRGVSSVVRRCVHRHTGQEFAVKiievtaerlSPEQLEEVRSSTLKEIHILRQVSGHPSIITLID-SYESSTFIFLVFD 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDkeCRKVKLSDFGMT--RRAGSPVKR 186
Cdd:cd14181  97 LMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDD--QLHIKLSDFGFSchLEPGEKLRE 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 187 VSGTIPYTAPELCDTS---KHDGFcvDYSTDVWAFGVLLFCMLTGNFPWekampsdtfyeefvrWQKR-----------R 252
Cdd:cd14181 175 LCGTPGYLAPEILKCSmdeTHPGY--GKEVDLWACGVILFTLLAGSPPF---------------WHRRqmlmlrmimegR 237
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 75570321 253 TGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14181 238 YQFSSPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQH 276
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
32-232 8.79e-23

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: 98.53  E-value: 8.79e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHK----IRGSKMALKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFgIAFETDEYYVFAQ 107
Cdd:cd05621  54 YDVVKVIGRGAFGEVQLVRHKasqkVYAMKLLSKFEMIKRSDSAFFWEERDI-MAFANSPWVVQLF-CAFQDDKYLYMVM 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPpQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFG----MTRRAGSP 183
Cdd:cd05621 132 EYMPGGDLVNLMS-NYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLL-DKYGH-LKLADFGtcmkMDETGMVH 208
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 75570321 184 VKRVSGTIPYTAPELCDTSKHDGFcVDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd05621 209 CDTAVGTPDYISPEVLKSQGGDGY-YGRECDWWSVGVFLFEMLVGDTPF 256
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
32-297 9.24e-23

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: 97.02  E-value: 9.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKsflREYSISLYLSPCPFIINMFGIAFETDEYYVfAQEYAP 111
Cdd:cd14175   3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPS---EEIEILLRYGQHPNIITLKDVYDDGKHVYL-VTELMR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 112 SGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDK----ECrkVKLSDFGMTR--RAGSPVK 185
Cdd:cd14175  79 GGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDEsgnpES--LRICDFGFAKqlRAENGLL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 186 RVSG-TIPYTAPELCDTSKHDGFCvdystDVWAFGVLLFCMLTGNFPWEKAmPSDTFYEEFVRWQKRRTGAVPSQWRRFT 264
Cdd:cd14175 157 MTPCyTANFVAPEVLKRQGYDEGC-----DIWSLGILLYTMLAGYTPFANG-PSDTPEEILTRIGSGKFTLSGGNWNTVS 230
                       250       260       270
                ....*....|....*....|....*....|...
gi 75570321 265 DESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14175 231 DAAKDLVSKMLHVDPHQRLTAKQV---LQHPWI 260
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
31-297 9.28e-23

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: 96.11  E-value: 9.28e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  31 YYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLR-EYSISLYLSPcPFIINMFGiAFETDEYYVFAQEY 109
Cdd:cd14114   3 HYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRkEIQIMNQLHH-PKLINLHD-AFEDDNEMVLILEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 110 APSGDLFDIIPPQ-VGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTRR--AGSPVKR 186
Cdd:cd14114  81 LSGGELFERIAAEhYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNEVKLIDFGLATHldPKESVKV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 187 VSGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYE-EFVRWQKRRtgavpSQWRRFTD 265
Cdd:cd14114 161 TTGTAEFAAPEIVEREP-----VGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNvKSCDWNFDD-----SAFSGISE 230
                       250       260       270
                ....*....|....*....|....*....|..
gi 75570321 266 ESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14114 231 EAKDFIRKLLLADPNKRMTIHQA---LEHPWL 259
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
36-297 1.36e-22

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: 96.16  E-value: 1.36e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  36 RELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKL---KSFLREYSISLYLSPCPFIINMFGIaFETDEYYVFAQEYAPS 112
Cdd:cd14197  15 RELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQdcrMEIIHEIAVLELAQANPWVINLHEV-YETASEMILVLEYAAG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 113 GDLFD--IIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIF-DKECRKVKLSDFGMTR--RAGSPVKRV 187
Cdd:cd14197  94 GEIFNqcVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTsESPLGDIKIVDFGLSRilKNSEELREI 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 188 SGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPWEkampSDTFYEEFVRWQKRRTGAVPSQWRRFTDES 267
Cdd:cd14197 174 MGTPEYVAPEILSYEP-----ISTATDMWSIGVLAYVMLTGISPFL----GDDKQETFLNISQMNVSYSEEEFEHLSESA 244
                       250       260       270
                ....*....|....*....|....*....|
gi 75570321 268 LRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14197 245 IDFIKTLLIKKPENRATAEDC---LKHPWL 271
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
32-291 1.55e-22

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: 95.54  E-value: 1.55e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSflREYS---ISLYLS-PCPFIINmFGIAFETDEYYVFAQ 107
Cdd:cd08530   2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLSQKE--REDSvneIRLLASvNHPNIIR-YKEAFLDGNRLCIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVG----LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRA-GS 182
Cdd:cd08530  79 EYAPFGDLSKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGD--LVKIGDLGISKVLkKN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 183 PVKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWE-KAMpsdtfyEEFvrWQKRRTGAVPSQWR 261
Cdd:cd08530 157 LAKTQIGTPLYAAPEVWKGRPY-----DYKSDIWSLGCLLYEMATFRPPFEaRTM------QEL--RYKVCRGKFPPIPP 223
                       250       260       270
                ....*....|....*....|....*....|
gi 75570321 262 RFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd08530 224 VYSQDLQQIIRSLLQVNPKKRPSCDKLLQS 253
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
28-316 1.61e-22

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: 96.21  E-value: 1.61e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  28 VNKYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIaFETDEYYVFAQ 107
Cdd:cd14166   1 IRETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLENEIAVLKRIKHENIVTLEDI-YESTTHYYLVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFD-KECRKVKLSDFGMTRRAGSPVKR 186
Cdd:cd14166  80 QLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTpDENSKIMITDFGLSKMEQNGIMS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 187 VS-GTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPwekampsdtFYEEFVR--WQKRRTGAVPSQ---W 260
Cdd:cd14166 160 TAcGTPGYVAPEVLAQKPYSK-----AVDCWSIGVITYILLCGYPP---------FYEETESrlFEKIKEGYYEFEspfW 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 261 RRFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWMLDGTSgnHHQSVLNSSSEE 316
Cdd:cd14166 226 DDISESAKDFIRHLLEKNPSKRYTCEKA---LSHPWIIGNTA--LHRDIYPSVSEQ 276
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
32-232 1.83e-22

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: 95.27  E-value: 1.83e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFL-----REYSISLYLSPcPFIINMFGIaFETDEYYVFA 106
Cdd:cd14070   4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYVtknlrREGRIQQMIRH-PNITQLLDI-LETENSYYLV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 107 QEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAGS---- 182
Cdd:cd14070  82 MELCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLL--DENDNIKLIDFGLSNCAGIlgys 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75570321 183 -PVKRVSGTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd14070 160 dPFSTQCGSPAYAAPELLARKKYGP-----KVDVWSIGVNMYAMLTGTLPF 205
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
32-291 1.97e-22

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: 95.63  E-value: 1.97e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGS---------KMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIaFETDEY 102
Cdd:cd14076   3 YILGRTLGEGEFGKVKLGWPLPKANhrsgvqvaiKLIRRDTQQENCQTSKIMREINILKGLTH-PNIVRLLDV-LKTKKY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 103 YVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKEcRKVKLSDFG------- 175
Cdd:cd14076  81 IGIVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLL-DKN-RNLVITDFGfantfdh 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 176 -----MTRRAGSPVkrvsgtipYTAPEL--CDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWEKAmPSDTFYEEFVRW 248
Cdd:cd14076 159 fngdlMSTSCGSPC--------YAAPELvvSDSMYAGR-----KADIWSCGVILYAMLAGYLPFDDD-PHNPNGDNVPRL 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 75570321 249 QKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14076 225 YRYICNTPLIFPEYVTPKARDLLRRILVPNPRKRIRLSAIMRH 267
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
32-233 3.50e-22

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: 94.40  E-value: 3.50e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKF---LKKKSTKLKSFLREYSISLYLSPcPFIINMFGIAFETDEYYVFaQE 108
Cdd:cd08529   2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQidiSRMSRKMREEAIDEARVLSKLNS-PYVIKYYDSFVDKGKLNIV-ME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLFDIIPPQVG--LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENilIFDKECRKVKLSDFGMTRRAGSP--- 183
Cdd:cd08529  80 YAENGDLHSLIKSQRGrpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMN--IFLDKGDNVKIGDLGVAKILSDTtnf 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 75570321 184 VKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd08529 158 AQTIVGTPYYLSPELCEDKPY-----NEKSDVWALGCVLYELCTGKHPFE 202
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
32-231 3.81e-22

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: 95.08  E-value: 3.81e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMAL---KFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFGiAFETDE--YYVFa 106
Cdd:cd07833   3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIkkfKESEDDEDVKKTALREVKV-LRQLRHENIVNLKE-AFRRKGrlYLVF- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 107 qEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR----RAGS 182
Cdd:cd07833  80 -EYVERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILV--SESGVLKLCDFGFARaltaRPAS 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 75570321 183 PVKRVSGTIPYTAPEL--CDTSKhdGFCVdystDVWAFGVLLFCMLTGN--FP 231
Cdd:cd07833 157 PLTDYVATRWYRAPELlvGDTNY--GKPV----DVWAIGCIMAELLDGEplFP 203
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
32-291 4.07e-22

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: 94.29  E-value: 4.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFL----REYSISLYLSPcPFIINMFGIAFETDEYYVFAQ 107
Cdd:cd14163   2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQrflpRELQIVERLDH-KNIIHVYEMLESADGKIYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdkECRKVKLSDFGMTRRAGSPVKRV 187
Cdd:cd14163  81 ELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL---QGFTLKLTDFGFAKQLPKGGREL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 188 S----GTIPYTAPELCDTSKHDgfcvDYSTDVWAFGVLLFCMLTGNFPWEkampsDTFYEEFVrWQKRRTGAVPSQWrRF 263
Cdd:cd14163 158 SqtfcGSTAYAAPEVLQGVPHD----SRKGDIWSMGVVLYVMLCAQLPFD-----DTDIPKML-CQQQKGVSLPGHL-GV 226
                       250       260
                ....*....|....*....|....*...
gi 75570321 264 TDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14163 227 SRTCQDLLKRLLEPDMVLRPSIEEVSWH 254
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
87-297 4.30e-22

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: 94.71  E-value: 4.30e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIaFET-DEYYVFAqEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDK- 164
Cdd:cd14088  59 PNILQLVDV-FETrKEYFIFL-ELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRl 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 165 ECRKVKLSDFGMTRRAGSPVKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTfYEE 244
Cdd:cd14088 137 KNSKIVISDFHLAKLENGLIKEPCGTPEYLAPEVVGRQRY-----GRPVDCWAIGVIMYILLSGNPPFYDEAEEDD-YEN 210
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 245 FVRWQKRRTGAVPSQ-----WRRFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14088 211 HDKNLFRKILAGDYEfdspyWDDISQAAKDLVTRLMEVEQDQRITAEEA---ISHEWI 265
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
32-233 5.88e-22

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: 94.32  E-value: 5.88e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMAL-KFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIAFETDEY---YVFAQ 107
Cdd:cd13985   2 YQVTKQLGEGGFSYVYLAHDVNTGRRYALkRMYFNDEEQLRVAIKEIEIMKRLCGHPNIVQYYDSAILSSEGrkeVLLLM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPsGDLFDIIP--PQVGLPEPVAKRCVHQVAIALEYLHSKK--LVHRDIKPENILIfdKECRKVKLSDFGMTRRAGSP 183
Cdd:cd13985  82 EYCP-GSLVDILEksPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILF--SNTGRFKLCDFGSATTEHYP 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75570321 184 VKRVSG------------TIPYTAPELCDTskHDGFCVDYSTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd13985 159 LERAEEvniieeeiqkntTPMYRAPEMIDL--YSKKPIGEKADIWALGCLLYKLCFFKLPFD 218
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
96-291 6.69e-22

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: 94.21  E-value: 6.69e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  96 AFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKecRKVKLSDFG 175
Cdd:cd14182  78 TYETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDD--MNIKLTDFG 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 176 MTRR--AGSPVKRVSGTIPYTAPELCDTS---KHDGFcvDYSTDVWAFGVLLFCMLTGNFP-WEKampSDTFYEEFVRWQ 249
Cdd:cd14182 156 FSCQldPGEKLREVCGTPGYLAPEIIECSmddNHPGY--GKEVDMWSTGVIMYTLLAGSPPfWHR---KQMLMLRMIMSG 230
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 75570321 250 KRRTGAvpSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14182 231 NYQFGS--PEWDDRSDTVKDLISRFLVVQPQKRYTAEEALAH 270
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
38-232 6.75e-22

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: 95.07  E-value: 6.75e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGS----KMALKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMfGIAFETDEYYVFAQEYAPSG 113
Cdd:cd05595   3 LGKGTFGKVILVREKATGRyyamKILRKEVIIAKDEVAHTVTESRV-LQNTRHPFLTAL-KYAFQTHDRLCFVMEYANGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENiLIFDKECRkVKLSDFGMTRRA---GSPVKRVSGT 190
Cdd:cd05595  81 ELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLEN-LMLDKDGH-IKITDFGLCKEGitdGATMKTFCGT 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 75570321 191 IPYTAPELCDTSKHdGFCVDYstdvWAFGVLLFCMLTGNFPW 232
Cdd:cd05595 159 PEYLAPEVLEDNDY-GRAVDW----WGLGVVMYEMMCGRLPF 195
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
38-235 6.78e-22

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: 94.06  E-value: 6.78e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMA---LKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFGIAFETDEYYVfAQEYAPSGD 114
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAikcLHSSPNCIEERKALLKEAEK-MERARHSYVLPLLGVCVERRSLGL-VMEYMENGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 115 L---FDIIPPQVglPEPVAKRCVHQVAIALEYLH--SKKLVHRDIKPENILIfDKECrKVKLSDFG----------MTRR 179
Cdd:cd13978  79 LkslLEREIQDV--PWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILL-DNHF-HVKISDFGlsklgmksisANRR 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75570321 180 AGSPvkRVSGTIPYTAPELCD------TSKHdgfcvdystDVWAFGVLLFCMLTGNFPWEKA 235
Cdd:cd13978 155 RGTE--NLGGTPIYMAPEAFDdfnkkpTSKS---------DVYSFAIVIWAVLTRKEPFENA 205
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
35-232 6.81e-22

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: 95.16  E-value: 6.81e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  35 IRELGKGTYGKVDLViHKIRGSKmalkflkKKSTKLKSFLREYSIS---------------LYLSPCPFIINMFgIAFET 99
Cdd:cd05584   1 LKVLGKGGYGKVFQV-RKTTGSD-------KGKIFAMKVLKKASIVrnqkdtahtkaerniLEAVKHPFIVDLH-YAFQT 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 100 DEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRR 179
Cdd:cd05584  72 GGKLYLILEYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILL-DAQGH-VKLTDFGLCKE 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 180 A---GSPVKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd05584 150 SihdGTVTHTFCGTIEYMAPEILTRSGH-----GKAVDWWSLGALMYDMLTGAPPF 200
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
26-291 7.62e-22

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: 94.33  E-value: 7.62e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  26 LEVNKYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLksfLREYSISL-YLSPC--PFIINMFGIAFETDEY 102
Cdd:cd06644   8 LDPNEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEE---LEDYMVEIeILATCnhPYIVKLLGAFYWDGKL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 103 YVFAqEYAPSGDLfDIIPPQV--GLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI-FDKEcrkVKLSDFGMTRR 179
Cdd:cd06644  85 WIMI-EFCPGGAV-DAIMLELdrGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLtLDGD---IKLADFGVSAK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 180 AGSPVKRVS---GTIPYTAPE--LCDTSKHDGFcvDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEefVRWQKRRTG 254
Cdd:cd06644 160 NVKTLQRRDsfiGTPYWMAPEvvMCETMKDTPY--DYKADIWSLGITLIEMAQIEPPHHELNPMRVLLK--IAKSEPPTL 235
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 75570321 255 AVPSQWR-RFTDeslrMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd06644 236 SQPSKWSmEFRD----FLKTALDKHPETRPSAAQLLEH 269
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
28-297 8.59e-22

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: 93.93  E-value: 8.59e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  28 VNKYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSF-------LREYSIsLYLSPCPFIINMFGIaFETD 100
Cdd:cd14194   3 VDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRgvsrediEREVSI-LKEIQHPNVITLHEV-YENK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 101 EYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRK--VKLSDFGMTR 178
Cdd:cd14194  81 TDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKprIKIIDFGLAH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 179 R--AGSPVKRVSGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDT----------FYEEFV 246
Cdd:cd14194 161 KidFGNEFKNIFGTPEFVAPEIVNYEP-----LGLEADMWSIGVITYILLSGASPFLGDTKQETlanvsavnyeFEDEYF 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 75570321 247 rwqkRRTGAVPSQWrrftdeslrmFRKLLALEQERRCSVKEvfaHLGHRWM 297
Cdd:cd14194 236 ----SNTSALAKDF----------IRRLLVKDPKKRMTIQD---SLQHPWI 269
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
86-282 1.18e-21

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: 93.36  E-value: 1.18e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  86 CPFIINMfGIAFETDEYYVFAQEYAPSGDL-FDIIP-PQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFD 163
Cdd:cd05577  52 SPFIVSL-AYAFETKDKLCLVLTLMNGGDLkYHIYNvGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDD 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 164 KEcrKVKLSDFGMT--RRAGSPVKRVSGTIPYTAPELCdtskHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKampsdtf 241
Cdd:cd05577 131 HG--HVRISDLGLAveFKGGKKIKGRVGTHGYMAPEVL----QKEVAYDFSVDWFALGCMLYEMIAGRSPFRQ------- 197
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 75570321 242 YEEFVRWQ--KRRTGAVPSQWR-RFTDESLRMFRKLLALEQERR 282
Cdd:cd05577 198 RKEKVDKEelKRRTLEMAVEYPdSFSPEARSLCEGLLQKDPERR 241
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
32-291 1.40e-21

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: 94.66  E-value: 1.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHK----------IRGSKMalkflkkkstklksfLREYSISLYL--------SPCPFIINMF 93
Cdd:cd05573   3 FEVIKVIGRGAFGEVWLVRDKdtgqvyamkiLRKSDM---------------LKREQIAHVRaerdiladADSPWIVRLH 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  94 gIAFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSD 173
Cdd:cd05573  68 -YAFQDEDHLYLVMEYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILL-DADGH-IKLAD 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 174 FGM------------------------------------TRRAGSPVkrvsGTIPYTAPE-LCDTSKhdGFCVDYstdvW 216
Cdd:cd05573 145 FGLctkmnksgdresylndsvntlfqdnvlarrrphkqrRVRAYSAV----GTPDYIAPEvLRGTGY--GPECDW----W 214
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 217 AFGVLLFCMLTGNFPWEKAMPSDTfYEEFVRWQKRRTgaVPSQwRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd05573 215 SLGVILYEMLYGFPPFYSDSLVET-YSKIMNWKESLV--FPDD-PDVSPEAIDLIRRLLCDPEDRLGSAEEIKAH 285
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
108-291 1.50e-21

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: 93.15  E-value: 1.50e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRK-------VKLSDFGMTR-- 178
Cdd:cd14202  81 EYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGGRKsnpnnirIKIADFGFARyl 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 179 RAGSPVKRVSGTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWEKAMPSD--TFYEEfvrwQKRRTGAV 256
Cdd:cd14202 161 QNNMMAATLCGSPMYMAPEVIMSQHYDA-----KADLWSIGTIIYQCLTGKAPFQASSPQDlrLFYEK----NKSLSPNI 231
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 75570321 257 PsqwrRFTDESLR-MFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14202 232 P----RETSSHLRqLLLGLLQRNQKDRMDFDEFFHH 263
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
32-291 1.80e-21

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: 92.93  E-value: 1.80e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKL---KSFLREYSISLYLSpCPFIINMFGIAFETDE-YYVFaq 107
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEEgipSTALREISLLKELK-HPNIVKLLDVIHTENKlYLVF-- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSgDLFDIIP-PQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTRRAGSPVKR 186
Cdd:cd07829  78 EYCDQ-DLKKYLDkRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGV--LKLADFGLARAFGIPLRT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 187 ---VSGTIPYTAPELCDTSKHdgfcvdYST--DVWAFGVLLFCMLTGN--FP----------------------WE--KA 235
Cdd:cd07829 155 ythEVVTLWYRAPEILLGSKH------YSTavDIWSVGCIFAELITGKplFPgdseidqlfkifqilgtpteesWPgvTK 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 236 MPSdtFYEEFVRWQKRRTGAVPSqwrRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07829 229 LPD--YKPTFPKWPKNDLEKVLP---RLDPEGIDLLSKMLQYNPAKRISAKEALKH 279
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
87-243 1.90e-21

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


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 92.60  E-value: 1.90e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYY-VFaqEYAPSGDL---------FDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKP 156
Cdd:cd00192  56 PNVVRLLGVCTEEEPLYlVM--EYMEGGDLldflrksrpVFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAA 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 157 ENILIfdKECRKVKLSDFGMTRR---AGSPVKRVSGTIP--YTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLT-GNF 230
Cdd:cd00192 134 RNCLV--GEDLVVKISDFGLSRDiydDDYYRKKTGGKLPirWMAPESLKDGIF-----TSKSDVWSFGVLLWEIFTlGAT 206
                       170
                ....*....|...
gi 75570321 231 PWEkAMPSDTFYE 243
Cdd:cd00192 207 PYP-GLSNEEVLE 218
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
18-237 2.22e-21

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: 93.20  E-value: 2.22e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  18 YTAQNLEKLEvnkyyevirELGKGTYGKVDLVIHKIRGSKMALK--FLKKKSTKLKSFLREYSISLYLSPCPFIINMFGI 95
Cdd:cd06616   3 FTAEDLKDLG---------EIGRGAFGTVNKMLHKPSGTIMAVKriRSTVDEKEQKRLLMDLDVVMRSSDCPYIVKFYGA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  96 AFETDEYYVFAQEYAPSGDLFDIIPPQVG---LPEPVAKRCVHQVAIALEYLHSK-KLVHRDIKPENILIFDKECrkVKL 171
Cdd:cd06616  74 LFREGDCWICMELMDISLDKFYKYVYEVLdsvIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGN--IKL 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75570321 172 SDFGMtrrAGSPVKRVSGTI-----PYTAPELCDTSK-HDGFcvDYSTDVWAFGVLLFCMLTGNFPWEKAMP 237
Cdd:cd06616 152 CDFGI---SGQLVDSIAKTRdagcrPYMAPERIDPSAsRDGY--DVRSDVWSLGITLYEVATGKFPYPKWNS 218
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
87-291 2.54e-21

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: 91.97  E-value: 2.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGiaFETDEYYVF-AQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKE 165
Cdd:cd14121  55 PHIVELKD--FQWDEEHIYlIMEYCSGGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRY 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 166 CRKVKLSDFGMTRRAGSPVKRVS--GTIPYTAPE-LCDTSkhdgfcVDYSTDVWAFGVLLFCMLTGNFPWEkampSDTFY 242
Cdd:cd14121 133 NPVLKLADFGFAQHLKPNDEAHSlrGSPLYMAPEmILKKK------YDARVDLWSVGVILYECLFGRAPFA----SRSFE 202
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 75570321 243 EEFVRWQKRRTGAVPSQwRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14121 203 ELEEKIRSSKPIEIPTR-PELSADCRDLLLRLLQRDPDRRISFEEFFAH 250
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
38-297 2.55e-21

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: 91.90  E-value: 2.55e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLR-EYSISLYLSPcPFIINMFGiAFETDEYYVFAQEYAPSGDLF 116
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVRnEIEIMNQLRH-PRLLQLYD-AFETPREMVLVMEYVAGGELF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 117 D-IIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTRR--AGSPVKRVSGTIPY 193
Cdd:cd14103  79 ErVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGNQIKIIDFGLARKydPDKKLKVLFGTPEF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 194 TAPELCdtsKHDgfCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFyeefvrwqkrrTGAVPSQWrRFTDESL----- 268
Cdd:cd14103 159 VAPEVV---NYE--PISYATDMWSVGVICYVLLSGLSPFMGDNDAETL-----------ANVTRAKW-DFDDEAFddisd 221
                       250       260       270
                ....*....|....*....|....*....|..
gi 75570321 269 --RMF-RKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14103 222 eaKDFiSKLLVKDPRKRMSAAQC---LQHPWL 250
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
32-291 2.60e-21

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


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 92.77  E-value: 2.60e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIAFETD----EYYVFAQ 107
Cdd:cd06638  20 WEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVKFYGMYYKKDvkngDQLWLVL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVG----LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRAGSP 183
Cdd:cd06638 100 ELCNGGSVTDLVKGFLKrgerMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEG--GVKLVDFGVSAQLTST 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 184 VKRVS---GTIPYTAPELCDTSKHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEefVRWQKRRTGAVPSQW 260
Cdd:cd06638 178 RLRRNtsvGTPFWMAPEVIACEQQLDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFK--IPRNPPPTLHQPELW 255
                       250       260       270
                ....*....|....*....|....*....|..
gi 75570321 261 R-RFTDeslrMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd06638 256 SnEFND----FIRKCLTKDYEKRPTVSDLLQH 283
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
32-291 2.88e-21

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: 92.10  E-value: 2.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDL----------VIHKIRGSKMALKFLKKKstklksfLREYSIsLYLSPCPFIINMFGiAFETDE 101
Cdd:cd08220   2 YEKIRVVGRGAYGTVYLcrrkddnklvIIKQIPVEQMTKEERQAA-------LNEVKV-LSMLHHPNIIEYYE-SFLEDK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 102 YYVFAQEYAPSGDLFDIIPPQVG--LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRKVKLSDFGMTRR 179
Cdd:cd08220  73 ALMIVMEYAPGGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILL-NKKRTVVKIGDFGISKI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 180 AGSPVK--RVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLF--CMLTGNFPWEKaMPSdtfyeeFVRWQKRRTGA 255
Cdd:cd08220 152 LSSKSKayTVVGTPCYISPELCEGKPY-----NQKSDIWALGCVLYelASLKRAFEAAN-LPA------LVLKIMRGTFA 219
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 75570321 256 VPSQwrRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd08220 220 PISD--RYSEELRHLILSMLHLDPNKRPTLSEIMAQ 253
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
38-291 3.57e-21

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: 91.83  E-value: 3.57e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYS--------ISLYLS-PCPFIINMFGIAFETDEYYVFAqE 108
Cdd:cd06628   8 IGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENKDRKKSmldalqreIALLRElQHENIVQYLGSSSDANHLNIFL-E 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTRR-------AG 181
Cdd:cd06628  87 YVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGG--IKISDFGISKKleanslsTK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 182 SPVKRVS--GTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWekamPSDTFYEEFVRWQKRRTGAVPSQ 259
Cdd:cd06628 165 NNGARPSlqGSVFWMAPEVVKQTSY-----TRKADIWSLGCLVVEMLTGTHPF----PDCTQMQAIFKIGENASPTIPSN 235
                       250       260       270
                ....*....|....*....|....*....|..
gi 75570321 260 wrrFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd06628 236 ---ISSEARDFLEKTFEIDHNKRPTADELLKH 264
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
80-291 3.92e-21

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 93.41  E-value: 3.92e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  80 SLYLSPCPFIINMFgIAFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENI 159
Cdd:cd05610  57 ALALSKSPFIVHLY-YSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNM 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 160 LIFDKEcrKVKLSDFGMT------------------------------------------------------RRAGSPV- 184
Cdd:cd05610 136 LISNEG--HIKLTDFGLSkvtlnrelnmmdilttpsmakpkndysrtpgqvlslisslgfntptpyrtpksvRRGAARVe 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 -KRVSGTIPYTAPELCDTSKHdGFCVDYstdvWAFGVLLFCMLTGNFPWEKAMPSDTFYEEFVR---WqkrrtgavPSQW 260
Cdd:cd05610 214 gERILGTPDYLAPELLLGKPH-GPAVDW----WALGVCLFEFLTGIPPFNDETPQQVFQNILNRdipW--------PEGE 280
                       250       260       270
                ....*....|....*....|....*....|.
gi 75570321 261 RRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd05610 281 EELSVNAQNAIEILLTMDPTKRAGLKELKQH 311
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
32-291 5.41e-21

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: 91.20  E-value: 5.41e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRE-LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLksflREYSISLYLSPCPFIINMFGI---AFETDEYYVFAQ 107
Cdd:cd14089   2 YTISKQvLGLGINGKVLECFHKKTGEKFALKVLRDNPKAR----REVELHWRASGCPHIVRIIDVyenTYQGRKCLLVVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLP--EPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKV-KLSDFGMtrrAGSPV 184
Cdd:cd14089  78 ECMEGGELFSRIQERADSAftEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAIlKLTDFGF---AKETT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 KRVSGTIP-----YTAPELCDTSKHDGFCvdystDVWAFGVLLFCMLTGNFPWEK----AMPSDTfyeefvrwQKR-RTG 254
Cdd:cd14089 155 TKKSLQTPcytpyYVAPEVLGPEKYDKSC-----DMWSLGVIMYILLCGYPPFYSnhglAISPGM--------KKRiRNG 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 75570321 255 --AVPS-QWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14089 222 qyEFPNpEWSNVSEEAKDLIRGLLKTDPSERLTIEEVMNH 261
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
32-291 5.71e-21

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: 91.75  E-value: 5.71e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVI--RELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKsflrEYSISLYLSPCPFIINMF-----GIAFETDEY-- 102
Cdd:cd14171   6 YEVNwtQKLGTGISGPVRVCVKKSTGERFALKILLDRPKART----EVRLHMMCSGHPNIVQIYdvyanSVQFPGESSpr 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 103 --YVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDK-ECRKVKLSDFGMTRR 179
Cdd:cd14171  82 arLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNsEDAPIKLCDFGFAKV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 180 AGSPVKRVSGTIPYTAPELCDTSKHDG------------FCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEEFVR 247
Cdd:cd14171 162 DQGDLMTPQFTPYYVAPQVLEAQRRHRkersgiptsptpYTYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTITKDMKR 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 75570321 248 WQKRRTGAVPS-QWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14171 242 KIMTGSYEFPEeEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHH 286
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
32-297 6.46e-21

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: 91.71  E-value: 6.46e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALK---FLKKKSTKLKSFLREYSISLYLSPcPFIINMF-GIAFETDEYYVFaq 107
Cdd:cd14086   3 YDLKEELGKGAFSVVRRCVQKSTGQEFAAKiinTKKLSARDHQKLEREARICRLLKH-PNIVRLHdSISEEGFHYLVF-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKE-CRKVKLSDFGMTRRAGSPVKR 186
Cdd:cd14086  80 DLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSkGAAVKLADFGLAIEVQGDQQA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 187 ---VSGTIPYTAPELCdtsKHDGFcvDYSTDVWAFGVLLFCMLTGNFPwekampsdtFYEEFVR--WQKRRTGA--VPS- 258
Cdd:cd14086 160 wfgFAGTPGYLSPEVL---RKDPY--GKPVDIWACGVILYILLVGYPP---------FWDEDQHrlYAQIKAGAydYPSp 225
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 75570321 259 QWRRFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14086 226 EWDTVTPEAKDLINQMLTVNPAKRITAAEA---LKHPWI 261
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
32-241 6.82e-21

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: 91.31  E-value: 6.82e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKlksfLR--------EYSIsLYLSPCPFIINMFGiAFETDEYY 103
Cdd:cd05609   2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLI----LRnqiqqvfvERDI-LTFAENPFVVSMYC-SFETKRHL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 104 VFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGM------- 176
Cdd:cd05609  76 CMVMEYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLI--TSMGHIKLTDFGLskiglms 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 177 -------------TRRAGSpvKRVSGTIPYTAPELCDTSKHdGFCVDYstdvWAFGVLLFCMLTGNFPWEKAMPSDTF 241
Cdd:cd05609 154 lttnlyeghiekdTREFLD--KQVCGTPEYIAPEVILRQGY-GKPVDW----WAMGIILYEFLVGCVPFFGDTPEELF 224
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
100-297 8.14e-21

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 90.80  E-value: 8.14e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 100 DEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRKVKLSDFGmtrr 179
Cdd:cd14100  78 DSFVLVLERPEPVQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILI-DLNTGELKLIDFG---- 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 180 AGSPVKRV-----SGTIPYTAPELCDTSKHDGfcvdYSTDVWAFGVLLFCMLTGNFPWEKAmpsdtfyEEFVRWQKRRTg 254
Cdd:cd14100 153 SGALLKDTvytdfDGTRVYSPPEWIRFHRYHG----RSAAVWSLGILLYDMVCGDIPFEHD-------EEIIRGQVFFR- 220
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 75570321 255 avpsqwRRFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14100 221 ------QRVSSECQHLIKWCLALRPSDRPSFEDI---QNHPWM 254
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
29-292 8.20e-21

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: 90.74  E-value: 8.20e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  29 NKYYEVIRE--LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLR-EYSISLYLSPCPfIINMFGiAFETDEYYVF 105
Cdd:cd14193   1 NSYYNVNKEeiLGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKnEIEVMNQLNHAN-LIQLYD-AFESRNDIVL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 106 AQEYAPSGDLFD-IIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTRRAGSPV 184
Cdd:cd14193  79 VMEYVDGGELFDrIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREANQVKIIDFGLARRYKPRE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 K-RVS-GTIPYTAPELCDTSkhdgfCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEEFV-RWQKRRtgavpSQWR 261
Cdd:cd14193 159 KlRVNfGTPEFLAPEVVNYE-----FVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILAcQWDFED-----EEFA 228
                       250       260       270
                ....*....|....*....|....*....|.
gi 75570321 262 RFTDESLRMFRKLLALEQERRCSVKEVFAHL 292
Cdd:cd14193 229 DISEEAKDFISKLLIKEKSWRMSASEALKHP 259
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
32-239 1.01e-20

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: 92.40  E-value: 1.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLV----IHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGiAFETDEYYVFAQ 107
Cdd:cd05618  22 FDLLRVIGRGSYAKVLLVrlkkTERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHS-CFQTESRLFFVI 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTR---RAGSPV 184
Cdd:cd05618 101 EYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLL-DSEGH-IKLTDYGMCKeglRPGDTT 178
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 185 KRVSGTIPYTAPELCDTSKHdGFCVDYstdvWAFGVLLFCMLTGNFPWEKAMPSD 239
Cdd:cd05618 179 STFCGTPNYIAPEILRGEDY-GFSVDW----WALGVLMFEMMAGRSPFDIVGSSD 228
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
97-297 1.23e-20

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: 90.29  E-value: 1.23e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  97 FETDEYYVFAQEYA-PSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRKVKLSDFG 175
Cdd:cd14101  76 FEIPEGFLLVLERPqHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILV-DLRTGDIKLIDFG 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 176 M-TRRAGSPVKRVSGTIPYTAPELCDTSKHDGFcvdySTDVWAFGVLLFCMLTGNFPWEKAmpsdtfyEEFVRwqkrrtg 254
Cdd:cd14101 155 SgATLKDSMYTDFDGTRVYSPPEWILYHQYHAL----PATVWSLGILLYDMVCGDIPFERD-------TDILK------- 216
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 75570321 255 AVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14101 217 AKPSFNKRVSNDCRSLIRSCLAYNPSDRPSLEQI---LLHPWM 256
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
27-297 1.40e-20

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: 90.40  E-value: 1.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  27 EVNKYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSF-------LREYSIsLYLSPCPFIINMFGIaFET 99
Cdd:cd14196   2 KVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRgvsreeiEREVSI-LRQVLHPNIITLHDV-YEN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 100 DEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEC--RKVKLSDFGMT 177
Cdd:cd14196  80 RTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiPHIKLIDFGLA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 178 RRA--GSPVKRVSGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDT----------FYEEF 245
Cdd:cd14196 160 HEIedGVEFKNIFGTPEFVAPEIVNYEP-----LGLEADMWSIGVITYILLSGASPFLGDTKQETlanitavsydFDEEF 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 75570321 246 VrwqkrrtgavpsqwrRFTDESLRMF-RKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14196 235 F---------------SHTSELAKDFiRKLLVKETRKRLTIQEA---LRHPWI 269
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
100-302 1.70e-20

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: 90.82  E-value: 1.70e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 100 DEYYVF-AQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDK-ECRKVKLSDFGMT 177
Cdd:cd14092  70 DELHTYlVMELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEdDDAEIKIVDFGFA 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 178 RRAGS--PVKRVSGTIPYTAPELCDTS-KHDGFcvDYSTDVWAFGVLLFCMLTGNFPWEkAMPSDTFYEEFVrwQKRRTG 254
Cdd:cd14092 150 RLKPEnqPLKTPCFTLPYAAPEVLKQAlSTQGY--DESCDLWSLGVILYTMLSGQVPFQ-SPSRNESAAEIM--KRIKSG 224
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75570321 255 AVP---SQWRRFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWMLDGTS 302
Cdd:cd14092 225 DFSfdgEEWKNVSSEAKSLIQGLLTVDPSKRLTMSEL---RNHPWLQGSSS 272
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
32-288 2.36e-20

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: 89.66  E-value: 2.36e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMA--LKFLKKKSTKLKSFLREySISLYLSPCPFIINMFGIAFETDeyYVFAQ-E 108
Cdd:cd13996   8 FEEIELLGSGGFGSVYKVRNKVDGVTYAikKIRLTEKSSASEKVLRE-VKALAKLNHPNIVRYYTAWVEEP--PLYIQmE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLFDIIPPQVGLP---EPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILiFDKECRKVKLSDFGMTRRAG---- 181
Cdd:cd13996  85 LCEGGTLRDWIDRRNSSSkndRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIF-LDNDDLQVKIGDFGLATSIGnqkr 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 182 ------SPVKRVS-------GTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLtgnfpwekaMPSDTFYEEFVRW 248
Cdd:cd13996 164 elnnlnNNNNGNTsnnsvgiGTPLYASPEQLDGEN-----YNEKADIYSLGIILFEML---------HPFKTAMERSTIL 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 75570321 249 QKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEV 288
Cdd:cd13996 230 TDLRNGILPESFKAKHPKEADLIQSLLSKNPEERPSAEQL 269
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
31-232 2.79e-20

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: 89.29  E-value: 2.79e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  31 YYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGiAFETDEYYVFAQEYA 110
Cdd:cd14191   3 FYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVD-AFEEKANIVMVLEMV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGDLFD-IIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTRR---AGSpVKR 186
Cdd:cd14191  82 SGGELFErIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKLIDFGLARRlenAGS-LKV 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75570321 187 VSGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd14191 161 LFGTPEFVAPEVINYEP-----IGYATDMWSIGVICYILVSGLSPF 201
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
100-301 2.98e-20

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: 90.10  E-value: 2.98e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 100 DEYYVF-AQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDK-ECRKVKLSDFGMT 177
Cdd:cd14179  73 DQLHTFlVMELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDEsDNSEIKIIDFGFA 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 178 RRA---GSPVKRVSGTIPYTAPELCdtsKHDGFcvDYSTDVWAFGVLLFCMLTGNFPW---EKAMPSDTFYEEFVRWQKR 251
Cdd:cd14179 153 RLKppdNQPLKTPCFTLHYAAPELL---NYNGY--DESCDLWSLGVILYTMLSGQVPFqchDKSLTCTSAEEIMKKIKQG 227
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 75570321 252 RTGAVPSQWRRFTDESLRMFRKLLALEQERR---CSVKEvfahlgHRWMLDGT 301
Cdd:cd14179 228 DFSFEGEAWKNVSQEAKDLIQGLLTVDPNKRikmSGLRY------NEWLQDGS 274
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
32-231 3.02e-20

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: 90.90  E-value: 3.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHK----IRGSKMALKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFgIAFETDEYYVFAQ 107
Cdd:cd05596  28 FDVIKVIGRGAFGEVQLVRHKstkkVYAMKLLSKFEMIKRSDSAFFWEERDI-MAHANSEWIVQLH-YAFQDDKYLYMVM 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPpQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAGSPVKRV 187
Cdd:cd05596 106 DYMPGGDLVNLMS-NYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLL-DASGH-LKLADFGTCMKMDKDGLVR 182
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 75570321 188 S----GTIPYTAPELCDTSKHDGfCVDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:cd05596 183 SdtavGTPDYISPEVLKSQGGDG-VYGRECDWWSVGVFLYEMLVGDTP 229
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
32-233 3.04e-20

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: 89.15  E-value: 3.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVI---HKIRGS-KMALKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFGIaFETDEYYVFAQ 107
Cdd:cd14164   2 YTLGTTIGEGSFSKVKLATsqkYCCKVAiKIVDRRRASPDFVQKFLPRELSI-LRRVNHPNIVQMFEC-IEVANGRLYIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcRKVKLSDFGMTRRAGSPVK-- 185
Cdd:cd14164  80 MEAAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADD-RKIKIADFGFARFVEDYPEls 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 75570321 186 -RVSGTIPYTAPELCDTSKHDGfcvdYSTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd14164 159 tTFCGSRAYTPPEVILGTPYDP----KKYDVWSLGVVLYVMVTGTMPFD 203
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
97-297 3.10e-20

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: 89.70  E-value: 3.10e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  97 FETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI-FDKECRKVKLSDFG 175
Cdd:cd14174  69 FEDDTRFYLVFEKLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCeSPDKVSPVKICDFD 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 176 MtrraGSPVKRVSGTIPYTAPEL---CDTSKH-----------DGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTF 241
Cdd:cd14174 149 L----GSGVKLNSACTPITTPELttpCGSAEYmapevvevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGHCGTDCG 224
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75570321 242 YEE-----------FVRWQKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14174 225 WDRgevcrvcqnklFESIQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQV---LQHPWV 288
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
108-299 3.25e-20

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: 89.28  E-value: 3.25e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKE--CRKVKLSDFGMTRRAGSPVK 185
Cdd:cd14183  84 ELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQdgSKSLKLGDFGLATVVDGPLY 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 186 RVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGnFPWEKAMPSD--TFYEEFVRWQKRrtgaVPSQ-WRR 262
Cdd:cd14183 164 TVCGTPTYVAPEIIAETGY-----GLKVDIWAAGVITYILLCG-FPPFRGSGDDqeVLFDQILMGQVD----FPSPyWDN 233
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 75570321 263 FTDESLRMFRKLLALEQERRCSVKEVfahLGHRWMLD 299
Cdd:cd14183 234 VSDSAKELITMMLQVDVDQRYSALQV---LEHPWVND 267
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
38-232 3.29e-20

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: 90.41  E-value: 3.29e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGS----KMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFgIAFETDEYYVFAQEYAPSG 113
Cdd:cd05603   3 IGKGSFGKVLLAKRKCDGKfyavKVLQKKTILKKKEQNHIMAERNVLLKNLKHPFLVGLH-YSFQTSEKLYFVLDYVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdkECR-KVKLSDFGMTRRAGSPVKRVS---G 189
Cdd:cd05603  82 ELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILL---DCQgHVVLTDFGLCKEGMEPEETTStfcG 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 75570321 190 TIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd05603 159 TPEYLAPEVLRKEPY-----DRTVDWWCLGAVLYEMLYGLPPF 196
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
38-291 3.48e-20

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: 89.36  E-value: 3.48e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMA----------LKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGiaFE-TDEYYVFA 106
Cdd:cd06629   9 IGKGTYGRVYLAMNATTGEMLAvkqvelpktsSDRADSRQKTVVDALKSEIDTLKDLDHPNIVQYLG--FEeTEDYFSIF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 107 QEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI-FDKECrkvKLSDFGMTRRA----- 180
Cdd:cd06629  87 LEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVdLEGIC---KISDFGISKKSddiyg 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 181 GSPVKRVSGTIPYTAPELCDtSKHDGfcvdYST--DVWAFGVLLFCMLTGNFPWEkamPSDTFYEEFVRWQKRRTGAVPS 258
Cdd:cd06629 164 NNGATSMQGSVFWMAPEVIH-SQGQG----YSAkvDIWSLGCVVLEMLAGRRPWS---DDEAIAAMFKLGNKRSAPPVPE 235
                       250       260       270
                ....*....|....*....|....*....|...
gi 75570321 259 QwRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd06629 236 D-VNLSPEALDFLNACFAIDPRDRPTAAELLSH 267
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
38-231 4.62e-20

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: 88.99  E-value: 4.62e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLViHKIRGSKMAL---------KFLKKKSTKLKSFLREYSISLYLSPCPFIINMFgIAFETDEYYVFAQE 108
Cdd:cd05583   2 LGTGAYGKVFLV-RKVGGHDAGKlyamkvlkkATIVQKAKTAEHTMTERQVLEAVRQSPFLVTLH-YAFQTDAKLHLILD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTR--------RA 180
Cdd:cd05583  80 YVNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILL-DSEGH-VVLTDFGLSKeflpgendRA 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 75570321 181 GSpvkrVSGTIPYTAPELC--DTSKHDgFCVDYstdvWAFGVLLFCMLTGNFP 231
Cdd:cd05583 158 YS----FCGTIEYMAPEVVrgGSDGHD-KAVDW----WSLGVLTYELLTGASP 201
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
31-236 4.70e-20

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: 88.42  E-value: 4.70e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  31 YYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFGiAFETDEYYVFAQEYA 110
Cdd:cd06614   1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELIINEILI-MKECKHPNIVDYYD-SYLVGDELWVVMEYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGDLFDIIPP-QVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFG----MTRRAGspvK 185
Cdd:cd06614  79 DGGSLTDIITQnPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILL-SKDGS-VKLADFGfaaqLTKEKS---K 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75570321 186 RVS--GTiPY-TAPELCdTSKhdgfcvDYST--DVWAFGVLLFCMLTG-----NFPWEKAM 236
Cdd:cd06614 154 RNSvvGT-PYwMAPEVI-KRK------DYGPkvDIWSLGIMCIEMAEGeppylEEPPLRAL 206
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
32-233 4.92e-20

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: 89.67  E-value: 4.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHK----IRGSKMALKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFGIAFETDEYYVFAQ 107
Cdd:cd05616   2 FNFLMVLGKGSFGKVMLAERKgtdeLYAVKILKKDVVIQDDDVECTMVEKRV-LALSGKPPFLTQLHSCFQTMDRLYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPpQVG-LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRA---GSP 183
Cdd:cd05616  81 EYVNGGDLMYHIQ-QVGrFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVML-DSEGH-IKIADFGMCKENiwdGVT 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 75570321 184 VKRVSGTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd05616 158 TKTFCGTPDYIAPEIIAYQPYGK-----SVDWWAFGVLLYEMLAGQAPFE 202
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
32-291 5.16e-20

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: 88.21  E-value: 5.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMA---LKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGiAFETDEYYVFAQE 108
Cdd:cd13997   2 FHELEQIGSGSFSEVFKVRSKVDGCLYAvkkSKKPFRGPKERARALREVEAHAALGQHPNIVRYYS-SWEEGGHLYIQME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSG---DLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI-FDKECrkvKLSDFGMTRRAGSPV 184
Cdd:cd13997  81 LCENGslqDALEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFIsNKGTC---KIGDFGLATRLETSG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 KRVSGTIPYTAPELCDTSKHdgfcVDYSTDVWAFGVLLFCMLTGNfpwekAMPsdtfyEEFVRWQKRRTGAVPsqwRRFT 264
Cdd:cd13997 158 DVEEGDSRYLAPELLNENYT----HLPKADIFSLGVTVYEAATGE-----PLP-----RNGQQWQQLRQGKLP---LPPG 220
                       250       260       270
                ....*....|....*....|....*....|.
gi 75570321 265 DESLRMFRKLLAL----EQERRCSVKEVFAH 291
Cdd:cd13997 221 LVLSQELTRLLKVmldpDPTRRPTADQLLAH 251
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
89-297 6.48e-20

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


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 88.09  E-value: 6.48e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRK 168
Cdd:cd14102  66 VIKLLDWYERPDGFLIVMERPEPVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLV-DLRTGE 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 169 VKLSDFGmtrrAGSPVKRV-----SGTIPYTAPELCDTSKHDGfcvdYSTDVWAFGVLLFCMLTGNFPWEKAmpsdtfyE 243
Cdd:cd14102 145 LKLIDFG----SGALLKDTvytdfDGTRVYSPPEWIRYHRYHG----RSATVWSLGVLLYDMVCGDIPFEQD-------E 209
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 75570321 244 EFVRwqkrrtGAVPSQwRRFTDESLRMFRKLLALEQERRCSVKEVFAhlgHRWM 297
Cdd:cd14102 210 EILR------GRLYFR-RRVSPECQQLIKWCLSLRPSDRPTLEQIFD---HPWM 253
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
38-231 7.30e-20

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: 89.34  E-value: 7.30e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGS----KMALKFLKKKSTKLKSFLREYSIslyLSPC--PFIINMfGIAFETDEYYVFAQEYAP 111
Cdd:cd05571   3 LGKGTFGKVILCREKATGElyaiKILKKEVIIAKDEVAHTLTENRV---LQNTrhPFLTSL-KYSFQTNDRLCFVMEYVN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 112 SGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTR---RAGSPVKRVS 188
Cdd:cd05571  79 GGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLL-DKDGH-IKITDFGLCKeeiSYGATTKTFC 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 75570321 189 GTIPYTAPELCDTSKHdGFCVDYstdvWAFGVLLFCMLTGNFP 231
Cdd:cd05571 157 GTPEYLAPEVLEDNDY-GRAVDW----WGLGVVMYEMMCGRLP 194
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
108-231 7.45e-20

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: 88.12  E-value: 7.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAG------ 181
Cdd:cd14010  74 EYCTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILL--DGNGTLKLSDFGLARREGeilkel 151
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75570321 182 -------------SPVKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:cd14010 152 fgqfsdegnvnkvSKKQAKRGTPYYMAPELFQGGVH-----SFASDLWALGCVLYEMFTGKPP 209
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
136-297 8.22e-20

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: 87.70  E-value: 8.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRR-----AGSPVKRVSGTIPYTAPEL---CDTskHDGF 207
Cdd:cd14119 105 QLIDGLEYLHSQGIIHKDIKPGNLLL--TTDGTLKISDFGVAEAldlfaEDDTCTTSQGSPAFQPPEIangQDS--FSGF 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 208 CVdystDVWAFGVLLFCMLTGNFPWEkampSDTFYEEFvrwqkRRTGAVPSQWRRFTDESLR-MFRKLLALEQERRCSVK 286
Cdd:cd14119 181 KV----DIWSAGVTLYNMTTGKYPFE----GDNIYKLF-----ENIGKGEYTIPDDVDPDLQdLLRGMLEKDPEKRFTIE 247
                       170
                ....*....|.
gi 75570321 287 EVFAhlgHRWM 297
Cdd:cd14119 248 QIRQ---HPWF 255
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
31-291 8.55e-20

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: 88.63  E-value: 8.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  31 YYEVIRELGKGTYGKVDLVIHKIRGSKMALKF-LKKKSTKLKSFLREYSISLYLSPCPFIINMFGIaFETDE--YYVFAQ 107
Cdd:cd14090   3 YKLTGELLGEGAYASVQTCINLYTGKEYAVKIiEKHPGHSRSRVFREVETLHQCQGHPNILQLIEY-FEDDErfYLVFEK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYApsGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI--FDKECrKVKLSDFGM------TRR 179
Cdd:cd14090  82 MRG--GPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCesMDKVS-PVKICDFDLgsgiklSST 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 180 AGSPVKRVS-----GTIPYTAPELCDTSKHDGFCVDYSTDVWAFGVLLFCMLTGNFP----------WEKAMPSDTFYEE 244
Cdd:cd14090 159 SMTPVTTPElltpvGSAEYMAPEVVDAFVGEALSYDKRCDLWSLGVILYIMLCGYPPfygrcgedcgWDRGEACQDCQEL 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 75570321 245 -FVRWQKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14090 239 lFHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQH 286
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
32-233 8.65e-20

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: 87.72  E-value: 8.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKK-KSTKLKSFLREYSISLYLSPCPFIInMFGIAFETDEYYVFAQEYA 110
Cdd:cd08219   2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLpKSSSAVEDSRKEAVLLAKMKHPNIV-AFKESFEADGHLYIVMEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGDLFDIIPPQVG--LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENilIFDKECRKVKLSDFGMTRRAGSPVKRVS 188
Cdd:cd08219  81 DGGDLMQKIKLQRGklFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKN--IFLTQNGKVKLGDFGSARLLTSPGAYAC 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 75570321 189 ---GTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd08219 159 tyvGTPYYVPPEIWENMPYNN-----KSDIWSLGCILYELCTLKHPFQ 201
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
32-291 8.74e-20

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: 87.90  E-value: 8.74e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINmFGIAFETDEYYVFAQEYAP 111
Cdd:cd14662   2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQREIINHRSLRH-PNIIR-FKEVVLTPTHLAIVMEYAA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 112 SGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTRRA--GSPVKRVSG 189
Cdd:cd14662  80 GGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGYSKSSvlHSQPKSTVG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 190 TIPYTAPELCDTSKHDGfcvdYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEEFVRWQKRRTgAVPsQWRRFTDESLR 269
Cdd:cd14662 160 TPAYIAPEVLSRKEYDG----KVADVWSCGVTLYVMLVGAYPFEDPDDPKNFRKTIQRIMSVQY-KIP-DYVRVSQDCRH 233
                       250       260
                ....*....|....*....|..
gi 75570321 270 MFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14662 234 LLSRIFVANPAKRITIPEIKNH 255
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
32-297 9.18e-20

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: 88.53  E-value: 9.18e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKsflREYSISLYLSPCPFIINMFGIaFETDEYYVFAQEYAP 111
Cdd:cd14177   6 YELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPS---EEIEILMRYGQHPNIITLKDV-YDDGRYVYLVTELMK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 112 SGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECR--KVKLSDFGMTRRagspVKRVSG 189
Cdd:cd14177  82 GGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANadSIRICDFGFAKQ----LRGENG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 190 -------TIPYTAPELCDTSKHDGFCvdystDVWAFGVLLFCMLTGNFPWEKAmPSDTFYEEFVRWQKRRTGAVPSQWRR 262
Cdd:cd14177 158 llltpcyTANFVAPEVLMRQGYDAAC-----DIWSLGVLLYTMLAGYTPFANG-PNDTPEEILLRIGSGKFSLSGGNWDT 231
                       250       260       270
                ....*....|....*....|....*....|....*
gi 75570321 263 FTDESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14177 232 VSDAAKDLLSHMLHVDPHQRYTAEQV---LKHSWI 263
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
36-241 1.25e-19

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: 88.81  E-value: 1.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  36 RELGKGTYGKVDLV----IHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFgIAFETDEYYVFAQEYAP 111
Cdd:cd05590   1 RVLGKGSFGKVMLArlkeSGRLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLY-CCFQTPDRLFFVMEFVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 112 SGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI-FDKECrkvKLSDFGMTR---RAGSPVKRV 187
Cdd:cd05590  80 GGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLdHEGHC---KLADFGMCKegiFNGKTTSTF 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 75570321 188 SGTIPYTAPELCDTSKHdGFCVDYstdvWAFGVLLFCMLTGNFPWEKAMPSDTF 241
Cdd:cd05590 157 CGTPDYIAPEILQEMLY-GPSVDW----WAMGVLLYEMLCGHAPFEAENEDDLF 205
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
32-233 1.28e-19

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: 88.92  E-value: 1.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHK----IRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGiAFETDEYYVFAQ 107
Cdd:cd05617  17 FDLIRVIGRGSYAKVLLVRLKkndqIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHS-CFQTTSRLFLVI 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTR---RAGSPV 184
Cdd:cd05617  96 EYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLL-DADGH-IKLTDYGMCKeglGPGDTT 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 75570321 185 KRVSGTIPYTAPELCDTSKHdGFCVDYstdvWAFGVLLFCMLTGNFPWE 233
Cdd:cd05617 174 STFCGTPNYIAPEILRGEEY-GFSVDW----WALGVLMFEMMAGRSPFD 217
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
32-292 1.35e-19

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: 87.55  E-value: 1.35e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYS------ISLYLSPCPFIINMFGIAFETD----E 101
Cdd:cd14047   8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEKAEREVKALAkldhpnIVRYNGCWDGFDYDPETSSSNSsrskT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 102 YYVFAQ-EYAPSGDLFDIIPPQVGLP-EPV-AKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKecRKVKLSDFGMTR 178
Cdd:cd14047  88 KCLFIQmEFCEKGTLESWIEKRNGEKlDKVlALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDT--GKVKIGDFGLVT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 179 RAGSPVKRVS--GTIPYTAPElcdtsKHDGFCVDYSTDVWAFGVLLFCMLTgnfpwekamPSDTFYEEFVRWQKRRTGAV 256
Cdd:cd14047 166 SLKNDGKRTKskGTLSYMSPE-----QISSQDYGKEVDIYALGLILFELLH---------VCDSAFEKSKFWTDLRNGIL 231
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 75570321 257 PSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAHL 292
Cdd:cd14047 232 PDIFDKRYKIEKTIIKKMLSKKPEDRPNASEILRTL 267
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
87-286 1.55e-19

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: 88.44  E-value: 1.55e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFgIAFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKEC 166
Cdd:cd05619  66 PFLTHLF-CTFQTKENLFFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILL-DKDG 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 167 RkVKLSDFGMTRRAGSPVKRVS---GTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFye 243
Cdd:cd05619 144 H-IKIADFGMCKENMLGDAKTStfcGTPDYIAPEILLGQKY-----NTSVDWWSFGVLLYEMLIGQSPFHGQDEEELF-- 215
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 75570321 244 efvrwQKRRTGAvPSQWRRFTDESLRMFRKLLALEQERRCSVK 286
Cdd:cd05619 216 -----QSIRMDN-PFYPRWLEKEAKDILVKLFVREPERRLGVR 252
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
32-291 1.61e-19

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


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 87.74  E-value: 1.61e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIAFETDEyYVFAQ---- 107
Cdd:cd06639  24 WDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEAEYNILRSLPNHPNVVKFYGMFYKADQ-YVGGQlwlv 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 -EYAPSGDLFDIIPPQVG----LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRAGS 182
Cdd:cd06639 103 lELCNGGSVTELVKGLLKcgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG--GVKLVDFGVSAQLTS 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 183 PVKRVS---GTIPYTAPELCDTSKHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEefVRWQKRRTGAVPSQ 259
Cdd:cd06639 181 ARLRRNtsvGTPFWMAPEVIACEQQYDYSYDARCDVWSLGITAIELADGDPPLFDMHPVKALFK--IPRNPPPTLLNPEK 258
                       250       260       270
                ....*....|....*....|....*....|...
gi 75570321 260 W-RRFTdeslRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd06639 259 WcRGFS----HFISQCLIKDFEKRPSVTHLLEH 287
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
87-240 1.84e-19

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: 86.39  E-value: 1.84e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVFaQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEC 166
Cdd:cd14059  41 PNIIKFKGVCTQAPCYCIL-MEYCPYGQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDV 119
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 167 rkVKLSDFGMTRRAGSPVKRVS--GTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPWeKAMPSDT 240
Cdd:cd14059 120 --LKISDFGTSKELSEKSTKMSfaGTVAWMAPEVIRNEP-----CSEKVDIWSFGVVLWELLTGEIPY-KDVDSSA 187
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
28-241 2.07e-19

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


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 87.16  E-value: 2.07e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  28 VNKYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSF-------LREYSIsLYLSPCPFIINMFGIaFETD 100
Cdd:cd14105   3 VEDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASRRgvsrediEREVSI-LRQVLHPNIITLHDV-FENK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 101 EYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEC--RKVKLSDFGMTR 178
Cdd:cd14105  81 TDVVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVpiPRIKLIDFGLAH 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 179 R--AGSPVKRVSGTIPYTAPELcdtskhdgfcVDYS-----TDVWAFGVLLFCMLTGNFPWEKAMPSDTF 241
Cdd:cd14105 161 KieDGNEFKNIFGTPEFVAPEI----------VNYEplgleADMWSIGVITYILLSGASPFLGDTKQETL 220
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
99-300 2.51e-19

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: 87.62  E-value: 2.51e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  99 TDEYYVF-AQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDK-ECRKVKLSDFGM 176
Cdd:cd14180  71 HDQYHTYlVMELLRGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADEsDGAVLKVIDFGF 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 177 TR---RAGSPVKRVSGTIPYTAPELCDTSKHDGFCvdystDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEEFVRWQKRRT 253
Cdd:cd14180 151 ARlrpQGSRPLQTPCFTLQYAAPELFSNQGYDESC-----DLWSLGVILYTMLSGQVPFQSKRGKMFHNHAADIMHKIKE 225
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 75570321 254 GAVPSQ---WRRFTDESLRMFRKLLALEQERRCSVKEVFAhlgHRWMLDG 300
Cdd:cd14180 226 GDFSLEgeaWKGVSEEAKDLVRGLLTVDPAKRLKLSELRE---SDWLQGG 272
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
38-287 2.83e-19

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: 87.44  E-value: 2.83e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKL----KSFLREYSISLYLSPCPFIINMFgIAFETDEYYVFAQEYAPSG 113
Cdd:cd05592   3 LGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEdddvECTMIERRVLALASQHPFLTHLF-CTFQTESHLFFVMEYLNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAGSPVKRVS---GT 190
Cdd:cd05592  82 DLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLL-DREGH-IKIADFGMCKENIYGENKAStfcGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 191 IPYTAPELCDTSKHDgfcvdYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFyeefvrWQKRRTGAVPSQWrrFTDESLRM 270
Cdd:cd05592 160 PDYIAPEILKGQKYN-----QSVDWWSFGVLLYEMLIGQSPFHGEDEDELF------WSICNDTPHYPRW--LTKEAASC 226
                       250
                ....*....|....*..
gi 75570321 271 FRKLLALEQERRCSVKE 287
Cdd:cd05592 227 LSLLLERNPEKRLGVPE 243
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
97-231 2.94e-19

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: 86.12  E-value: 2.94e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  97 FETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGM 176
Cdd:cd06627  68 VKTKDSLYIILEYVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDG--LVKLADFGV 145
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75570321 177 TRRAGSPVKR---VSGTiPY-TAPELCDTSkhdGFCVdySTDVWAFGVLLFCMLTGNFP 231
Cdd:cd06627 146 ATKLNEVEKDensVVGT-PYwMAPEVIEMS---GVTT--ASDIWSVGCTVIELLTGNPP 198
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
32-297 3.21e-19

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: 86.43  E-value: 3.21e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIaFETDEYYVFAQEYAP 111
Cdd:cd14087   3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCESELNVLRRVRH-TNIIQLIEV-FETKERVYMVMELAT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 112 SGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECR-KVKLSDFGM-TRRAGSP---VKR 186
Cdd:cd14087  81 GGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDsKIMITDFGLaSTRKKGPnclMKT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 187 VSGTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWEKAMPSdTFYEEFVRWQKRRTGavpSQWRRFTDE 266
Cdd:cd14087 161 TCGTPEYIAPEILLRKPYTQ-----SVDMWAVGVIAYILLSGTMPFDDDNRT-RLYRQILRAKYSYSG---EPWPSVSNL 231
                       250       260       270
                ....*....|....*....|....*....|.
gi 75570321 267 SLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14087 232 AKDFIDRLLTVNPGERLSATQA---LKHPWI 259
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
29-232 3.43e-19

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: 86.72  E-value: 3.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  29 NKYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLK--KKSTKLKSFLREYSIsLYLSPCPFIINMFGIAFETDEYYVFA 106
Cdd:cd06620   4 NQDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHidAKSSVRKQILRELQI-LHECHSPYIVSFYGAFLNENNNIIIC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 107 QEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSK-KLVHRDIKPENILIFDKEcrKVKLSDFGMTRR-AGSPV 184
Cdd:cd06620  83 MEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKG--QIKLCDFGVSGElINSIA 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 KRVSGTIPYTAPELCDTSKhdgfcvdYS--TDVWAFGVLLFCMLTGNFPW 232
Cdd:cd06620 161 DTFVGTSTYMSPERIQGGK-------YSvkSDVWSLGLSIIELALGEFPF 203
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
28-232 5.07e-19

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: 85.83  E-value: 5.07e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  28 VNKYYEVIRELGKGTYGKVDLVIHKIRGSKMALK-------FLKKKSTKLKSFLREYSIsLYLSPCPFIINMFGIaFETD 100
Cdd:cd14195   3 VEDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKfikkrrlSSSRRGVSREEIEREVNI-LREIQHPNIITLHDI-FENK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 101 EYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEC--RKVKLSDFGMTR 178
Cdd:cd14195  81 TDVVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpnPRIKLIDFGIAH 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 179 R--AGSPVKRVSGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd14195 161 KieAGNEFKNIFGTPEFVAPEIVNYEP-----LGLEADMWSIGVITYILLSGASPF 211
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
31-291 5.44e-19

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: 86.23  E-value: 5.44e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  31 YYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLksfLREYSISL-YLSPC--PFIINMFGIAFETDEYYVFAQ 107
Cdd:cd06643   6 FWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEE---LEDYMVEIdILASCdhPNIVKLLDAFYYENNLWILIE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYApsGDLFDIIPPQVGLP--EPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI-FDKEcrkVKLSDFGMTRRAGSPV 184
Cdd:cd06643  83 FCA--GGAVDAVMLELERPltEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFtLDGD---IKLADFGVSAKNTRTL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 KRVS---GTIPYTAPE--LCDTSKHDGFcvDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEefVRWQKRRTGAVPSQ 259
Cdd:cd06643 158 QRRDsfiGTPYWMAPEvvMCETSKDRPY--DYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLK--IAKSEPPTLAQPSR 233
                       250       260       270
                ....*....|....*....|....*....|...
gi 75570321 260 WR-RFTDeslrMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd06643 234 WSpEFKD----FLRKCLEKNVDARWTTSQLLQH 262
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
13-232 6.19e-19

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: 87.01  E-value: 6.19e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  13 EELQLYTAQNLEKLEVNKYyEVIRELGKGTYGKVDLVIHKIRGS----KMALKFLKKKSTKLKSFLREYSIsLYLSPCPF 88
Cdd:cd05594   9 EEMEVSLTKPKHKVTMNDF-EYLKLLGKGTFGKVILVKEKATGRyyamKILKKEVIVAKDEVAHTLTENRV-LQNSRHPF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMfGIAFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKK-LVHRDIKPENiLIFDKECR 167
Cdd:cd05594  87 LTAL-KYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLEN-LMLDKDGH 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 168 kVKLSDFGMTR---RAGSPVKRVSGTIPYTAPELCDTSKHdGFCVDYstdvWAFGVLLFCMLTGNFPW 232
Cdd:cd05594 165 -IKITDFGLCKegiKDGATMKTFCGTPEYLAPEVLEDNDY-GRAVDW----WGLGVVMYEMMCGRLPF 226
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
32-232 7.59e-19

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: 86.51  E-value: 7.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLV-------IHKIRGSKMALKFLKKKSTKLKSFLR-EYSISLYLSPCPFIINMFgIAFETDEYY 103
Cdd:cd05614   2 FELLKVLGTGAYGKVFLVrkvsghdANKLYAMKVLRKAALVQKAKTVEHTRtERNVLEHVRQSPFLVTLH-YAFQTDAKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 104 VFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRKVkLSDFGMTRRAGSP 183
Cdd:cd05614  81 HLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILL-DSEGHVV-LTDFGLSKEFLTE 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 75570321 184 VKRVS----GTIPYTAPELCDTSKHDGFCVDYstdvWAFGVLLFCMLTGNFPW 232
Cdd:cd05614 159 EKERTysfcGTIEYMAPEIIRGKSGHGKAVDW----WSLGILMFELLTGASPF 207
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
38-232 1.01e-18

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: 84.97  E-value: 1.01e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKF-LKKKSTKLKSFLREYSISLYLSPcPFIINMFGiAFETDEYYVFAQEYAPSGDLF 116
Cdd:cd14190  12 LGGGKFGKVHTCTEKRTGLKLAAKViNKQNSKDKEMVLLEIQVMNQLNH-RNLIQLYE-AIETPNEIVLFMEYVEGGELF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 117 D-IIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTRRAGSPVK-RVS-GTIPY 193
Cdd:cd14190  90 ErIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGHQVKIIDFGLARRYNPREKlKVNfGTPEF 169
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 75570321 194 TAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd14190 170 LSPEVVNYDQ-----VSFPTDMWSMGVITYMLLSGLSPF 203
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
32-291 1.02e-18

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: 85.42  E-value: 1.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKL---KSFLREYSIsLYLSPCPFIINMFGIAF-ETDEYYVFaq 107
Cdd:cd07835   1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETEDEgvpSTAIREISL-LKELNHPNIVRLLDVVHsENKLYLVF-- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSgDL---FDIIPPQvGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKEcRKVKLSDFGMTRRAGSPV 184
Cdd:cd07835  78 EFLDL-DLkkyMDSSPLT-GLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLI-DTE-GALKLADFGLARAFGVPV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 KRVSG---TIPYTAPELCDTSKHdgfcvdYST--DVWAFGVLLFCMLTGN--FP----------------------WEKA 235
Cdd:cd07835 154 RTYTHevvTLWYRAPEILLGSKH------YSTpvDIWSVGCIFAEMVTRRplFPgdseidqlfrifrtlgtpdedvWPGV 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75570321 236 MPSDTFYEEFVRWQKRRTG-AVPSqwrrFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07835 228 TSLPDYKPTFPKWARQDLSkVVPS----LDEDGLDLLSQMLVYDPAKRISAKAALQH 280
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
35-289 1.03e-18

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


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 86.17  E-value: 1.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  35 IRELGKGTYGKVDLVIHKIRGS----KMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFgIAFETDEYYVFAQEYA 110
Cdd:cd05604   1 LKVIGKGSFGKVLLAKRKRDGKyyavKVLQKKVILNRKEQKHIMAERNVLLKNVKHPFLVGLH-YSFQTTDKLYFVLDFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRKVkLSDFGMTRRAGSPVKRVS-- 188
Cdd:cd05604  80 NGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILL-DSQGHIV-LTDFGLCKEGISNSDTTTtf 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 189 -GTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPW----EKAMPSDTFYEEFVrwqkRRTGAVPSQWrrf 263
Cdd:cd05604 158 cGTPEYLAPEVIRKQPYDN-----TVDWWCLGSVLYEMLYGLPPFycrdTAEMYENILHKPLV----LRPGISLTAW--- 225
                       250       260
                ....*....|....*....|....*.
gi 75570321 264 tdeslRMFRKLLALEQERRCSVKEVF 289
Cdd:cd05604 226 -----SILEELLEKDRQLRLGAKEDF 246
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
96-291 1.24e-18

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: 85.83  E-value: 1.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  96 AFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFG 175
Cdd:cd05598  69 SFQDKENLYFVMDYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILI-DRDGH-IKLTDFG 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 176 MTR-----------RAGSPVkrvsGTIPYTAPELCDTSKHDGFCvdystDVWAFGVLLFCMLTGNFPWEKAMPSDTfYEE 244
Cdd:cd05598 147 LCTgfrwthdskyyLAHSLV----GTPNYIAPEVLLRTGYTQLC-----DWWSVGVILYEMLVGQPPFLAQTPAET-QLK 216
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 75570321 245 FVRWQKrrTGAVPSQwRRFTDESLRMFRKLLALEQER--RCSVKEVFAH 291
Cdd:cd05598 217 VINWRT--TLKIPHE-ANLSPEAKDLILRLCCDAEDRlgRNGADEIKAH 262
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
28-309 1.43e-18

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: 84.94  E-value: 1.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  28 VNKYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSIS-LYLSPCPFIINMFGIaFETDEYYVFA 106
Cdd:cd14169   1 INSVYELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMVENEIAvLRRINHENIVSLEDI-YESPTHLYLA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 107 QEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDK-ECRKVKLSDFGMTR-RAGSPV 184
Cdd:cd14169  80 MELVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPfEDSKIMISDFGLSKiEAQGML 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 KRVSGTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPwekampsdtFYEE-----FVRWQKRRTGAVPSQ 259
Cdd:cd14169 160 STACGTPGYVAPELLEQKPYGK-----AVDVWAIGVISYILLCGYPP---------FYDEndselFNQILKAEYEFDSPY 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 75570321 260 WRRFTDESLRMFRKLLALEQERRCSVKEVFAHLghrWMLDGTS--GNHHQSV 309
Cdd:cd14169 226 WDDISESAKDFIRHLLERDPEKRFTCEQALQHP---WISGDTAldRDIHGSV 274
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
29-282 1.48e-18

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: 84.96  E-value: 1.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  29 NKYYEVIRELGKGTYGKVDLV------------------IHKIRGSKMAlkflkkkstklksfLREYSIsLYLSPCPFII 90
Cdd:cd05607   1 DKYFYEFRVLGKGGFGEVCAVqvkntgqmyackkldkkrLKKKSGEKMA--------------LLEKEI-LEKVNSPFIV 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  91 NMfGIAFETDEYYVFAQEYAPSGDL-FDIIppQVGLPEPVAKRCVH---QVAIALEYLHSKKLVHRDIKPENILIFDK-E 165
Cdd:cd05607  66 SL-AYAFETKTHLCLVMSLMNGGDLkYHIY--NVGERGIEMERVIFysaQITCGILHLHSLKIVYRDMKPENVLLDDNgN 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 166 CRkvkLSDFGMT--RRAGSPVKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWeKAMPSDTFYE 243
Cdd:cd05607 143 CR---LSDLGLAveVKEGKPITQRAGTNGYMAPEILKEESY-----SYPVDWFAMGCSIYEMVAGRTPF-RDHKEKVSKE 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 75570321 244 EFvrwqKRRT--GAVPSQWRRFTDESLRMFRKLLALEQERR 282
Cdd:cd05607 214 EL----KRRTleDEVKFEHQNFTEEAKDICRLFLAKKPENR 250
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
31-291 1.62e-18

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: 84.88  E-value: 1.62e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  31 YYEVIRELGKGTYGkvdlVIHKIR--GSKMALKFLKKKSTKLKSFLR-EYSISLYLSPcPFIINMFGIaFETDEYYVFAQ 107
Cdd:cd14085   4 FFEIESELGRGATS----VVYRCRqkGTQKPYAVKKLKKTVDKKIVRtEIGVLLRLSH-PNIIKLKEI-FETPTEISLVL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFD-KECRKVKLSDFGMTRRAGSPV-- 184
Cdd:cd14085  78 ELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATpAPDAPLKIADFGLSKIVDQQVtm 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 KRVSGTIPYTAPE-LCdtskhdGFCVDYSTDVWAFGVLLFCMLTGNFPwekampsdtFYEE------FVRWQKRRTGAVP 257
Cdd:cd14085 158 KTVCGTPGYCAPEiLR------GCAYGPEVDMWSVGVITYILLCGFEP---------FYDErgdqymFKRILNCDYDFVS 222
                       250       260       270
                ....*....|....*....|....*....|....
gi 75570321 258 SQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14085 223 PWWDDVSLNAKDLVKKLIVLDPKKRLTTQQALQH 256
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
96-231 1.67e-18

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: 85.44  E-value: 1.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  96 AFETDEYYVFAQEYAPSGDLFDIIPPQVG-LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKeCRKVKLSDF 174
Cdd:cd05601  69 AFQDSENLYLVMEYHPGGDLLSLLSRYDDiFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILI-DR-TGHIKLADF 146
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 175 G--------MTRRAGSPVkrvsGTIPYTAPELC-----DTSKHDGFCVDYstdvWAFGVLLFCMLTGNFP 231
Cdd:cd05601 147 GsaaklssdKTVTSKMPV----GTPDYIAPEVLtsmngGSKGTYGVECDW----WSLGIVAYEMLYGKTP 208
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
89-292 1.83e-18

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: 84.25  E-value: 1.83e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFETDEY---YvfaqEYAPSGDLFDIIPPQVGLPE-PVAKR---CVHqVAIALEYLHS---KKLVHRDIKPEN 158
Cdd:cd14066  52 LVRLLGYCLESDEKllvY----EYMPNGSLEDRLHCHKGSPPlPWPQRlkiAKG-IARGLEYLHEecpPPIIHGDIKSSN 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 159 ILIfdKECRKVKLSDFGMTR-----RAGSPVKRVSGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd14066 127 ILL--DEDFEPKLTDFGLARlippsESVSKTSAVKGTIGYLAPEYIRTGR-----VSTKSDVYSFGVVLLELLTGKPAVD 199
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 234 KAMPSDTFY-----------EEFVRWQKRRTGAVPSQWRrftDESLRMFRklLALE-----QERRCSVKEVFAHL 292
Cdd:cd14066 200 ENRENASRKdlvewveskgkEELEDILDKRLVDDDGVEE---EEVEALLR--LALLctrsdPSLRPSMKEVVQML 269
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
107-235 1.84e-18

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: 83.95  E-value: 1.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 107 QEYAPSGDLFDIIppQVGLPEPV--AKRCVHQVAIALEYLHSKKLVHRDIKPENILIF-DKECRKVKLSDFGMTRRA--- 180
Cdd:cd14012  83 TEYAPGGSLSELL--DSVGSVPLdtARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDrDAGTGIVKLTDYSLGKTLldm 160
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 181 -GSPVKRVSGTIPYTAPELCDTSKHDGFCvdysTDVWAFGVLLFCMLTGNFPWEKA 235
Cdd:cd14012 161 cSRGSLDEFKQTYWLPPELAQGSKSPTRK----TDVWDLGLLFLQMLFGLDVLEKY 212
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
36-291 1.93e-18

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: 84.27  E-value: 1.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  36 RELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLksflREYSISLYLSPCPFIINMFGI---AFETDEYYVFAQEYAPS 112
Cdd:cd14172  10 QVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKAR----REVEHHWRASGGPHIVHILDVyenMHHGKRCLLIIMECMEG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 113 GDLFDIIPPQ--VGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKV-KLSDFGMTRRAG--SPVKRV 187
Cdd:cd14172  86 GELFSRIQERgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVlKLTDFGFAKETTvqNALQTP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 188 SGTIPYTAPELCDTSKHDGFCvdystDVWAFGVLLFCMLTGnFPwekampsdTFY----EEFVRWQKRRT-----GAVPS 258
Cdd:cd14172 166 CYTPYYVAPEVLGPEKYDKSC-----DMWSLGVIMYILLCG-FP--------PFYsntgQAISPGMKRRIrmgqyGFPNP 231
                       250       260       270
                ....*....|....*....|....*....|...
gi 75570321 259 QWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14172 232 EWAEVSEEAKQLIRHLLKTDPTERMTITQFMNH 264
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
98-291 2.03e-18

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


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 84.29  E-value: 2.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  98 ETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRK-------VK 170
Cdd:cd14201  75 EMPNSVFLVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKKssvsgirIK 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 171 LSDFGMTRRAGSPVKRVS--GTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWEKAMPSD--TFYEEfv 246
Cdd:cd14201 155 IADFGFARYLQSNMMAATlcGSPMYMAPEVIMSQHYDA-----KADLWSIGTVIYQCLVGKPPFQANSPQDlrMFYEK-- 227
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75570321 247 rwQKRRTGAVPSQwrrfTDESLR-MFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14201 228 --NKNLQPSIPRE----TSPYLAdLLLGLLQRNQKDRMDFEAFFSH 267
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
33-298 2.19e-18

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: 84.52  E-value: 2.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  33 EVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKK--STKLKSFLREYSIsLYLSPCPFIINMFGiAFETDEYYVFAQEYA 110
Cdd:cd06622   4 EVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLEldESKFNQIIMELDI-LHKAVSPYIVDFYG-AFFIEGAVYMCMEYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGD---LFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSK-KLVHRDIKPENILIFDKEcrKVKLSDFGMTrraGSPVKR 186
Cdd:cd06622  82 DAGSldkLYAGGVATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNG--QVKLCDFGVS---GNLVAS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 187 VS----GTIPYTAPE-LCDTSKHDGFCVDYSTDVWAFGVLLFCMLTGNFPWekamPSDTFYEEFVRWQKRRTGAVPSQWR 261
Cdd:cd06622 157 LAktniGCQSYMAPErIKSGGPNQNPTYTVQSDVWSLGLSILEMALGRYPY----PPETYANIFAQLSAIVDGDPPTLPS 232
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 75570321 262 RFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWML 298
Cdd:cd06622 233 GYSDDAQDFVAKCLNKIPNRRPTYAQL---LEHPWLV 266
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
32-291 2.66e-18

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: 83.50  E-value: 2.66e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINmFGIAFETDEYYVFAQEYAP 111
Cdd:cd14665   2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQREIINHRSLRH-PNIVR-FKEVILTPTHLAIVMEYAA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 112 SGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTRRA--GSPVKRVSG 189
Cdd:cd14665  80 GGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFGYSKSSvlHSQPKSTVG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 190 TIPYTAPELCDTSKHDGfcvdYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEEFVRWQKRRTgAVPsQWRRFTDESLR 269
Cdd:cd14665 160 TPAYIAPEVLLKKEYDG----KIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKTIQRILSVQY-SIP-DYVHISPECRH 233
                       250       260
                ....*....|....*....|..
gi 75570321 270 MFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14665 234 LISRIFVADPATRITIPEIRNH 255
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
36-233 2.74e-18

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


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 84.78  E-value: 2.74e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  36 RELGKGTYGKVDLVIHK----IRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGiAFETDEYYVFAQEYAP 111
Cdd:cd05588   1 RVIGRGSYAKVLMVELKktkrIYAMKVIKKELVNDDEDIDWVQTEKHVFETASNHPFLVGLHS-CFQTESRLFFVIEFVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 112 SGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTR---RAGSPVKRVS 188
Cdd:cd05588  80 GGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLL-DSEGH-IKLTDYGMCKeglRPGDTTSTFC 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 75570321 189 GTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd05588 158 GTPNYIAPEILRGEDY-----GFSVDWWALGVLMFEMLAGRSPFD 197
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
87-233 2.89e-18

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: 84.75  E-value: 2.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGiAFETDEYYVFAQEYAPSGDL-FDIipPQVG-LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDK 164
Cdd:cd05587  57 PFLTQLHS-CFQTMDRLYFVMEYVNGGDLmYHI--QQVGkFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVML-DA 132
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75570321 165 ECRkVKLSDFGMTRR---AGSPVKRVSGTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd05587 133 EGH-IKIADFGMCKEgifGGKTTRTFCGTPDYIAPEIIAYQPYGK-----SVDWWAYGVLLYEMLAGQPPFD 198
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
89-291 2.93e-18

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: 83.64  E-value: 2.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFETDEYYVFaQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrk 168
Cdd:cd06631  65 IVGYLGTCLEDNVVSIF-MEFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGV-- 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 169 VKLSDFGMTRR---AGSPV------KRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWEKAMP-S 238
Cdd:cd06631 142 IKLIDFGCAKRlciNLSSGsqsqllKSMRGTPYWMAPEVINETGH-----GRKSDIWSIGCTVFEMATGKPPWADMNPmA 216
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 75570321 239 DTFYeefvrwQKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd06631 217 AIFA------IGSGRKPVPRLPDKFSPEARDFVHACLTRDQDERPSAEQLLKH 263
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
32-291 2.94e-18

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: 83.64  E-value: 2.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPC--PFIInMFGIAFETDEYYVF-AQE 108
Cdd:cd08223   2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLkhPNIV-SYKESFEGEDGFLYiVMG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLFDIIPPQVG--LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENilIFDKECRKVKLSDFGMTRRAGSPVKR 186
Cdd:cd08223  81 FCEGGDLYTRLKEQKGvlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQN--IFLTKSNIIKVGDLGIARVLESSSDM 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 187 VS---GTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWE-KAMPSDTFyeefvrwqKRRTGAVPSQWRR 262
Cdd:cd08223 159 ATtliGTPYYMSPELFSNKPY-----NHKSDVWALGCCVYEMATLKHAFNaKDMNSLVY--------KILEGKLPPMPKQ 225
                       250       260
                ....*....|....*....|....*....
gi 75570321 263 FTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd08223 226 YSPELGELIKAMLHQDPEKRPSVKRILRQ 254
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
97-291 3.02e-18

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: 83.54  E-value: 3.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  97 FETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFD-KECRKVKLSDFG 175
Cdd:cd14167  70 YESGGHLYLIMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSlDEDSKIMISDFG 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 176 MTR--RAGSPVKRVSGTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPwekampsdtFYEE-----FVRW 248
Cdd:cd14167 150 LSKieGSGSVMSTACGTPGYVAPEVLAQKPYSK-----AVDCWSIGVIAYILLCGYPP---------FYDEndaklFEQI 215
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 75570321 249 QKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14167 216 LKAEYEFDSPYWDDISDSAKDFIQHLMEKDPEKRFTCEQALQH 258
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
99-232 3.28e-18

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: 84.04  E-value: 3.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  99 TDEYYVFAQEYAPSGDLFDII-PPQ--VGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKV-KLSDF 174
Cdd:cd13989  70 PNDLPLLAMEYCSGGDLRKVLnQPEncCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIyKLIDL 149
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 175 GMTRR--AGSPVKRVSGTIPYTAPELCDTSKHDgFCVDYstdvWAFGVLLFCMLTGNFPW 232
Cdd:cd13989 150 GYAKEldQGSLCTSFVGTLQYLAPELFESKKYT-CTVDY----WSFGTLAFECITGYRPF 204
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
32-291 3.62e-18

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: 84.20  E-value: 3.62e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLV----------IHKIRGSKMalkflkkkstklksfLREYSIS--------LYLSPCPFIINMF 93
Cdd:cd05599   3 FEPLKVIGRGAFGEVRLVrkkdtghvyaMKKLRKSEM---------------LEKEQVAhvraerdiLAEADNPWVVKLY 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  94 gIAFETDEYYVFAQEYAPSGDLF------DIippqvgLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECR 167
Cdd:cd05599  68 -YSFQDEENLYLIMEFLPGGDMMtllmkkDT------LTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLL-DARGH 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 168 kVKLSDFGM------TRRAGSPVkrvsGTIPYTAPELCdtsKHDGFcvDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTf 241
Cdd:cd05599 140 -IKLSDFGLctglkkSHLAYSTV----GTPDYIAPEVF---LQKGY--GKECDWWSLGVIMYEMLIGYPPFCSDDPQET- 208
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 75570321 242 YEEFVRWQKrrTGAVPSQwRRFTDESLRMFRKLLALEQER--RCSVKEVFAH 291
Cdd:cd05599 209 CRKIMNWRE--TLVFPPE-VPISPEAKDLIERLLCDAEHRlgANGVEEIKSH 257
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
32-232 3.72e-18

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: 83.90  E-value: 3.72e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLViHKIRGS--------KMALKFLKKKSTKLKSFLR-EYSISLYLSPCPFIINMFgIAFETDEY 102
Cdd:cd05613   2 FELLKVLGTGAYGKVFLV-RKVSGHdagklyamKVLKKATIVQKAKTAEHTRtERQVLEHIRQSPFLVTLH-YAFQTDTK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 103 YVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRR-AG 181
Cdd:cd05613  80 LHLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILL--DSSGHVVLTDFGLSKEfLL 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 182 SPVKR---VSGTIPYTAPELCD--TSKHDGfcvdySTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd05613 158 DENERaysFCGTIEYMAPEIVRggDSGHDK-----AVDWWSLGVLMYELLTGASPF 208
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
30-297 3.85e-18

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: 83.37  E-value: 3.85e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  30 KYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKST-KLKSFLREYSISLYLSPCPFIINMFGIAFETDEYYVFAQE 108
Cdd:cd14097   1 KIYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAgSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENIL----IFDKECR-KVKLSDFGMTRRAG-- 181
Cdd:cd14097  81 LCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILvkssIIDNNDKlNIKVTDFGLSVQKYgl 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 182 --SPVKRVSGTIPYTAPELCDTSKHDGFCvdystDVWAFGVLLFCMLTGNFPWeKAMPSDTFYEEFVRWQKRRTGAVpsq 259
Cdd:cd14097 161 geDMLQETCGTPIYMAPEVISAHGYSQQC-----DIWSIGVIMYMLLCGEPPF-VAKSEEKLFEEIRKGDLTFTQSV--- 231
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 75570321 260 WRRFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWM 297
Cdd:cd14097 232 WQSVSDAAKNVLQQLLKVDPAHRMTASEL---LDNPWI 266
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
32-220 4.16e-18

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: 83.12  E-value: 4.16e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLR-EYSIslyLSPC--PFIINMFGiAFETDEYYVFAQE 108
Cdd:cd06613   2 YELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPGDDFEIIQqEISM---LKECrhPNIVAYFG-SYLRRDKLWIVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTRRAGSPV-KRV 187
Cdd:cd06613  78 YCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGD--VKLADFGVSAQLTATIaKRK 155
                       170       180       190
                ....*....|....*....|....*....|....*
gi 75570321 188 S--GTIPYTAPELCDTSKHDGFcvDYSTDVWAFGV 220
Cdd:cd06613 156 SfiGTPYWMAPEVAAVERKGGY--DGKCDIWALGI 188
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
136-231 5.09e-18

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 84.49  E-value: 5.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  136 QVAIALEYLHSKKLVHRDIKPENILIFDKecRKVKLSDFGMTR---RAGSPVKRVSGTIPYTAPELCDTSKHDGFCVDYS 212
Cdd:PLN00034 176 QILSGIAYLHRRHIVHRDIKPSNLLINSA--KNVKIADFGVSRilaQTMDPCNSSVGTIAYMSPERINTDLNHGAYDGYA 253
                         90
                 ....*....|....*....
gi 75570321  213 TDVWAFGVLLFCMLTGNFP 231
Cdd:PLN00034 254 GDIWSLGVSILEFYLGRFP 272
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
32-301 5.15e-18

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: 83.37  E-value: 5.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFGiAFETDEYYVFAQEYAP 111
Cdd:cd14104   2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVKKEISI-LNIARHRNILRLHE-SFESHEELVMIFEFIS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 112 SGDLFDII-PPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTRRAgSPVKRVSgt 190
Cdd:cd14104  80 GVDIFERItTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYIKIIEFGQSRQL-KPGDKFR-- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 191 IPYTAPELCDTSKHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTfyEEFVRwqKRRTGAVPSQWRRFTDESLRM 270
Cdd:cd14104 157 LQYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQT--IENIR--NAEYAFDDEAFKNISIEALDF 232
                       250       260       270
                ....*....|....*....|....*....|.
gi 75570321 271 FRKLLALEQERRCSVKEVfahLGHRWMLDGT 301
Cdd:cd14104 233 VDRLLVKERKSRMTAQEA---LNHPWLKQGM 260
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
32-291 5.23e-18

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: 83.38  E-value: 5.23e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKL---KSFLREYSISLYLSPcPFIINMFGIA-------FETDE 101
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKEgfpITAIREIKLLQKLDH-PNVVRLKEIVtskgsakYKGSI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 102 YYVFaqEYAPSgDLFDIIP-PQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTR-- 178
Cdd:cd07840  80 YMVF--EYMDH-DLTGLLDnPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILI-NNDGV-LKLADFGLARpy 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 179 -RAGSPV--KRVSgTIPYTAPELCDTSKHDGFCVdystDVWAFGVLLFCMLTG--------------------------N 229
Cdd:cd07840 155 tKENNADytNRVI-TLWYRPPELLLGATRYGPEV----DMWSVGCILAELFTGkpifqgkteleqlekifelcgspteeN 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75570321 230 FPWEKAMPsdtFYEEF--VRWQKRRTGAVPSQWRrfTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07840 230 WPGVSDLP---WFENLkpKKPYKRRLREVFKNVI--DPSALDLLDKLLTLDPKKRISADQALQH 288
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
36-227 6.35e-18

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: 82.40  E-value: 6.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  36 RELGKGTYGKVDLVIHKIRGSK-----MALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIAFEtdEYYVFAQEYA 110
Cdd:cd05060   1 KELGHGNFGSVRKGVYLMKSGKevevaVKTLKQEHEKAGKKEFLREASVMAQLDH-PCIVRLIGVCKG--EPLMLVMELA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTR--RAGS------ 182
Cdd:cd05060  78 PLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRH--QAKISDFGMSRalGAGSdyyrat 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 183 -----PVKrvsgtipYTAPElcdtskhdgfCVDY-----STDVWAFGVLLFCMLT 227
Cdd:cd05060 156 tagrwPLK-------WYAPE----------CINYgkfssKSDVWSYGVTLWEAFS 193
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
32-291 6.49e-18

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: 82.31  E-value: 6.49e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSfLREYSIsLYLSPCPFIINMFGIAFETDEYYVFaQEYAP 111
Cdd:cd06612   5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEI-IKEISI-LKQCDSPYIVKYYGSYFKNTDLWIV-MEYCG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 112 SGDLFDIIP-PQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECrKVKLSDFGM-TRRAGSPVKR--V 187
Cdd:cd06612  82 AGSVSDIMKiTNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILL-NEEG-QAKLADFGVsGQLTDTMAKRntV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 188 SGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWE-----KAM------PSDTFyeefvrwqkrrtgAV 256
Cdd:cd06612 160 IGTPFWMAPEVIQEIGY-----NNKADIWSLGITAIEMAEGKPPYSdihpmRAIfmipnkPPPTL-------------SD 221
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 75570321 257 PSQW-RRFTDeslrMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd06612 222 PEKWsPEFND----FVKKCLVKDPEERPSAIQLLQH 253
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
38-285 6.73e-18

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: 83.45  E-value: 6.73e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLR----EYSISLYLSPCPFIINMFgIAFETDEYYVFAQEYAPSG 113
Cdd:cd05620   3 LGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVEctmvEKRVLALAWENPFLTHLY-CTFQTKEHLFFVMEFLNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAGSPVKRVS---GT 190
Cdd:cd05620  82 DLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVML-DRDGH-IKIADFGMCKENVFGDNRAStfcGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 191 IPYTAPELCDTSKHDgfcvdYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFyeEFVRWQkrrtgaVPSQWRRFTDESLRM 270
Cdd:cd05620 160 PDYIAPEILQGLKYT-----FSVDWWSFGVLLYEMLIGQSPFHGDDEDELF--ESIRVD------TPHYPRWITKESKDI 226
                       250
                ....*....|....*
gi 75570321 271 FRKLLALEQERRCSV 285
Cdd:cd05620 227 LEKLFERDPTRRLGV 241
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
28-244 6.85e-18

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: 82.42  E-value: 6.85e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  28 VNKYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLyLSPC--PFIINMFGIaFETDEYYVF 105
Cdd:cd14083   1 IRDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDSLENEIAV-LRKIkhPNIVQLLDI-YESKSHLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 106 AQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFD-KECRKVKLSDFGMTRRAGSPV 184
Cdd:cd14083  79 VMELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSpDEDSKIMISDFGLSKMEDSGV 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75570321 185 -KRVSGTIPYTAPELCdTSKHDGFCVdystDVWAFGVLLFCMLTGNFPwekampsdtFYEE 244
Cdd:cd14083 159 mSTACGTPGYVAPEVL-AQKPYGKAV----DCWSIGVISYILLCGYPP---------FYDE 205
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
32-299 6.88e-18

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: 83.36  E-value: 6.88e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFL------REYSISLYLSPcPFIINMFGiAFETDEYYVF 105
Cdd:cd14094   5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLstedlkREASICHMLKH-PHIVELLE-TYSSDGMLYM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 106 AQEYAPSGDL-FDIIPPQVG---LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKE-CRKVKLSDFGMTRRA 180
Cdd:cd14094  83 VFEFMDGADLcFEIVKRADAgfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKEnSAPVKLGGFGVAIQL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 181 GS----PVKRVsGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPWEKAmpSDTFYEEFVrwqKRRTGAV 256
Cdd:cd14094 163 GEsglvAGGRV-GTPHFMAPEVVKREP-----YGKPVDVWGCGVILFILLSGCLPFYGT--KERLFEGII---KGKYKMN 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 75570321 257 PSQWRRFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWMLD 299
Cdd:cd14094 232 PRQWSHISESAKDLVRRMLMLDPAERITVYEA---LNHPWIKE 271
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
32-232 7.32e-18

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: 83.98  E-value: 7.32e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGS----KMALKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMfGIAFETDEYYVFAQ 107
Cdd:cd05593  17 FDYLKLLGKGTFGKVILVREKASGKyyamKILKKEVIIAKDEVAHTLTESRV-LKNTRHPFLTSL-KYSFQTKDRLCFVM 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENiLIFDKECRkVKLSDFGMTRRA---GSPV 184
Cdd:cd05593  95 EYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLEN-LMLDKDGH-IKITDFGLCKEGitdAATM 172
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 75570321 185 KRVSGTIPYTAPELCDTSKHdGFCVDYstdvWAFGVLLFCMLTGNFPW 232
Cdd:cd05593 173 KTFCGTPEYLAPEVLEDNDY-GRAVDW----WGLGVVMYEMMCGRLPF 215
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
108-291 8.04e-18

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: 82.38  E-value: 8.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILifDKECRKVKLSDFGMTRR------AG 181
Cdd:cd06653  86 EYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANIL--RDSAGNVKLGDFGASKRiqticmSG 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 182 SPVKRVSGTIPYTAPELCdtskhDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKampsdtfYEEFVRWQKRRTGAVPSQWR 261
Cdd:cd06653 164 TGIKSVTGTPYWMSPEVI-----SGEGYGRKADVWSVACTVVEMLTEKPPWAE-------YEAMAAIFKIATQPTKPQLP 231
                       170       180       190
                ....*....|....*....|....*....|
gi 75570321 262 RFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd06653 232 DGVSDACRDFLRQIFVEEKRRPTAEFLLRH 261
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
32-227 8.59e-18

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


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 83.10  E-value: 8.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKV------------DLVIHKIRGSKMALKFLKKKSTKLKSFLREYSislylspCPFIINMFGIAFET 99
Cdd:cd07842   2 YEIEGCIGRGTYGRVykakrkngkdgkEYAIKKFKGDKEQYTGISQSACREIALLRELK-------HENVVSLVEVFLEH 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 100 DE---YYVFaqEYAPSgDLFDII-----PPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI--FDKECRKV 169
Cdd:cd07842  75 ADksvYLLF--DYAEH-DLWQIIkfhrqAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgEGPERGVV 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 170 KLSDFGMTRRAGSPVK------RVSGTIPYTAPELCDTSKHdgfcvdY--STDVWAFGVLLFCMLT 227
Cdd:cd07842 152 KIGDLGLARLFNAPLKpladldPVVVTIWYRAPELLLGARH------YtkAIDIWAIGCIFAELLT 211
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
32-232 8.96e-18

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


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 83.53  E-value: 8.96e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIH----KIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFgIAFETDEYYVFAQ 107
Cdd:cd05602   9 FHFLKVIGKGSFGKVLLARHksdeKFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLH-FSFQTTDKLYFVL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRKVkLSDFGMTRRAGSPVKRV 187
Cdd:cd05602  88 DYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILL-DSQGHIV-LTDFGLCKENIEPNGTT 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 75570321 188 S---GTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd05602 166 StfcGTPEYLAPEVLHKQPY-----DRTVDWWCLGAVLYEMLYGLPPF 208
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
27-231 9.43e-18

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: 83.51  E-value: 9.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  27 EVNKYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLK--KKSTKLKSFLREYSISLYLSpCPFIINMFGI----AFET- 99
Cdd:cd07849   2 DVGPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISpfEHQTYCLRTLREIKILLRFK-HENIIGILDIqrppTFESf 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 100 -DEYYVfaQEYAPSgDLFDIIPPQVgLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECrKVKLSDFGMTR 178
Cdd:cd07849  81 kDVYIV--QELMET-DLYKLIKTQH-LSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLL-NTNC-DLKICDFGLAR 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75570321 179 RAgSPVKRVSGTIP-------YTAPELCDTSKhdgfcvDYST--DVWAFGVLLFCMLTGN--FP 231
Cdd:cd07849 155 IA-DPEHDHTGFLTeyvatrwYRAPEIMLNSK------GYTKaiDIWSVGCILAEMLSNRplFP 211
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
32-241 1.16e-17

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: 82.02  E-value: 1.16e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKkkstklksfLREYSISL--------YLSPC--PFIINMFGIAFETDE 101
Cdd:cd06610   3 YELIEVIGSGATAVVYAAYCLPKKEKVAIKRID---------LEKCQTSMdelrkeiqAMSQCnhPNVVSYYTSFVVGDE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 102 YYVfAQEYAPSGDLFDIIP---PQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFG--- 175
Cdd:cd06610  74 LWL-VMPLLSGGSLLDIMKssyPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILL--GEDGSVKIADFGvsa 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75570321 176 -------MTRRAgspVKRVSGTIPYTAPELcdTSKHDGFcvDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTF 241
Cdd:cd06610 151 slatggdRTRKV---RKTFVGTPCWMAPEV--MEQVRGY--DFKADIWSFGITAIELATGAAPYSKYPPMKVL 216
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
38-241 1.33e-17

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 82.93  E-value: 1.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHK----IRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGiAFETDEYYVFAQEYAPSG 113
Cdd:cd05591   3 LGKGSFGKVMLAERKgtdeVYAIKVLKKDVILQDDDVDCTMTEKRILALAAKHPFLTALHS-CFQTKDRLFFVMEYVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAGSPVKRVS---GT 190
Cdd:cd05591  82 DLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILL-DAEGH-CKLADFGMCKEGILNGKTTTtfcGT 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75570321 191 IPYTAPELCDTSKHdGFCVDYstdvWAFGVLLFCMLTGNFPWEKAMPSDTF 241
Cdd:cd05591 160 PDYIAPEILQELEY-GPSVDW----WALGVLMYEMMAGQPPFEADNEDDLF 205
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
28-231 1.41e-17

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: 82.99  E-value: 1.41e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  28 VNKYYEVIRELGKGTYGKVDLVIHKIRGSKMAlkflkkkstklksfL-----------------REYSISLYLSPCPFII 90
Cdd:cd07852   5 ILRRYEILKKLGKGAYGIVWKAIDKKTGEVVA--------------LkkifdafrnatdaqrtfREIMFLQELNDHPNII 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  91 NMFGI---AFETDEYYVFaqEYAPSgDLFDIIppQVGLPEPVAKRCV-HQVAIALEYLHSKKLVHRDIKPENILIfDKEC 166
Cdd:cd07852  71 KLLNViraENDKDIYLVF--EYMET-DLHAVI--RANILEDIHKQYImYQLLKALKYLHSGGVIHRDLKPSNILL-NSDC 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75570321 167 RkVKLSDFGMTRRAGSpvKRVSGTIP----------YTAPELCDTSKHdgfcvdYST--DVWAFGVLLFCMLTGN--FP 231
Cdd:cd07852 145 R-VKLADFGLARSLSQ--LEEDDENPvltdyvatrwYRAPEILLGSTR------YTKgvDMWSVGCILGEMLLGKplFP 214
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
89-232 1.72e-17

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: 81.25  E-value: 1.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFETDEYYVFaQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILifdkecR- 167
Cdd:cd06625  64 IVQYYGCLQDEKSLSIF-MEYMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANIL------Rd 136
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75570321 168 ---KVKLSDFGMTRR-----AGSPVKRVSGTIPYTAPELCDTSKHdGFcvdySTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd06625 137 sngNVKLGDFGASKRlqticSSTGMKSVTGTPYWMSPEVINGEGY-GR----KADIWSVGCTVVEMLTTKPPW 204
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
30-231 1.88e-17

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: 81.11  E-value: 1.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  30 KYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLK------KKSTKLKSFLREYSISLYLSPCPFIINMFGiAFETDEYY 103
Cdd:cd14019   1 NKYRIIEKIGEGTFSSVYKAEDKLHDLYDRNKGRLvalkhiYPTSSPSRILNELECLERLGGSNNVSGLIT-AFRNEDQV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 104 VFAQEYAPSGDLFDIIPpQVGLPEpvAKRCVHQVAIALEYLHSKKLVHRDIKPENILiFDKECRKVKLSDFGMTRRAGSP 183
Cdd:cd14019  80 VAVLPYIEHDDFRDFYR-KMSLTD--IRIYLRNLFKALKHVHSFGIIHRDVKPGNFL-YNRETGKGVLVDFGLAQREEDR 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 75570321 184 VKRVS---GTIPYTAPELCdtskhdgF-CVDYST--DVWAFGVLLFCMLTGNFP 231
Cdd:cd14019 156 PEQRApraGTRGFRAPEVL-------FkCPHQTTaiDIWSAGVILLSILSGRFP 202
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
33-233 1.95e-17

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: 82.04  E-value: 1.95e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  33 EVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSF--LREYSISLYLSPCPFIINMFGiAFETDEYYVFAQEYA 110
Cdd:cd06618  18 ENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEENKriLMDLDVVLKSHDCPYIVKCYG-YFITDSDVFICMELM 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 psGDLFD--IIPPQVGLPEPVAKRCVHQVAIALEYLHSKK-LVHRDIKPENILIFDKECrkVKLSDFGMT-RRAGSPVK- 185
Cdd:cd06618  97 --STCLDklLKRIQGPIPEDILGKMTVSIVKALHYLKEKHgVIHRDVKPSNILLDESGN--VKLCDFGISgRLVDSKAKt 172
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 75570321 186 RVSGTIPYTAPELCDTSKHDGFcvDYSTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd06618 173 RSAGCAAYMAPERIDPPDNPKY--DIRADVWSLGISLVELATGQFPYR 218
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
35-227 2.63e-17

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: 81.27  E-value: 2.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  35 IRELGKGTYGKVDLVIHKIRGSK------MALKFLKKKSTKLKSFLREYSI--SLYlspCPFIINMFGIAFETDEYYV-F 105
Cdd:cd05038   9 IKQLGEGHFGSVELCRYDPLGDNtgeqvaVKSLQPSGEEQHMSDFKREIEIlrTLD---HEYIVKYKGVCESPGRRSLrL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 106 AQEYAPSGDLFDIIP---PQVGLPEPVakRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKEcRKVKLSDFGMTRRA-- 180
Cdd:cd05038  86 IMEYLPSGSLRDYLQrhrDQIDLKRLL--LFASQICKGMEYLGSQRYIHRDLAARNILV-ESE-DLVKISDFGLAKVLpe 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75570321 181 --GSPVKRVSGTIP--YTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLT 227
Cdd:cd05038 162 dkEYYYVKEPGESPifWYAPECLRESR-----FSSASDVWSFGVTLYELFT 207
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
87-291 2.64e-17

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: 80.94  E-value: 2.64e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVFaQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKEC 166
Cdd:cd06630  63 PNIVRMLGATQHKSHFNIF-VEWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLV-DSTG 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 167 RKVKLSDFGMTRRAGSPVKRVS-------GTIPYTAPELCDTSKHDGFCvdystDVWAFGVLLFCMLTGNFPWEKAMPSD 239
Cdd:cd06630 141 QRLRIADFGAAARLASKGTGAGefqgqllGTIAFMAPEVLRGEQYGRSC-----DVWSVGCVIIEMATAKPPWNAEKISN 215
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 75570321 240 TFYEEFVRWQKRRTGAVPSQWR-RFTDESLRmfrkLLALEQERRCSVKEVFAH 291
Cdd:cd06630 216 HLALIFKIASATTPPPIPEHLSpGLRDVTLR----CLELQPEDRPPARELLKH 264
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
125-233 3.69e-17

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


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 80.80  E-value: 3.69e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 125 LPEPVAKRCVHQVAIALEYLHSKKLV---HRDIKPENILIFDKecRKVKLSDFGMTRRAGSPVKRVS------------G 189
Cdd:cd13986 103 FPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSED--DEPILMDLGSMNPARIEIEGRRealalqdwaaehC 180
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 75570321 190 TIPYTAPELCDTSKHDgfCVDYSTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd13986 181 TMPYRAPELFDVKSHC--TIDEKTDIWSLGCTLYALMYGESPFE 222
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
32-233 4.40e-17

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: 80.00  E-value: 4.40e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDL----------VIHKIRGSKMALKFLKKKstklksflREYSISLYLSPCPFIINMFGIAFETDE 101
Cdd:cd08225   2 YEIIKKIGEGSFGKIYLakaksdsehcVIKEIDLTKMPVKEKEAS--------KKEVILLAKMKHPNIVTFFASFQENGR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 102 YYVfAQEYAPSGDLFDIIPPQVGL--PEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRKVKLSDFGMTRR 179
Cdd:cd08225  74 LFI-VMEYCDGGDLMKRINRQRGVlfSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFL-SKNGMVAKLGDFGIARQ 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75570321 180 AGSPV---KRVSGTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd08225 152 LNDSMelaYTCVGTPYYLSPEICQNRPYNN-----KTDIWSLGCVLYELCTLKHPFE 203
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
32-291 4.54e-17

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: 80.78  E-value: 4.54e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKL---KSFLREYSI--SLYLSPCPFIINMFGIAF------ETD 100
Cdd:cd07838   1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEgipLSTIREIALlkQLESFEHPNVVRLLDVCHgprtdrELK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 101 EYYVFaqEYAPSgDLFDIIP--PQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKecRKVKLSDFGMTR 178
Cdd:cd07838  81 LTLVF--EHVDQ-DLATYLDkcPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSD--GQVKLADFGLAR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 179 RAGSPVKRVS--GTIPYTAPE--LCDTskhdgfcvdYST--DVWAFGVL---------LFC------MLTGNF------- 230
Cdd:cd07838 156 IYSFEMALTSvvVTLWYRAPEvlLQSS---------YATpvDMWSVGCIfaelfnrrpLFRgsseadQLGKIFdviglps 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 231 ----PWEKAMPSDTFYEEFVRwqkRRTGAVPSqwrrFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07838 227 eeewPRNSALPRSSFPSYTPR---PFKSFVPE----IDEEGLDLLKKMLTFNPHKRISAFEALQH 284
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
32-231 4.80e-17

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: 80.94  E-value: 4.80e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKF--LKKKSTKLKSFLREYSIslyLSPC--PFIINMFGiAFETDEYYVFAQ 107
Cdd:cd06615   3 FEKLGELGAGNGGVVTKVLHRPSGLIMARKLihLEIKPAIRNQIIRELKV---LHECnsPYIVGFYG-AFYSDGEISICM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLfDIIPPQVG-LPEPVAKRCVHQVAIALEYLHSK-KLVHRDIKPENILI-FDKECrkvKLSDFGMTRR----- 179
Cdd:cd06615  79 EHMDGGSL-DQVLKKAGrIPENILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVnSRGEI---KLCDFGVSGQlidsm 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 75570321 180 AGSPVkrvsGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:cd06615 155 ANSFV----GTRSYMSPERLQGTHY-----TVQSDIWSLGLSLVEMAIGRYP 197
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
38-328 4.93e-17

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: 80.85  E-value: 4.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLksflREYSISLYLSPCPFIINMFGI---AFETDEYYVFAQEYAPSGD 114
Cdd:cd14170  10 LGLGINGKVLQIFNKRTQEKFALKMLQDCPKAR----REVELHWRASQCPHIVRIVDVyenLYAGRKCLLIVMECLDGGE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 115 LFDIIPPQ--VGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKV-KLSDFGMTRRAGS--PVKRVSG 189
Cdd:cd14170  86 LFSRIQDRgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAIlKLTDFGFAKETTShnSLTTPCY 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 190 TIPYTAPELCDTSKHDGFCvdystDVWAFGVLLFCMLTGNFPWEkampSDTFYEEFVRWQKR-RTGAVP---SQWRRFTD 265
Cdd:cd14170 166 TPYYVAPEVLGPEKYDKSC-----DMWSLGVIMYILLCGYPPFY----SNHGLAISPGMKTRiRMGQYEfpnPEWSEVSE 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 266 ESLRMFRKLLALEQERRCSVKEVfahLGHRWMLDgtSGNHHQSVLNSS---SEEDELLVDRMKQQT 328
Cdd:cd14170 237 EVKMLIRNLLKTEPTQRMTITEF---MNHPWIMQ--STKVPQTPLHTSrvlKEDKERWEDVKEEMT 297
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
88-292 5.06e-17

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: 80.45  E-value: 5.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  88 FIINMfGIAFETDEYYVFAQEYAPSGDL-FDIIP-PQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKE 165
Cdd:cd05630  61 FVVSL-AYAYETKDALCLVLTLMNGGDLkFHIYHmGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHG 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 166 crKVKLSDFGMTRRA--GSPVKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWEKaMPSDTFYE 243
Cdd:cd05630 140 --HIRISDLGLAVHVpeGQTIKGRVGTVGYMAPEVVKNERY-----TFSPDWWALGCLLYEMIAGQSPFQQ-RKKKIKRE 211
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 244 EFVRWQKRrtgaVPSQW-RRFTDESLRMFRKLLALEQERR--C---SVKEVFAHL 292
Cdd:cd05630 212 EVERLVKE----VPEEYsEKFSPQARSLCSMLLCKDPAERlgCrggGAREVKEHP 262
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
131-295 5.77e-17

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: 80.43  E-value: 5.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 131 KRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRAGSPVKRVSG---TIPYTAPELCDTSkhdgf 207
Cdd:cd07873 103 KLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERG--ELKLADFGLARAKSIPTKTYSNevvTLWYRPPDILLGS----- 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 208 cVDYST--DVWAFGVLLFCMLTG--------------------NFPWEKAMPSDTFYEEFVRWQ--KRRTGAVPSQWRRF 263
Cdd:cd07873 176 -TDYSTqiDMWGVGCIFYEMSTGrplfpgstveeqlhfifrilGTPTEETWPGILSNEEFKSYNypKYRADALHNHAPRL 254
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 75570321 264 TDESLRMFRKLLALEQERRCSVKEVFAH-----LGHR 295
Cdd:cd07873 255 DSDGADLLSKLLQFEGRKRISAEEAMKHpyfhsLGER 291
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
98-243 6.52e-17

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: 79.72  E-value: 6.52e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  98 ETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRK-------VK 170
Cdd:cd14120  62 ETSSSVYLVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRKpspndirLK 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 171 LSDFGMTRR----------AGSPVkrvsgtipYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWEKAMPSD- 239
Cdd:cd14120 142 IADFGFARFlqdgmmaatlCGSPM--------YMAPEVIMSLQYDA-----KADLWSIGTIVYQCLTGKAPFQAQTPQEl 208

                ....*
gi 75570321 240 -TFYE 243
Cdd:cd14120 209 kAFYE 213
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
32-227 6.67e-17

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


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 79.85  E-value: 6.67e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSK---MALKFLKKKSTKLKSFLREYSISLYLSPC---------PFIINMFGIAFET 99
Cdd:cd08528   2 YAVLELLGSGAFGCVYKVRKKSNGQTllaLKEINMTNPAFGRTEQERDKSVGDIISEVniikeqlrhPNIVRYYKTFLEN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 100 DEYYVFAQ--EYAPSGDLFDIIPPQVG-LPEPVAKRCVHQVAIALEYLH-SKKLVHRDIKPENILIFDKEcrKVKLSDFG 175
Cdd:cd08528  82 DRLYIVMEliEGAPLGEHFSSLKEKNEhFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDD--KVTITDFG 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 176 MTRRAG---SPVKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLT 227
Cdd:cd08528 160 LAKQKGpesSKMTSVVGTILYSCPEIVQNEPY-----GEKADIWALGCILYQMCT 209
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
32-291 6.81e-17

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: 80.26  E-value: 6.81e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKL---KSFLREYSISLYLSPCPFIINMFGIAfETDE------Y 102
Cdd:cd07837   3 YEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEEgvpSTALREVSLLQMLSQSIYIVRLLDVE-HVEEngkpllY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 103 YVFaqEYAPSgDLFDIIP-----PQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRKVKLSDFGMT 177
Cdd:cd07837  82 LVF--EYLDT-DLKKFIDsygrgPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLV-DKQKGLLKIADLGLG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 178 RRAGSPVKRVSG---TIPYTAPELCDTSKHdgfcvdYST--DVWAFGVLLFCM---------------------LTGNfP 231
Cdd:cd07837 158 RAFTIPIKSYTHeivTLWYRAPEVLLGSTH------YSTpvDMWSVGCIFAEMsrkqplfpgdselqqllhifrLLGT-P 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75570321 232 WEKAMPSDTF---YEEFVRWQKRR-TGAVPSqwrrFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07837 231 NEEVWPGVSKlrdWHEYPQWKPQDlSRAVPD----LEPEGVDLLTKMLAYDPAKRISAKAALQH 290
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
35-233 6.95e-17

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: 80.16  E-value: 6.95e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  35 IRELGKGTYGKVDLVIHKIRGSKMALKFLKKKS--TKLKSFLREYSIslyLSPC--PFIINMFGiAF--ETDEYYVFAQE 108
Cdd:cd06621   6 LSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPnpDVQKQILRELEI---NKSCasPYIVKYYG-AFldEQDSSIGIAME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLfDIIPPQVG-----LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdkeCRK--VKLSDFGMTRRAG 181
Cdd:cd06621  82 YCEGGSL-DSIYKKVKkkggrIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILL----TRKgqVKLCDFGVSGELV 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 75570321 182 SPV-KRVSGTIPYTAPElcdtsKHDGFCVDYSTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd06621 157 NSLaGTFTGTSYYMAPE-----RIQGGPYSITSDVWSLGLTLLEVAQNRFPFP 204
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
32-296 7.00e-17

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: 80.07  E-value: 7.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTK---LKSFLREYSISLYLSPCPFIINMFGIaFETDEYYVFAQE 108
Cdd:cd07832   2 YKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEggiPNQALREIKALQACQGHPYVVKLRDV-FPHGTGFVLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSgDLFDIIPPQV-GLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRAGSPVKRV 187
Cdd:cd07832  81 YMLS-SLSEVLRDEErPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTG--VLKIADFGLARLFSEEDPRL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 188 S----GTIPYTAPELCDTSKhdgfcvDYST--DVWAFGVLLFCMLTGN--FPWEK------------AMPSDTFYEEFVR 247
Cdd:cd07832 158 YshqvATRWYRAPELLYGSR------KYDEgvDLWAVGCIFAELLNGSplFPGENdieqlaivlrtlGTPNEKTWPELTS 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75570321 248 ---WQK-RRTGAVPSQWRR-FTDES---LRMFRKLLALEQERRCSVKEVfahLGHRW 296
Cdd:cd07832 232 lpdYNKiTFPESKGIRLEEiFPDCSpeaIDLLKGLLVYNPKKRLSAEEA---LRHPY 285
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
136-239 7.14e-17

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: 79.36  E-value: 7.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENilIFDKECRKVKLSDFGM----TRRAGSP-VKRVSGTIPYTAPELCDTSKHDGFCVd 210
Cdd:cd14062  97 QTAQGMDYLHAKNIIHRDLKSNN--IFLHEDLTVKIGDFGLatvkTRWSGSQqFEQPTGSILWMAPEVIRMQDENPYSF- 173
                        90       100
                ....*....|....*....|....*....
gi 75570321 211 ySTDVWAFGVLLFCMLTGNFPWEKAMPSD 239
Cdd:cd14062 174 -QSDVYAFGIVLYELLTGQLPYSHINNRD 201
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
102-233 7.25e-17

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: 79.71  E-value: 7.25e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 102 YYVFaqEYAPSGDLFDIiPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRR-A 180
Cdd:cd14118  92 YMVF--ELVDKGAVMEV-PTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDG--HVKIADFGVSNEfE 166
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 181 GSPVK--RVSGTIPYTAPELCDTSKHdgfcvDYS---TDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd14118 167 GDDALlsSTAGTPAFMAPEALSESRK-----KFSgkaLDIWAMGVTLYCFVFGRCPFE 219
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
38-232 7.33e-17

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: 80.69  E-value: 7.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHK----IRGSKMALKFLKKKSTKLKSFLREYSI--SLYLSPCPFIINMfGIAFETDEYYVFAQEYAP 111
Cdd:cd05586   1 IGKGTFGQVYQVRKKdtrrIYAMKVLSKKVIVAKKEVAHTIGERNIlvRTALDESPFIVGL-KFSFQTPTDLYLVTDYMS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 112 SGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR---RAGSPVKRVS 188
Cdd:cd05586  80 GGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILL--DANGHIALCDFGLSKadlTDNKTTNTFC 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 75570321 189 GTIPYTAPELCDTSKHDGFCVDYstdvWAFGVLLFCMLTGNFPW 232
Cdd:cd05586 158 GTTEYLAPEVLLDEKGYTKMVDF----WSLGVLVFEMCCGWSPF 197
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
31-232 8.08e-17

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: 79.56  E-value: 8.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  31 YYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLS-PCpfiINMFGIAFETDEYYVFAQEY 109
Cdd:cd14108   3 YYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARRELALLAELDhKS---IVRFHDAFEKRRVVIIVTEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 110 ApSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTRR--AGSPVKRV 187
Cdd:cd14108  80 C-HEELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTDQVRICDFGNAQEltPNEPQYCK 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 75570321 188 SGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd14108 159 YGTPEFVAPEIVNQSP-----VSKVTDIWPVGVIAYLCLTGISPF 198
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
31-232 9.82e-17

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: 79.16  E-value: 9.82e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  31 YYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGiAFETDEYYVFAQEYA 110
Cdd:cd14107   3 VYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAFQERDILARLSH-RRLTCLLD-QFETRKTLILILELC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTRRAGSPVKRVS-- 188
Cdd:cd14107  81 SSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTREDIKICDFGFAQEITPSEHQFSky 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 75570321 189 GTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd14107 161 GSPEFVAPEIVHQEP-----VSAATDIWALGVIAYLSLTCHSPF 199
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
31-232 1.06e-16

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: 79.25  E-value: 1.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  31 YYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGiAFETDEYYVFAQEYA 110
Cdd:cd14113   8 FYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSLQH-PQLVGLLD-TFETPTSYILVLEMA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRK--VKLSDFGMTRRAGSP--VKR 186
Cdd:cd14113  86 DQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILV-DQSLSKptIKLADFGDAVQLNTTyyIHQ 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75570321 187 VSGTIPYTAPELCdtskhDGFCVDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd14113 165 LLGSPEFAAPEII-----LGNPVSLTSDLWSIGVLTYVLLSGVSPF 205
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
30-291 1.11e-16

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


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 80.85  E-value: 1.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  30 KYYEVIRELGKGTYGKVDLV----IHKIRGSKMALKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFgIAFETDEYYVF 105
Cdd:cd05600  11 SDFQILTQVGQGGYGSVFLArkkdTGEICALKIMKKKVLFKLNEVNHVLTERDI-LTTTNSPWLVKLL-YAFQDPENVYL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 106 AQEYAPSGDlFDIIPPQVG-LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAGSP- 183
Cdd:cd05600  89 AMEYVPGGD-FRTLLNNSGiLSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLI-DSSGH-IKLTDFGLASGTLSPk 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 184 ---------------------------------------VKRVSGTIPYTAPELCDTSKHDgFCVDYstdvWAFGVLLFC 224
Cdd:cd05600 166 kiesmkirleevkntafleltakerrniyramrkedqnyANSVVGSPDYMAPEVLRGEGYD-LTVDY----WSLGCILFE 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 225 MLTGNFPWEKAMPSDTFyEEFVRWQKRRTGAV---PSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd05600 241 CLVGFPPFSGSTPNETW-ANLYHWKKTLQRPVytdPDLEFNLSDEAWDLITKLITDPQDRLQSPEQIKNH 309
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
29-232 1.14e-16

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: 79.24  E-value: 1.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  29 NKYYEV--IRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLR-EYSISLYLSPCPfIINMFGiAFETDEYYVF 105
Cdd:cd14192   1 NSYYAVcpHEVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKnEINIMNQLNHVN-LIQLYD-AFESKTNLTL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 106 AQEYAPSGDLFD-IIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTRRAgSPV 184
Cdd:cd14192  79 IMEYVDGGELFDrITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQIKIIDFGLARRY-KPR 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75570321 185 KRVS---GTIPYTAPELCDTSkhdgfCVDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd14192 158 EKLKvnfGTPEFLAPEVVNYD-----FVSFPTDMWSVGVITYMLLSGLSPF 203
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
134-297 1.14e-16

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: 79.09  E-value: 1.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 134 VHQVAIALEYLHSKKLVHRDIKPENILIFDKecrKVKLSDFGMTRRAgspVKRVSGTIPYTAPELCDTSKHDGFCVDYST 213
Cdd:cd14109 105 VRQLLLALKHMHDLGIAHLDLRPEDILLQDD---KLKLADFGQSRRL---LRGKLTTLIYGSPEFVSPEIVNSYPVTLAT 178
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 214 DVWAFGVLLFCMLTGNFPWEkampSDTFYEEFVRWQKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVfahLG 293
Cdd:cd14109 179 DMWSVGVLTYVLLGGISPFL----GDNDRETLTNVRSGKWSFDSSPLGNISDDARDFIKKLLVYIPESRLTVDEA---LN 251

                ....
gi 75570321 294 HRWM 297
Cdd:cd14109 252 HPWF 255
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
87-291 1.21e-16

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


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 79.32  E-value: 1.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMfGIAFETDEYYVFAQEYAPSGDL----FDIIPPqvGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIF 162
Cdd:cd05605  60 RFVVSL-AYAYETKDALCLVLTIMNGGDLkfhiYNMGNP--GFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLD 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 163 DKEcrKVKLSDFGMTRR--AGSPVKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWEKampsdt 240
Cdd:cd05605 137 DHG--HVRISDLGLAVEipEGETIRGRVGTVGYMAPEVVKNERY-----TFSPDWWGLGCLIYEMIEGQAPFRA------ 203
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75570321 241 fYEEFVRWQK--RRTGAVPSQW-RRFTDESLRMFRKLLALEQERR--C---SVKEVFAH 291
Cdd:cd05605 204 -RKEKVKREEvdRRVKEDQEEYsEKFSEEAKSICSQLLQKDPKTRlgCrgeGAEDVKSH 261
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
108-291 1.62e-16

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: 78.55  E-value: 1.62e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILifDKECRKVKLSDFGMTRR------AG 181
Cdd:cd06652  86 EYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANIL--RDSVGNVKLGDFGASKRlqticlSG 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 182 SPVKRVSGTIPYTAPELCdtskhDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKampsdtfYEEFVRWQKRRTGAVPSQWR 261
Cdd:cd06652 164 TGMKSVTGTPYWMSPEVI-----SGEGYGRKADIWSVGCTVVEMLTEKPPWAE-------FEAMAAIFKIATQPTNPQLP 231
                       170       180       190
                ....*....|....*....|....*....|
gi 75570321 262 RFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd06652 232 AHVSDHCRDFLKRIFVEAKLRPSADELLRH 261
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
104-260 1.90e-16

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: 78.85  E-value: 1.90e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 104 VFAQEYAPSGDL---FDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKV-KLSDFGMTRR 179
Cdd:cd14038  74 LLAMEYCQGGDLrkyLNQFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRLIhKIIDLGYAKE 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 180 --AGSPVKRVSGTIPYTAPELCDTSKHDgFCVDYstdvWAFGVLLFCMLTGNFPWekaMPSdtfyeefvrWQkrrtgavP 257
Cdd:cd14038 154 ldQGSLCTSFVGTLQYLAPELLEQQKYT-VTVDY----WSFGTLAFECITGFRPF---LPN---------WQ-------P 209

                ...
gi 75570321 258 SQW 260
Cdd:cd14038 210 VQW 212
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
87-232 2.06e-16

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: 78.15  E-value: 2.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVFaqEYAPSGDLFDIIPpQVGLPEPVAKRCVH--QVAIALEYLHSKKLVHRDIKPENILIFDK 164
Cdd:cd05040  58 PNLIRLYGVVLSSPLMMVT--ELAPLGSLLDRLR-KDQGHFLISTLCDYavQIANGMAYLESKRFIHRDLAARNILLASK 134
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75570321 165 EcrKVKLSDFGMTRRAG--------SPVKRVSgtIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLT-GNFPW 232
Cdd:cd05040 135 D--KVKIGDFGLMRALPqnedhyvmQEHRKVP--FAWCAPESLKTRK-----FSHASDVWMFGVTLWEMFTyGEEPW 202
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
32-231 2.74e-16

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: 78.74  E-value: 2.74e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKsfLREYSISLYLSPCPFIINMFGIAFETDE-YYVFAQEYA 110
Cdd:cd14132  20 YEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKPVKKKKI--KREIKILQNLRGGPNIVKLLDVVKDPQSkTPSLIFEYV 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGDlFDIIPPQVGLPEpvAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRKVKLSDFGMT-----RRAGSPvk 185
Cdd:cd14132  98 NNTD-FKTLYPTLTDYD--IRYYMYELLKALDYCHSKGIMHRDVKPHNIMI-DHEKRKLRLIDWGLAefyhpGQEYNV-- 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75570321 186 RVsGTIPYTAPELCdtskHDGFCVDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:cd14132 172 RV-ASRYYKGPELL----VDYQYYDYSLDMWSLGCMLASMIFRKEP 212
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
38-291 2.83e-16

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: 78.53  E-value: 2.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKS-TKLKSFLREYSIslyLSPCPFIINMFGIA--FETDEYYVFAQEYAPSGD 114
Cdd:cd14173  10 LGEGAYARVQTCINLITNKEYAVKIIEKRPgHSRSRVFREVEM---LYQCQGHRNVLELIefFEEEDKFYLVFEKMRGGS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 115 LFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI-FDKECRKVKLSDFGMtrraGSPVKRVS----- 188
Cdd:cd14173  87 ILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCeHPNQVSPVKICDFDL----GSGIKLNSdcspi 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 189 ---------GTIPYTAPELCDTSKHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEE-----------FVRW 248
Cdd:cd14173 163 stpelltpcGSAEYMAPEVVEAFNEEASIYDKRCDLWSLGVILYIMLSGYPPFVGRCGSDCGWDRgeacpacqnmlFESI 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 75570321 249 QKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14173 243 QEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQH 285
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
32-291 3.01e-16

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: 78.45  E-value: 3.01e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDL-------------VIHKI--------------RGSKMALKFLKKKSTKLKSFLREYSISLYLS 84
Cdd:cd14200   2 YKLQSEIGKGSYGVVKLaynesddkyyamkVLSKKkllkqygfprrpppRGSKAAQGEQAKPLAPLERVYQEIAILKKLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  85 PCPFI--INMFGIAFETDEYYVFaqEYAPSGDLFDIiPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIF 162
Cdd:cd14200  82 HVNIVklIEVLDDPAEDNLYMVF--DLLRKGPVMEV-PSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 163 DKEcrKVKLSDFGMTRR---AGSPVKRVSGTIPYTAPE-LCDTSKhdGFCvDYSTDVWAFGVLLFCMLTGNFPwekamps 238
Cdd:cd14200 159 DDG--HVKIADFGVSNQfegNDALLSSTAGTPAFMAPEtLSDSGQ--SFS-GKALDVWAMGVTLYCFVYGKCP------- 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 239 dtFYEEFVRWQKRRTGAVPSQW---RRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14200 227 --FIDEFILALHNKIKNKPVEFpeePEISEELKDLILKMLDKNPETRITVPEIKVH 280
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
32-291 3.28e-16

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: 78.08  E-value: 3.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMA--LKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIAFEtdeyyvfaqey 109
Cdd:cd07831   1 YKILGKIGEGTFSEVLKAQSRKTGKYYAikCMKKHFKSLEQVNNLREIQALRRLSPHPNILRLIEVLFD----------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 110 APSG-----------DLFDIIPPQVG-LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECrkVKLSDFGMT 177
Cdd:cd07831  70 RKTGrlalvfelmdmNLYELIKGRKRpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI-KDDI--LKLADFGSC 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 178 RragspvkRVSGTIPYT---------APELCDTskhDGFcVDYSTDVWAFGVLLFCMLTGN--FPWEKAM---------- 236
Cdd:cd07831 147 R-------GIYSKPPYTeyistrwyrAPECLLT---DGY-YGPKMDIWAVGCVFFEILSLFplFPGTNELdqiakihdvl 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 237 --PSDTFYEEFVRW--------QKRRTGaVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07831 216 gtPDAEVLKKFRKSrhmnynfpSKKGTG-LRKLLPNASAEGLDLLKKLLAYDPDERITAKQALRH 279
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
108-291 3.38e-16

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: 77.81  E-value: 3.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILifDKECRKVKLSDFGMTRR------AG 181
Cdd:cd06651  91 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL--RDSAGNVKLGDFGASKRlqticmSG 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 182 SPVKRVSGTIPYTAPELCdtskhDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKampsdtfYEEFVRWQKRRTGAVPSQWR 261
Cdd:cd06651 169 TGIRSVTGTPYWMSPEVI-----SGEGYGRKADVWSLGCTVVEMLTEKPPWAE-------YEAMAAIFKIATQPTNPQLP 236
                       170       180       190
                ....*....|....*....|....*....|
gi 75570321 262 RFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd06651 237 SHISEHARDFLGCIFVEARHRPSAEELLRH 266
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
30-291 3.74e-16

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: 77.56  E-value: 3.74e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  30 KYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSpCPFIINMFGiAFETDEYYVFAQEY 109
Cdd:cd14111   3 KPYTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVLQEYEILKSLH-HERIMALHE-AYITPRYLVLIAEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 110 APSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTRR----AGSPVK 185
Cdd:cd14111  81 CSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNA--IKIVDFGSAQSfnplSLRQLG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 186 RVSGTIPYTAPELCdtskhDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTfyeefvrwQKRRTGAV--PSQWRRF 263
Cdd:cd14111 159 RRTGTLEYMAPEMV-----KGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQET--------EAKILVAKfdAFKLYPN 225
                       250       260
                ....*....|....*....|....*....
gi 75570321 264 TDESLRMF-RKLLALEQERRCSVKEVFAH 291
Cdd:cd14111 226 VSQSASLFlKKVLSSYPWSRPTTKDCFAH 254
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
38-233 4.23e-16

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: 78.50  E-value: 4.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHK----IRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGiAFETDEYYVFAQEYAPSG 113
Cdd:cd05615  18 LGKGSFGKVMLAERKgsdeLYAIKILKKDVVIQDDDVECTMVEKRVLALQDKPPFLTQLHS-CFQTVDRLYFVMEYVNGG 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPpQVG-LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRR---AGSPVKRVSG 189
Cdd:cd05615  97 DLMYHIQ-QVGkFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVML-DSEGH-IKIADFGMCKEhmvEGVTTRTFCG 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 75570321 190 TIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd05615 174 TPDYIAPEIIAYQPY-----GRSVDWWAYGVLLYEMLAGQPPFD 212
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
88-282 4.37e-16

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: 77.73  E-value: 4.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  88 FIINMfGIAFETDEYYVFAQEYAPSGDL-FDIIppQVGLPEPVAKRCVHQVA---IALEYLHSKKLVHRDIKPENILIFD 163
Cdd:cd05631  61 FVVSL-AYAYETKDALCLVLTIMNGGDLkFHIY--NMGNPGFDEQRAIFYAAelcCGLEDLQRERIVYRDLKPENILLDD 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 164 keCRKVKLSDFGMTRR--AGSPVKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWEKampsdtf 241
Cdd:cd05631 138 --RGHIRISDLGLAVQipEGETVRGRVGTVGYMAPEVINNEKY-----TFSPDWWGLGCLIYEMIQGQSPFRK------- 203
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 75570321 242 YEEFVRWQK--RRTGAVPSQW-RRFTDESLRMFRKLLALEQERR 282
Cdd:cd05631 204 RKERVKREEvdRRVKEDQEEYsEKFSEDAKSICRMLLTKNPKER 247
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
87-233 4.38e-16

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 79.84  E-value: 4.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   87 PFIINMF--GiafETDEYYVFAQEYAPSGDLFDIIppQVGLPEPVaKRCVH---QVAIALEYLHSKKLVHRDIKPENILI 161
Cdd:NF033483  67 PNIVSVYdvG---EDGGIPYIVMEYVDGRTLKDYI--REHGPLSP-EEAVEimiQILSALEHAHRNGIVHRDIKPQNILI 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  162 fDKEcRKVKLSDFG---------MTRRAGspvkrVSGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:NF033483 141 -TKD-GRVKVTDFGiaralssttMTQTNS-----VLGTVHYLSPEQARGGT-----VDARSDIYSLGIVLYEMLTGRPPF 208

                 .
gi 75570321  233 E 233
Cdd:NF033483 209 D 209
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
74-291 5.26e-16

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: 77.36  E-value: 5.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  74 LREYSISLYLSPcPFIINMFGIaFETD-EYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYL--HSKKLV 150
Cdd:cd13990  52 LREYEIHKSLDH-PRIVKLYDV-FEIDtDSFCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPII 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 151 HRDIKPENILIFDKE-CRKVKLSDFG----MTRRAGSP-----VKRVSGTIPYTAPELCDTSKhDGFCVDYSTDVWAFGV 220
Cdd:cd13990 130 HYDLKPGNILLHSGNvSGEIKITDFGlskiMDDESYNSdgmelTSQGAGTYWYLPPECFVVGK-TPPKISSKVDVWSVGV 208
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75570321 221 LLFCMLTGNFPWEKAMPSDTFYEEFVrWQKRRTGAVPSQwRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd13990 209 IFYQMLYGRKPFGHNQSQEAILEENT-ILKATEVEFPSK-PVVSSEAKDFIRRCLTYRKEDRPDVLQLAND 277
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
140-291 5.39e-16

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: 77.61  E-value: 5.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 140 ALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRAGSPVKRVSG---TIPYTAPELCDTSKHDGFCVdystDVW 216
Cdd:cd07841 114 GLEYLHSNWILHRDLKPNNLLIASDG--VLKLADFGLARSFGSPNRKMTHqvvTRWYRAPELLFGARHYGVGV----DMW 187
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 217 AFGVLLFCMLTGN--FPWEKAM------------PSDTFYEE------FVRWQKrRTGavPSQWRRFT---DESLRMFRK 273
Cdd:cd07841 188 SVGCIFAELLLRVpfLPGDSDIdqlgkifealgtPTEENWPGvtslpdYVEFKP-FPP--TPLKQIFPaasDDALDLLQR 264
                       170
                ....*....|....*...
gi 75570321 274 LLALEQERRCSVKEVFAH 291
Cdd:cd07841 265 LLTLNPNKRITARQALEH 282
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
87-232 7.12e-16

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: 77.00  E-value: 7.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFEtDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCV--H-------QVAIALEYLHSKKLV---HRDI 154
Cdd:cd14146  53 PNIIKLEGVCLE-EPNLCLVMEFARGGTLNRALAAANAAPGPRRARRIppHilvnwavQIARGMLYLHEEAVVpilHRDL 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 155 KPENILIFDKE-----CRK-VKLSDFGMTRRAGSPVK-RVSGTIPYTAPELCDTSkhdgfCVDYSTDVWAFGVLLFCMLT 227
Cdd:cd14146 132 KSSNILLLEKIehddiCNKtLKITDFGLAREWHRTTKmSAAGTYAWMAPEVIKSS-----LFSKGSDIWSYGVLLWELLT 206

                ....*
gi 75570321 228 GNFPW 232
Cdd:cd14146 207 GEVPY 211
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
87-233 7.16e-16

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: 76.71  E-value: 7.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVFaQEYAPSGDLFDIIPPQVGLPEPVAKRCVH---QVAIALEYLHS---KKLVHRDIKPENIL 160
Cdd:cd14058  46 PNIIKLYGACSNQKPVCLV-MEYAEGGSLYNVLHGKEPKPIYTAAHAMSwalQCAKGVAYLHSmkpKALIHRDLKPPNLL 124
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75570321 161 IFDKEcRKVKLSDFGMTRRAGSPVKRVSGTIPYTAPELCDTSKHDGFCvdystDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd14058 125 LTNGG-TVLKICDFGTACDISTHMTNNKGSAAWMAPEVFEGSKYSEKC-----DVFSWGIILWEVITRRKPFD 191
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
97-289 8.64e-16

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: 76.51  E-value: 8.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  97 FETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKecRKVKLSDFGM 176
Cdd:cd14187  76 FEDNDFVYVVLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDD--MEVKIGDFGL 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 177 TRRA---GSPVKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWEkampSDTFYEEFVRWQKRRT 253
Cdd:cd14187 154 ATKVeydGERKKTLCGTPNYIAPEVLSKKGH-----SFEVDIWSIGCIMYTLLVGKPPFE----TSCLKETYLRIKKNEY 224
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 75570321 254 gAVPsqwRRFTDESLRMFRKLLALEQERRCSVKEVF 289
Cdd:cd14187 225 -SIP---KHINPVAASLIQKMLQTDPTARPTINELL 256
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
32-282 1.06e-15

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 77.33  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   32 YEVIRELGKGTYGKVDLVIHKIR-----GSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGiAFETDEYYVFA 106
Cdd:PTZ00426  32 FNFIRTLGTGSFGRVILATYKNEdfppvAIKRFEKSKIIKQKQVDHVFSERKILNYINH-PFCVNLYG-SFKDESYLYLV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  107 QEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAGSPVKR 186
Cdd:PTZ00426 110 LEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLL-DKDGF-IKMTDFGFAKVVDTRTYT 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  187 VSGTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPwekampsdtFY--EEFVRWQKRRTGAVpsQWRRFT 264
Cdd:PTZ00426 188 LCGTPEYIAPEILLNVGHGK-----AADWWTLGIFIYEILVGCPP---------FYanEPLLIYQKILEGII--YFPKFL 251
                        250
                 ....*....|....*....
gi 75570321  265 DESLR-MFRKLLALEQERR 282
Cdd:PTZ00426 252 DNNCKhLMKKLLSHDLTKR 270
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
87-291 1.07e-15

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: 76.33  E-value: 1.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVfAQEYAPSGDLFDIIPpQVGLPEP-VAKRCVhQVAIALEYLHSKKLVHRDIKPENILIfdKE 165
Cdd:cd06648  64 PNIVEMYSSYLVGDELWV-VMEFLEGGALTDIVT-HTRMNEEqIATVCR-AVLKALSFLHSQGVIHRDIKSDSILL--TS 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 166 CRKVKLSDFGMTRRAGSPV-KRVS--GTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWekampsdtFY 242
Cdd:cd06648 139 DGRVKLSDFGFCAQVSKEVpRRKSlvGTPYWMAPEVISRLPYGT-----EVDIWSLGIMVIEMVDGEPPY--------FN 205
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 75570321 243 EEFVRWQKRRTGAVPSQWRRFTDES--LRMF-RKLLALEQERRCSVKEVFAH 291
Cdd:cd06648 206 EPPLQAMKRIRDNEPPKLKNLHKVSprLRSFlDRMLVRDPAQRATAAELLNH 257
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
86-231 1.07e-15

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: 76.51  E-value: 1.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  86 CPFIINMFGIAFETDEYYVFaQEYAPSGDLFDIIPPQvGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKE 165
Cdd:cd06609  58 SPYITKYYGSFLKGSKLWII-MEYCGGGSVLDLLKPG-PLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILL--SE 133
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 166 CRKVKLSDFGMTRRAGSPVKRVS---GTiPY-TAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:cd06609 134 EGDVKLADFGVSGQLTSTMSKRNtfvGT-PFwMAPEVIKQSGY-----DEKADIWSLGITAIELAKGEPP 197
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
32-227 1.15e-15

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: 76.39  E-value: 1.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKL---KSFLREYSISLYLSPcPFIINMFG-IAFETDEYYVFaq 107
Cdd:cd07860   2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEgvpSTAIREISLLKELNH-PNIVKLLDvIHTENKLYLVF-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYApSGDL---FDIIPPQvGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAGSPV 184
Cdd:cd07860  79 EFL-HQDLkkfMDASALT-GIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLI--NTEGAIKLADFGLARAFGVPV 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 75570321 185 KRVSG---TIPYTAPELCDTSKHdgfcvdYST--DVWAFGVLLFCMLT 227
Cdd:cd07860 155 RTYTHevvTLWYRAPEILLGCKY------YSTavDIWSLGCIFAEMVT 196
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
32-231 1.18e-15

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: 77.02  E-value: 1.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKF--LKKKSTKLKSFLREYSIsLYLSPCPFIINMFGiAFETDEYYVFAQEY 109
Cdd:cd06650   7 FEKISELGAGNGGVVFKVSHKPSGLVMARKLihLEIKPAIRNQIIRELQV-LHECNSPYIVGFYG-AFYSDGEISICMEH 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 110 APSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSK-KLVHRDIKPENILIFDKEcrKVKLSDFGMT-RRAGSPVKRV 187
Cdd:cd06650  85 MDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRG--EIKLCDFGVSgQLIDSMANSF 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 75570321 188 SGTIPYTAPElcdtsKHDGFCVDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:cd06650 163 VGTRSYMSPE-----RLQGTHYSVQSDIWSMGLSLVEMAVGRYP 201
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
32-233 1.53e-15

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: 75.62  E-value: 1.53e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHK----------IRGSKMALKFLKKKStklksflREYSISLYLSPcPFIINmFGIAFETDE 101
Cdd:cd08218   2 YVRIKKIGEGSFGKALLVKSKedgkqyvikeINISKMSPKEREESR-------KEVAVLSKMKH-PNIVQ-YQESFEENG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 102 YYVFAQEYAPSGDLFDIIPPQVGL--PEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENilIFDKECRKVKLSDFGMTRR 179
Cdd:cd08218  73 NLYIVMDYCDGGDLYKRINAQRGVlfPEDQILDWFVQLCLALKHVHDRKILHRDIKSQN--IFLTKDGIIKLGDFGIARV 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75570321 180 AGSPV---KRVSGTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd08218 151 LNSTVelaRTCIGTPYYLSPEICENKPYNN-----KSDIWALGCVLYEMCTLKHAFE 202
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
32-220 1.54e-15

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: 76.19  E-value: 1.54e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIAF------ETDEYYvF 105
Cdd:cd06608   8 FELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKLEINILRKFSNHPNIATFYGAFIkkdppgGDDQLW-L 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 106 AQEYAPSGDLFD----IIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAG 181
Cdd:cd06608  87 VMEYCGGGSVTDlvkgLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILL-TEEAE-VKLVDFGVSAQLD 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 75570321 182 SPVKR---VSGTiPY-TAPELCDTSKHDGFCVDYSTDVWAFGV 220
Cdd:cd06608 165 STLGRrntFIGT-PYwMAPEVIACDQQPDASYDARCDVWSLGI 206
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
87-291 2.49e-15

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: 74.95  E-value: 2.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDE-YYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKK--LVHRDIKPENILIfD 163
Cdd:cd13983  60 PNIIKFYDSWESKSKkEVIFITELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFI-N 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 164 KECRKVKLSDFGM-TRRAGSPVKRVSGTIPYTAPELCDTSkhdgfcVDYSTDVWAFGVLLFCMLTGNFPW-EKAMPSDTF 241
Cdd:cd13983 139 GNTGEVKIGDLGLaTLLRQSFAKSVIGTPEFMAPEMYEEH------YDEKVDIYAFGMCLLEMATGEYPYsECTNAAQIY 212
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 75570321 242 yeefvrwQKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd13983 213 -------KKVTSGIKPESLSKVKDPELKDFIEKCLKPPDERPSARELLEH 255
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
127-297 2.75e-15

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: 74.88  E-value: 2.75e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 127 EPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTRRAGSPVKR-VSGTIPYTAPELCDTSKHd 205
Cdd:cd14112  98 EEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQVKLVDFGRAQKVSKLGKVpVDGDTDWASPEFHNPETP- 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 206 gfcVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEEFVRWQKRRTGAVPSQwrrFTDESLRMFRKLLALEQERRCSV 285
Cdd:cd14112 177 ---ITVQSDIWGLGVLTFCLLSGFHPFTSEYDDEEETKENVIFVKCRPNLIFVE---ATQEALRFATWALKKSPTRRMRT 250
                       170
                ....*....|..
gi 75570321 286 KEVFAhlgHRWM 297
Cdd:cd14112 251 DEALE---HRWL 259
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
97-309 2.99e-15

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: 75.47  E-value: 2.99e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  97 FETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFD-KECRKVKLSDFG 175
Cdd:cd14168  77 YESPNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSqDEESKIMISDFG 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 176 MTRRAGSP--VKRVSGTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWEKAMPSDTFyEEFVRWQKRRT 253
Cdd:cd14168 157 LSKMEGKGdvMSTACGTPGYVAPEVLAQKPYSK-----AVDCWSIGVIAYILLCGYPPFYDENDSKLF-EQILKADYEFD 230
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 254 GAVpsqWRRFTDESLRMFRKLLALEQERRCSVKEVfahLGHRWMLDGTS--GNHHQSV 309
Cdd:cd14168 231 SPY---WDDISDSAKDFIRNLMEKDPNKRYTCEQA---LRHPWIAGDTAlcKNIHESV 282
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
38-228 3.01e-15

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: 75.82  E-value: 3.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGS----KMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFgIAFETDEYYVFAQEYAPSG 113
Cdd:cd05575   3 IGKGSFGKVLLARHKAEGKlyavKVLQKKAILKRNEVKHIMAERNVLLKNVKHPFLVGLH-YSFQTKDKLYFVLDYVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILiFDKECRkVKLSDFGMTRRAGSPVKRVS---GT 190
Cdd:cd05575  82 ELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENIL-LDSQGH-VVLTDFGLCKEGIEPSDTTStfcGT 159
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 75570321 191 IPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTG 228
Cdd:cd05575 160 PEYLAPEVLRKQPY-----DRTVDWWCLGAVLYEMLYG 192
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
29-291 3.05e-15

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: 74.96  E-value: 3.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  29 NKYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIAFETDEYYVfAQE 108
Cdd:cd06647   6 KKKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWV-VME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLFDIIPP---QVGLPEPVAKRCVHqvaiALEYLHSKKLVHRDIKPENILI-FDKEcrkVKLSDFGMTRRAgSPV 184
Cdd:cd06647  85 YLAGGSLTDVVTEtcmDEGQIAAVCRECLQ----ALEFLHSNQVIHRDIKSDNILLgMDGS---VKLTDFGFCAQI-TPE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 KRVSGTI---PY-TAPELCdTSKHDGFCVdystDVWAFGVLLFCMLTGNFPWEKAMPSDTFY-------EEFVRWQKrrt 253
Cdd:cd06647 157 QSKRSTMvgtPYwMAPEVV-TRKAYGPKV----DIWSLGIMAIEMVEGEPPYLNENPLRALYliatngtPELQNPEK--- 228
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 75570321 254 gaVPSQWRRFTDESLRMfrkllalEQERRCSVKEVFAH 291
Cdd:cd06647 229 --LSAIFRDFLNRCLEM-------DVEKRGSAKELLQH 257
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
10-282 3.21e-15

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: 76.59  E-value: 3.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  10 DILEELQLYTAQnleklevnkyYEVIRELGKGTYGKVDLV----IHKIRGSKMaLKFLKKKSTKLKSFLREYSISLYLSP 85
Cdd:cd05624  62 QLVKEMQLHRDD----------FEIIKVIGRGAFGEVAVVkmknTERIYAMKI-LNKWEMLKRAETACFREERNVLVNGD 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  86 CPFIINMFgIAFETDEYYVFAQEYAPSGDLFDIIPP-QVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDK 164
Cdd:cd05624 131 CQWITTLH-YAFQDENYLYLVMDYYVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLL-DM 208
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 165 ECRkVKLSDFG----MTRRAGSPVKRVSGTIPYTAPELCDtSKHDGFCvDY--STDVWAFGVLLFCMLTGNFPWEKAMPS 238
Cdd:cd05624 209 NGH-IRLADFGsclkMNDDGTVQSSVAVGTPDYISPEILQ-AMEDGMG-KYgpECDWWSLGVCMYEMLYGETPFYAESLV 285
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 75570321 239 DTF-----YEEfvRWQkrrtgaVPSQWRRFTDESLRMFRKLLAlEQERR 282
Cdd:cd05624 286 ETYgkimnHEE--RFQ------FPSHVTDVSEEAKDLIQRLIC-SRERR 325
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
87-223 4.29e-15

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: 74.40  E-value: 4.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVfAQEYAPSGDLFDII-PPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKE 165
Cdd:cd05041  53 PNIVKLIGVCVQKQPIMI-VMELVPGGSLLTFLrKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENN 131
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75570321 166 crKVKLSDFGMTRRAGSPVKRVS---GTIP--YTAPELCDTSKHDGFCvdystDVWAFGVLLF 223
Cdd:cd05041 132 --VLKISDFGMSREEEDGEYTVSdglKQIPikWTAPEALNYGRYTSES-----DVWSFGILLW 187
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
32-225 4.72e-15

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: 74.23  E-value: 4.72e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSF----LREysISLYLSPC-PFIINMFGIAFETDEYYVfA 106
Cdd:cd08224   2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMDAKArqdcLKE--IDLLQQLNhPNIIKYLASFIENNELNI-V 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 107 QEYAPSGDLFDII----PPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTR---- 178
Cdd:cd08224  79 LELADAGDLSRLIkhfkKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANG--VVKLGDLGLGRffss 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 75570321 179 ---RAGSPVkrvsGTIPYTAPELCdtsKHDGFcvDYSTDVWAFGVLLFCM 225
Cdd:cd08224 157 kttAAHSLV----GTPYYMSPERI---REQGY--DFKSDIWSLGCLLYEM 197
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
33-222 4.73e-15

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: 74.31  E-value: 4.73e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  33 EVIRELGKGTYGKVDLVIHkiRGSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIAFETDEYYVFAqEYAPS 112
Cdd:cd05039   9 KLGELIGKGEFGDVMLGDY--RGQKVAVKCLKDDSTAAQAFLAEASVMTTLRH-PNLVQLLGVVLEGNGLYIVT-EYMAK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 113 GDLFDIIPP---QVglpepVAKRCVHQVAI----ALEYLHSKKLVHRDIKPENILIFDKECRKVklSDFGMTRRAGSPVK 185
Cdd:cd05039  85 GSLVDYLRSrgrAV-----ITRKDQLGFALdvceGMEYLESKKFVHRDLAARNVLVSEDNVAKV--SDFGLAKEASSNQD 157
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 75570321 186 rvSGTIP--YTAPElcdTSKHDGFCVdySTDVWAFGVLL 222
Cdd:cd05039 158 --GGKLPikWTAPE---ALREKKFST--KSDVWSFGILL 189
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
136-232 5.06e-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: 74.28  E-value: 5.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENilIFDKECRKVKLSDFGM----TRRAGS-PVKRVSGTIPYTAPELCDTSKHDGFcvD 210
Cdd:cd14150 104 QTAQGMDYLHAKNIIHRDLKSNN--IFLHEGLTVKIGDFGLatvkTRWSGSqQVEQPSGSILWMAPEVIRMQDTNPY--S 179
                        90       100
                ....*....|....*....|..
gi 75570321 211 YSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd14150 180 FQSDVYAYGVVLYELMSGTLPY 201
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
133-291 5.25e-15

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


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 74.66  E-value: 5.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 133 CVHQVAI-------ALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRAGSPVKRVSG---TIPYTAPELCDTS 202
Cdd:cd07871 101 SMHNVKIfmfqllrGLSYCHKRKILHRDLKPQNLLINEKG--ELKLADFGLARAKSVPTKTYSNevvTLWYRPPDVLLGS 178
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 203 khdgfcVDYST--DVWAFGVLLFCMLTG--------------------NFPWEKAMPSDTFYEEFVRWQ--KRRTGAVPS 258
Cdd:cd07871 179 ------TEYSTpiDMWGVGCILYEMATGrpmfpgstvkeelhlifrllGTPTEETWPGVTSNEEFRSYLfpQYRAQPLIN 252
                       170       180       190
                ....*....|....*....|....*....|...
gi 75570321 259 QWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07871 253 HAPRLDTDGIDLLSSLLLYETKSRISAEAALRH 285
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
38-291 5.72e-15

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: 73.89  E-value: 5.72e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGK----VDLVIHKIRGSKMALKFLKKKSTKLKSFLREysISLYLSPCPFIINMFGIAFETDEYYVFAQEYAPSG 113
Cdd:cd14188   9 LGKGGFAKcyemTDLTTNKVYAAKIIPHSRVSKPHQREKIDKE--IELHRILHHKHVVQFYHYFEDKENIYILLEYCSRR 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRR---AGSPVKRVSGT 190
Cdd:cd14188  87 SMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFI--NENMELKVGDFGLAARlepLEHRRRTICGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 191 IPYTAPELCDTSKHDgfCvdySTDVWAFGVLLFCMLTGNFPWEKAMPSDTFyeefvRWQKRRTGAVPSQwrrFTDESLRM 270
Cdd:cd14188 165 PNYLSPEVLNKQGHG--C---ESDIWALGCVMYTMLLGRPPFETTNLKETY-----RCIREARYSLPSS---LLAPAKHL 231
                       250       260
                ....*....|....*....|.
gi 75570321 271 FRKLLALEQERRCSVKEVFAH 291
Cdd:cd14188 232 IASMLSKNPEDRPSLDEIIRH 252
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
38-245 6.56e-15

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: 74.31  E-value: 6.56e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISL----YLSPCPFIINMFGiAFETDEYYVFAQEYAPSG 113
Cdd:cd05047   3 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELevlcKLGHHPNIINLLG-ACEHRGYLYLAIEYAPHG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDII--------PPQVGLPEPVAKRCVHQ--------VAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMT 177
Cdd:cd05047  82 NLLDFLrksrvletDPAFAIANSTASTLSSQqllhfaadVARGMDYLSQKQFIHRDLAARNILVGENYV--AKIADFGLS 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75570321 178 RRAGSPVKRVSGTIP--YTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLT-GNFPWeKAMPSDTFYEEF 245
Cdd:cd05047 160 RGQEVYVKKTMGRLPvrWMAIESLNYSVYTT-----NSDVWSYGVLLWEIVSlGGTPY-CGMTCAELYEKL 224
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
87-234 6.62e-15

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: 73.87  E-value: 6.62e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFEtDEYYVFAQEYAPSGDLFDI-----IPPQVGLPEPVakrcvhQVAIALEYLHSKKLV---HRDIKPEN 158
Cdd:cd14148  53 PNIIALRGVCLN-PPHLCLVMEYARGGALNRAlagkkVPPHVLVNWAV------QIARGMNYLHNEAIVpiiHRDLKSSN 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 159 ILIFDKECRK------VKLSDFGMTRRAGSPVK-RVSGTIPYTAPELCdtsKHDGFcvDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:cd14148 126 ILILEPIENDdlsgktLKITDFGLAREWHKTTKmSAAGTYAWMAPEVI---RLSLF--SKSSDVWSFGVLLWELLTGEVP 200

                ...
gi 75570321 232 WEK 234
Cdd:cd14148 201 YRE 203
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
108-227 7.23e-15

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: 73.62  E-value: 7.23e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVG--LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENilIFDKECRKVKLSDFGMTRRAGSP-- 183
Cdd:cd08221  79 EYCNGGNLHDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLN--IFLTKADLVKLGDFGISKVLDSEss 156
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 75570321 184 -VKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLT 227
Cdd:cd08221 157 mAESIVGTPYYMSPELVQGVKY-----NFKSDIWAVGCVLYELLT 196
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
98-291 9.90e-15

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: 73.15  E-value: 9.90e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  98 ETDEYYVFAQEYapsGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLS---DF 174
Cdd:cd14022  57 ETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLEsleDA 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 175 GMTRRAGSPVKRVSGTIPYTAPELCDTSkhdGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFyeefvrwQKRRTG 254
Cdd:cd14022 134 YILRGHDDSLSDKHGCPAYVSPEILNTS---GSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLF-------SKIRRG 203
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 75570321 255 A--VPSQwrrFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14022 204 QfnIPET---LSPKAKCLIRSILRREPSERLTSQEILDH 239
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
87-291 1.50e-14

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: 73.48  E-value: 1.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVFaQEYAPSGDLFDIIPpQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI-FDKe 165
Cdd:cd06659  78 PNVVEMYKSYLVGEELWVL-MEYLQGGALTDIVS-QTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLtLDG- 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 166 crKVKLSDFGMTRRAGSPV-KRVS--GTIPYTAPELCDTSKhdgfcvdYST--DVWAFGVLLFCMLTGNFPWekampsdt 240
Cdd:cd06659 155 --RVKLSDFGFCAQISKDVpKRKSlvGTPYWMAPEVISRCP-------YGTevDIWSLGIMVIEMVDGEPPY-------- 217
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 75570321 241 FYEEFVRWQKRRTGAVPSQWRRFTDES--LRMF-RKLLALEQERRCSVKEVFAH 291
Cdd:cd06659 218 FSDSPVQAMKRLRDSPPPKLKNSHKASpvLRDFlERMLVRDPQERATAQELLDH 271
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
124-231 1.59e-14

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: 73.23  E-value: 1.59e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 124 GLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAGSPVKRVS---GTIPYTAPELCD 200
Cdd:cd07846  96 GLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILV--SQSGVVKLCDFGFARTLAAPGEVYTdyvATRWYRAPELLV 173
                        90       100       110
                ....*....|....*....|....*....|...
gi 75570321 201 TSKHDGFCVdystDVWAFGVLLFCMLTGN--FP 231
Cdd:cd07846 174 GDTKYGKAV----DVWAVGCLVTEMLTGEplFP 202
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
126-228 1.80e-14

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: 72.69  E-value: 1.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 126 PEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI---FDKECRKVKLSDFGMTRR----AGSPVKR--VSGTIPYTAP 196
Cdd:cd13982  97 PGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILIstpNAHGNVRAMISDFGLCKKldvgRSSFSRRsgVAGTSGWIAP 176
                        90       100       110
                ....*....|....*....|....*....|..
gi 75570321 197 ELCDTSKHDGfcVDYSTDVWAFGVLLFCMLTG 228
Cdd:cd13982 177 EMLSGSTKRR--QTRAVDIFSLGCVFYYVLSG 206
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
108-233 1.87e-14

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: 72.43  E-value: 1.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLF-----DIIPPQVGLPEPVakrcvhQVAIALEYLHSKK---LVHRDIKPENILIFDK-----ECRKV-KLSD 173
Cdd:cd14061  73 EYARGGALNrvlagRKIPPHVLVDWAI------QIARGMNYLHNEApvpIIHRDLKSSNILILEAienedLENKTlKITD 146
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75570321 174 FGMTRRAgSPVKRVS--GTIPYTAPELCDTSKHDgfcvdYSTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd14061 147 FGLAREW-HKTTRMSaaGTYAWMAPEVIKSSTFS-----KASDVWSYGVLLWELLTGEVPYK 202
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
87-233 1.94e-14

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


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 73.03  E-value: 1.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETdeyYVFAQEYAPSGDLFDII----PPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIF 162
Cdd:cd14000  70 PSIVYLLGIGIHP---LMLVLELAPLGSLDHLLqqdsRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVW 146
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 163 D---KECRKVKLSDFGMTRR-AGSPVKRVSGTIPYTAPELcdtsKHDGFCVDYSTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd14000 147 TlypNSAIIIKIADYGISRQcCRMGAKGSEGTPGFRAPEI----ARGNVIYNEKVDVFSFGMLLYEILSGGAPMV 217
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
27-231 3.00e-14

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: 72.54  E-value: 3.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  27 EVNKYYEVIRELGKGTYGKVDLVIHKIRGSKMAlkflkkkstklksfL-----------REYSISLYLSpCPFIINMFGi 95
Cdd:cd14137   1 PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVA--------------IkkvlqdkryknRELQIMRRLK-HPNIVKLKY- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  96 AFET-----DEYYVF-AQEYAPSgDLFDII----PPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKE 165
Cdd:cd14137  65 FFYSsgekkDEVYLNlVMEYMPE-TLYRVIrhysKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLV-DPE 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 166 CRKVKLSDFGMTRR--AGSPvkRVS--GTIPYTAPELCdtskhdgF-CVDYST--DVWAFGVLLFCMLTGN--FP 231
Cdd:cd14137 143 TGVLKLCDFGSAKRlvPGEP--NVSyiCSRYYRAPELI-------FgATDYTTaiDIWSAGCVLAELLLGQplFP 208
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
32-291 3.04e-14

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: 72.19  E-value: 3.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHK----------IRGSKMALKFLKKKstklksfLREYSISLYLSPcPFIINMFGIAFETDE 101
Cdd:cd08217   2 YEVLETIGKGSFGTVRKVRRKsdgkilvwkeIDYGKMSEKEKQQL-------VSEVNILRELKH-PNIVRYYDRIVDRAN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 102 YYVF-AQEYAPSGDLFDIIppQVG------LPEPVAKRCVHQVAIALEYLH-----SKKLVHRDIKPENILIFDKECrkV 169
Cdd:cd08217  74 TTLYiVMEYCEGGDLAQLI--KKCkkenqyIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDNN--V 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 170 KLSDFGMTRRAGSPVKRVS---GTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWEKAMpsdtfYEEFV 246
Cdd:cd08217 150 KLGDFGLARVLSHDSSFAKtyvGTPYYMSPELLNEQSYDE-----KSDIWSLGCLIYELCALHPPFQAAN-----QLELA 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 75570321 247 rwQKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd08217 220 --KKIKEGKFPRIPSRYSSELNEVIKSMLNVDPDKRPSVEELLQL 262
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
96-291 3.17e-14

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


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 73.51  E-value: 3.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  96 AFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI-FDKEcrkVKLSDF 174
Cdd:cd05626  69 SFQDKDNLYFVMDYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIdLDGH---IKLTDF 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 175 GMTR-----------RAGSPVKRVS---------------------------------------GTIPYTAPELCDTSKH 204
Cdd:cd05626 146 GLCTgfrwthnskyyQKGSHIRQDSmepsdlwddvsncrcgdrlktleqratkqhqrclahslvGTPNYIAPEVLLRKGY 225
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 205 DGFCvdystDVWAFGVLLFCMLTGNFPWEKAMPSDTFYeEFVRWQKrrTGAVPSQwRRFTDESLRMFRKLLALEQER--R 282
Cdd:cd05626 226 TQLC-----DWWSVGVILFEMLVGQPPFLAPTPTETQL-KVINWEN--TLHIPPQ-VKLSPEAVDLITKLCCSAEERlgR 296

                ....*....
gi 75570321 283 CSVKEVFAH 291
Cdd:cd05626 297 NGADDIKAH 305
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
88-232 3.42e-14

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: 72.22  E-value: 3.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  88 FIINMfGIAFETDEYYVFAQEYAPSGDL----FDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFD 163
Cdd:cd05608  62 FIVSL-AYAFQTKTDLCLVMTIMNGGDLryhiYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDD 140
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75570321 164 KEcrKVKLSDFGMT---RRAGSPVKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd05608 141 DG--NVRISDLGLAvelKDGQTKTKGYAGTPGFMAPELLLGEEY-----DYSVDYFTLGVTLYEMIAARGPF 205
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
81-234 3.66e-14

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: 72.22  E-value: 3.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  81 LYLSPCPFIINMFGiAFETDEYYVFAQEYAPSGDLfDIIPPqvgLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENIL 160
Cdd:cd06619  53 LYKCDSPYIIGFYG-AFFVENRISICTEFMDGGSL-DVYRK---IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNML 127
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 161 IFDKEcrKVKLSDFGMTRR-AGSPVKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWEK 234
Cdd:cd06619 128 VNTRG--QVKLCDFGVSTQlVNSIAKTYVGTNAYMAPERISGEQY-----GIHSDVWSLGISFMELALGRFPYPQ 195
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
125-231 3.72e-14

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: 72.40  E-value: 3.72e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 125 LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTRRAGSPVKRVSG---TIPYTAPEL--- 198
Cdd:cd07845 105 FSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGC--LKIADFGLARTYGLPAKPMTPkvvTLWYRAPELllg 182
                        90       100       110
                ....*....|....*....|....*....|....*
gi 75570321 199 CDTSkhdgfcvDYSTDVWAFGVLLFCMLTGN--FP 231
Cdd:cd07845 183 CTTY-------TTAIDMWAVGCILAELLAHKplLP 210
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
89-232 3.93e-14

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 72.52  E-value: 3.93e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFE-TDEYYVFAQEYAPSGDLFDII--PPQV-GLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENIL-IFD 163
Cdd:cd13988  53 IVKLFAIEEElTTRHKVLVMELCPCGSLYTVLeePSNAyGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrVIG 132
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 164 KECRKV-KLSDFGMTRRAGSPVKRVS--GTIPYTAPELCDTS---KHDGFCVDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd13988 133 EDGQSVyKLTDFGAARELEDDEQFVSlyGTEEYLHPDMYERAvlrKDHQKKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
124-230 5.20e-14

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 72.22  E-value: 5.20e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 124 GLPEPVAKRCVHQVAIALEYLHSK-KLVHRDIKPENILIFDKECRkVKLSDFGmtrRAGSPVKRVSGTI---PYTAPELC 199
Cdd:cd14136 115 GIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCISKIE-VKIADLG---NACWTDKHFTEDIqtrQYRSPEVI 190
                        90       100       110
                ....*....|....*....|....*....|.
gi 75570321 200 DTSKHdgfcvDYSTDVWAFGVLLFCMLTGNF 230
Cdd:cd14136 191 LGAGY-----GTPADIWSTACMAFELATGDY 216
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
87-231 5.24e-14

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: 71.53  E-value: 5.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETdeyYVFAQEYAPSGDLFDIIPPQ------VGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENIL 160
Cdd:cd14067  70 PCIVYLIGISIHP---LCFALELAPLGSLNTVLEENhkgssfMPLGHMLTFKIAYQIAAGLAYLHKKNIIFCDLKSDNIL 146
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 161 IFDKECRK---VKLSDFGMTRRA-GSPVKRVSGTIPYTAPELcdtskHDGFCVDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:cd14067 147 VWSLDVQEhinIKLSDYGISRQSfHEGALGVEGTPGYQAPEI-----RPRIVYDEKVDMFSYGMVLYELLSGQRP 216
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
87-233 6.08e-14

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: 71.21  E-value: 6.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFEtDEYYVFAQEYAPSGDLFDI-----IPPQVGLPEPVakrcvhQVAIALEYLHSKKLV---HRDIKPEN 158
Cdd:cd14147  62 PNIIALKAVCLE-EPNLCLVMEYAAGGPLSRAlagrrVPPHVLVNWAV------QIARGMHYLHCEALVpviHRDLKSNN 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 159 ILIF------DKECRKVKLSDFGMTRRAGSPVK-RVSGTIPYTAPELCDTSKHDGFcvdysTDVWAFGVLLFCMLTGNFP 231
Cdd:cd14147 135 ILLLqpiendDMEHKTLKITDFGLAREWHKTTQmSAAGTYAWMAPEVIKASTFSKG-----SDVWSFGVLLWELLTGEVP 209

                ..
gi 75570321 232 WE 233
Cdd:cd14147 210 YR 211
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
32-229 6.52e-14

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: 71.83  E-value: 6.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMAL---------KFLKKKSTKLKSFLREYSISlYLSPCpfiINMFGiAFETDEY 102
Cdd:cd14134  14 YKILRLLGEGTFGKVLECWDRKRKRYVAVkiirnvekyREAAKIEIDVLETLAEKDPN-GKSHC---VQLRD-WFDYRGH 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 103 YVFAQE-YAPSgdLFDIIPPQVGLPEPVAKrCVH---QVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTR 178
Cdd:cd14134  89 MCIVFElLGPS--LYDFLKKNNYGPFPLEH-VQHiakQLLEAVAFLHDLKLTHTDLKPENILLVDSDYVKVYNPKKKRQI 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 179 RagsPVKR---------------------VSgTIPYTAPElcdtskhdgfcV------DYSTDVWAFGVLLFCMLTGN 229
Cdd:cd14134 166 R---VPKStdiklidfgsatfddeyhssiVS-TRHYRAPE-----------VilglgwSYPCDVWSIGCILVELYTGE 228
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
87-293 6.99e-14

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: 70.73  E-value: 6.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVfAQEYAPSGDLFDIIP---PQVGLPEPVakRCVHQVAIALEYLHSKKLVHRDIKPENILIFD 163
Cdd:cd05084  54 PNIVRLIGVCTQKQPIYI-VMELVQGGDFLTFLRtegPRLKVKELI--RMVENAAAGMEYLESKHCIHRDLAARNCLVTE 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 164 KECrkVKLSDFGMTRRAGSPVKRVSG---TIP--YTAPELCDTSKhdgfcvdYST--DVWAFGVLLFCMLT-GNFPWekA 235
Cdd:cd05084 131 KNV--LKISDFGMSREEEDGVYAATGgmkQIPvkWTAPEALNYGR-------YSSesDVWSFGILLWETFSlGAVPY--A 199
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 236 MPSDTFYEEFVRWQKRRtgAVPSQWrrfTDESLRMFRKLLALEQERRCSVKEVFAHLG 293
Cdd:cd05084 200 NLSNQQTREAVEQGVRL--PCPENC---PDEVYRLMEQCWEYDPRKRPSFSTVHQDLQ 252
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
89-242 9.88e-14

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: 70.61  E-value: 9.88e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFEtDEYYVFAQEYAPSGDLFDIIPpQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRk 168
Cdd:cd14027  53 VVKLLGVILE-EGKYSLVMEYMEKGNLMHVLK-KVSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILV-DNDFH- 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 169 VKLSDFGMT----------------RRAGSPVKRVSGTIPYTAPE-LCDTSKHDgfcvDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:cd14027 129 IKIADLGLAsfkmwskltkeehneqREVDGTAKKNAGTLYYMAPEhLNDVNAKP----TEKSDVYSFAIVLWAIFANKEP 204
                       170
                ....*....|.
gi 75570321 232 WEKAMPSDTFY 242
Cdd:cd14027 205 YENAINEDQII 215
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
87-232 1.04e-13

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: 70.46  E-value: 1.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFEtDEYYVFAQEYAPSGDLFDI-----IPPQVGLPEPVakrcvhQVAIALEYLHSKKLV---HRDIKPEN 158
Cdd:cd14145  65 PNIIALRGVCLK-EPNLCLVMEFARGGPLNRVlsgkrIPPDILVNWAV------QIARGMNYLHCEAIVpviHRDLKSSN 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 159 ILIF------DKECRKVKLSDFGMTRRAGSPVK-RVSGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:cd14145 138 ILILekvengDLSNKILKITDFGLAREWHRTTKmSAAGTYAWMAPEVIRSSM-----FSKGSDVWSYGVLLWELLTGEVP 212

                .
gi 75570321 232 W 232
Cdd:cd14145 213 F 213
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
93-241 1.07e-13

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


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 70.34  E-value: 1.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  93 FGIAFE-TDEYYVFAqEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKL 171
Cdd:cd14189  66 FSHHFEdAENIYIFL-ELCSRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFI--NENMELKV 142
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75570321 172 SDFGMTRRAGSPVKR---VSGTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWEKAMPSDTF 241
Cdd:cd14189 143 GDFGLAARLEPPEQRkktICGTPNYLAPEVLLRQGHGP-----ESDVWSLGCVMYTLLCGNPPFETLDLKETY 210
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
137-282 1.08e-13

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: 70.60  E-value: 1.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 137 VAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRragsPVKRVSGTIPYT----APELCdTSKHDGfcvdyS 212
Cdd:cd13975 111 VVEGIRFLHSQGLVHRDIKLKNVLL-DKKNR-AKITDLGFCK----PEAMMSGSIVGTpihmAPELF-SGKYDN-----S 178
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75570321 213 TDVWAFGVLLFCMLTGNFPWEKAmpsdtfYEEFVR----WQKRRTGAVPSQWRRFTDESLRMFRKLLALEQERR 282
Cdd:cd13975 179 VDVYAFGILFWYLCAGHVKLPEA------FEQCASkdhlWNNVRKGVRPERLPVFDEECWNLMEACWSGDPSQR 246
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
32-228 1.09e-13

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: 71.40  E-value: 1.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMA---LKFLKKKSTKLKSFLREYSISLYLSpCPFIINMFGI--AFETDEY---Y 103
Cdd:cd07834   2 YELLKPIGSGAYGVVCSAYDKRTGRKVAikkISNVFDDLIDAKRILREIKILRHLK-HENIIGLLDIlrPPSPEEFndvY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 104 VfAQEYAPSgDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECrKVKLSDFGMTRRAGSP 183
Cdd:cd07834  81 I-VTELMET-DLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILV-NSNC-DLKICDFGLARGVDPD 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75570321 184 ----------VKRVsgtipYTAPELCDTSKHdgfcvdYST--DVWAFGVLLFCMLTG 228
Cdd:cd07834 157 edkgflteyvVTRW-----YRAPELLLSSKK------YTKaiDIWSVGCIFAELLTR 202
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
30-296 1.17e-13

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 71.33  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   30 KYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFlkkkstklksfLREYSISLYLSPCPFIINMFGIAFET---------- 99
Cdd:PTZ00024   9 RYIQKGAHLGEGTYGKVEKAYDTLTGKIVAIKK-----------VKIIEISNDVTKDRQLVGMCGIHFTTlrelkimnei 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  100 --------------DEYYVFAQEYApSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKE 165
Cdd:PTZ00024  78 khenimglvdvyveGDFINLVMDIM-ASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  166 crKVKLSDFGMTRRAGSPV-------------------KRVsgTIPYTAPELCDTSKhdgfCVDYSTDVWAFGVLLFCML 226
Cdd:PTZ00024 157 --ICKIADFGLARRYGYPPysdtlskdetmqrreemtsKVV--TLWYRAPELLMGAE----KYHFAVDMWSVGCIFAELL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  227 TGN--FPWEKAM------------PSDTFYEE------FVRWQKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVK 286
Cdd:PTZ00024 229 TGKplFPGENEIdqlgrifellgtPNEDNWPQakklplYTEFTPRKPKDLKTIFPNASDDAIDLLQSLLKLNPLERISAK 308
                        330
                 ....*....|
gi 75570321  287 EVfahLGHRW 296
Cdd:PTZ00024 309 EA---LKHEY 315
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
125-293 1.21e-13

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: 70.51  E-value: 1.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 125 LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENIlIFDKECRKVKLSDFGMTRRAGSP---VKRVSGTIPYTAPELCDT 201
Cdd:cd13974 129 LSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNM-VLNKRTRKITITNFCLGKHLVSEddlLKDQRGSPAYISPDVLSG 207
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 202 SKHDGfcvdYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFyeefvRWQKRRTGAVPSQwRRFTDESLRMFRKLLALEQER 281
Cdd:cd13974 208 KPYLG----KPSDMWALGVVLFTMLYGQFPFYDSIPQELF-----RKIKAAEYTIPED-GRVSENTVCLIRKLLVLNPQK 277
                       170
                ....*....|..
gi 75570321 282 RCSVKEVFAHLG 293
Cdd:cd13974 278 RLTASEVLDSLE 289
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
108-233 1.31e-13

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: 70.11  E-value: 1.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIppqVGLPEPV-AKRCVH---QVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRR---- 179
Cdd:cd13979  82 EYCGNGTLQQLI---YEGSEPLpLAHRILislDIARALRFCHSHGIVHLDVKPANILISEQG--VCKLCDFGCSVKlgeg 156
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 180 --AGSPVKRVSGTIPYTAPELCdtskhDGFCVDYSTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd13979 157 neVGTPRSHIGGTYTYRAPELL-----KGERVTPKADIYSFGITLWQMLTRELPYA 207
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
124-232 1.34e-13

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: 70.48  E-value: 1.34e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 124 GLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAGSPVKRVS---GTIPYTAPELC- 199
Cdd:cd07847  96 GVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILI-TKQGQ-IKLCDFGFARILTGPGDDYTdyvATRWYRAPELLv 173
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 75570321 200 -DTSkhdgfcvdYST--DVWAFGVLLFCMLTGNFPW 232
Cdd:cd07847 174 gDTQ--------YGPpvDVWAIGCVFAELLTGQPLW 201
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
38-232 1.37e-13

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: 70.23  E-value: 1.37e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVdlviHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIAFEtDEYYVFAQEYAPSGDLFD 117
Cdd:cd13991  14 IGRGSFGEV----HRMEDKQTGFQCAVKKVRLEVFRAEELMACAGLTS-PRVVPLYGAVRE-GPWVNIFMDLKEGGSLGQ 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 118 IIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDkECRKVKLSDFGMTRRA-----GSPVKR---VSG 189
Cdd:cd13991  88 LIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSS-DGSDAFLCDFGHAECLdpdglGKSLFTgdyIPG 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 75570321 190 TIPYTAPELCdtskhDGFCVDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd13991 167 TETHMAPEVV-----LGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
87-232 1.49e-13

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: 70.14  E-value: 1.49e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVFaQEYAPSGDLFDII---------PPQVGLPEPVAKrCVHqVAIALEYLHSKKLVHRDIKPE 157
Cdd:cd05044  59 PNILKLLGVCLDNDPQYII-LELMEGGDLLSYLraarptaftPPLLTLKDLLSI-CVD-VAKGCVYLEDMHFVHRDLAAR 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 158 NILIFDKECRK--VKLSDFGMTR---RAGSPVKRVSGTIP--YTAPElcdtSKHDGFCVDYStDVWAFGVLLFCMLT-GN 229
Cdd:cd05044 136 NCLVSSKDYRErvVKIGDFGLARdiyKNDYYRKEGEGLLPvrWMAPE----SLVDGVFTTQS-DVWAFGVLMWEILTlGQ 210

                ...
gi 75570321 230 FPW 232
Cdd:cd05044 211 QPY 213
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
96-244 1.64e-13

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: 70.84  E-value: 1.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  96 AFETDEYYVFAQEYAPSGDLFDIIPP-QVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKeCRKVKLSDF 174
Cdd:cd05597  69 AFQDENYLYLVMDYYCGGDLLTLLSKfEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLL-DR-NGHIRLADF 146
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 175 G---MTRRAGSPVKRVS-GTIPYTAPELCDTSKhDGFCVdYST--DVWAFGVLLFCMLTGNFPwekampsdtFYEE 244
Cdd:cd05597 147 GsclKLREDGTVQSSVAvGTPDYISPEILQAME-DGKGR-YGPecDWWSLGVCMYEMLYGETP---------FYAE 211
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
32-291 1.74e-13

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: 70.38  E-value: 1.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDL-------------VIHKI--------------RGSKMALKFLKKKSTKLKSFLREYSISLYLS 84
Cdd:cd14199   4 YKLKDEIGKGSYGVVKLayneddntyyamkVLSKKklmrqagfprrpppRGARAAPEGCTQPRGPIERVYQEIAILKKLD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  85 PcPFIINMFGIAFETDE---YYVFaqEYAPSGDLFDIiPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI 161
Cdd:cd14199  84 H-PNVVKLVEVLDDPSEdhlYMVF--ELVKQGPVMEV-PTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 162 fdKECRKVKLSDFGMTRR---AGSPVKRVSGTIPYTAPE-LCDTSKHdgFCVDySTDVWAFGVLLFCMLTGNFPW--EKA 235
Cdd:cd14199 160 --GEDGHIKIADFGVSNEfegSDALLTNTVGTPAFMAPEtLSETRKI--FSGK-ALDVWAMGVTLYCFVFGQCPFmdERI 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 236 MpsdTFYEEFvrwqKRRTGAVPSQwRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14199 235 L---SLHSKI----KTQPLEFPDQ-PDISDDLKDLLFRMLDKNPESRISVPEIKLH 282
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
124-231 1.92e-13

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: 69.60  E-value: 1.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 124 GLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFG----MTRRAGSPVKRVSgtipYTAPELC 199
Cdd:cd14133  98 YLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQIKIIDFGsscfLTQRLYSYIQSRY----YRAPEVI 173
                        90       100       110
                ....*....|....*....|....*....|....
gi 75570321 200 DTSKHDGfcvdySTDVWAFGVLLFCMLTGN--FP 231
Cdd:cd14133 174 LGLPYDE-----KIDMWSLGCILAELYTGEplFP 202
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
32-179 2.15e-13

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: 69.41  E-value: 2.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSfLREYSISLYLSPCPFI--INMFGiafETDEYYVFAQEY 109
Cdd:cd14016   2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHPQL-EYEAKVYKLLQGGPGIprLYWFG---QEGDYNVMVMDL 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75570321 110 -APS-GDLFDIIPPQVGLpepvakRCVHQVAI----ALEYLHSKKLVHRDIKPENILI-FDKECRKVKLSDFGMTRR 179
Cdd:cd14016  78 lGPSlEDLFNKCGRKFSL------KTVLMLADqmisRLEYLHSKGYIHRDIKPENFLMgLGKNSNKVYLIDFGLAKK 148
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
38-232 2.19e-13

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: 70.03  E-value: 2.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISL----YLSPCPFIINMFGiAFETDEYYVFAQEYAPSG 113
Cdd:cd05089  10 IGEGNFGQVIKAMIKKDGLKMNAAIKMLKEFASENDHRDFAGELevlcKLGHHPNIINLLG-ACENRGYLYIAIEYAPYG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDII-PPQVGLPEPV-AK--------------RCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVklSDFGMT 177
Cdd:cd05089  89 NLLDFLrKSRVLETDPAfAKehgtastltsqqllQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKI--ADFGLS 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 178 RRAGSPVKRVSGTIP--YTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLT-GNFPW 232
Cdd:cd05089 167 RGEEVYVKKTMGRLPvrWMAIESLNYSVYTT-----KSDVWSFGVLLWEIVSlGGTPY 219
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
30-234 2.21e-13

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: 69.81  E-value: 2.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  30 KYYEVIrelGKGTYGKVDLVIHKIRGSKMALKFLK--KKSTKLKSFLREYSI--SLYLSPCPFIINMFGIAFETDEYYVf 105
Cdd:cd06917   4 RRLELV---GRGSYGAVYRGYHVKTGRVVALKVLNldTDDDDVSDIQKEVALlsQLKLGQPKNIIKYYGSYLKGPSLWI- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 106 AQEYAPSGDLFDIIPPQvglpePVAKRC----VHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRR-A 180
Cdd:cd06917  80 IMDYCEGGSIRTLMRAG-----PIAERYiaviMREVLVALKFIHKDGIIHRDIKAANILV--TNTGNVKLCDFGVAASlN 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 181 GSPVKRVS--GTIPYTAPELCdtskHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEK 234
Cdd:cd06917 153 QNSSKRSTfvGTPYWMAPEVI----TEGKYYDTKADIWSLGITTYEMATGNPPYSD 204
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
38-231 2.66e-13

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: 69.36  E-value: 2.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKV----DLVIHKirgsKMALKFLKKKSTKLKSFLREySISLYLSPC-PFIINMFGIAFETDEYYVFaQEYAPS 112
Cdd:cd06624  16 LGKGTFGVVyaarDLSTQV----RIAIKEIPERDSREVQPLHE-EIALHSRLShKNIVQYLGSVSEDGFFKIF-MEQVPG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 113 GDLFDIIPPQVGlP----EPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRKVKLSDFGMTRR-AG-SPV-K 185
Cdd:cd06624  90 GSLSALLRSKWG-PlkdnENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLV-NTYSGVVKISDFGTSKRlAGiNPCtE 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75570321 186 RVSGTIPYTAPELCDTSKHdGFcvDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:cd06624 168 TFTGTLQYMAPEVIDKGQR-GY--GPPADIWSLGCTIIEMATGKPP 210
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
108-251 2.87e-13

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: 69.45  E-value: 2.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDII----PPQVGLPEPVAKRCVHQVAIALEYLH---SKKLVHRDIKPENILIfDKECRKVkLSDFGMTR-- 178
Cdd:cd14664  70 EYMPNGSLGELLhsrpESQPPLDWETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILL-DEEFEAH-VADFGLAKlm 147
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 179 --RAGSPVKRVSGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFyeEFVRWQKR 251
Cdd:cd14664 148 ddKDSHVMSSVAGSYGYIAPEYAYTGK-----VSEKSDVYSYGVVLLELITGKRPFDEAFLDDGV--DIVDWVRG 215
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
136-288 3.02e-13

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: 69.61  E-value: 3.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR---RAGSPVKRVSGTIP--YTAPE-LCD---TSKhdg 206
Cdd:cd05045 135 QISRGMQYLAEMKLVHRDLAARNVLV--AEGRKMKISDFGLSRdvyEEDSYVKRSKGRIPvkWMAIEsLFDhiyTTQ--- 209
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 207 fcvdysTDVWAFGVLLFCMLT-GNFPWEKAMPSDTfyeefvrWQKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSV 285
Cdd:cd05045 210 ------SDVWSFGVLLWEIVTlGGNPYPGIAPERL-------FNLLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTF 276

                ...
gi 75570321 286 KEV 288
Cdd:cd05045 277 ADI 279
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
10-291 3.12e-13

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: 69.75  E-value: 3.12e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  10 DILEELQLYTAQNLEKlevnKYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFI 89
Cdd:cd06654   4 EILEKLRSIVSVGDPK----KKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  90 INMFGIAFETDEYYVfAQEYAPSGDLFDIIPPQV---GLPEPVAKRCVHqvaiALEYLHSKKLVHRDIKPENILI-FDKE 165
Cdd:cd06654  80 VNYLDSYLVGDELWV-VMEYLAGGSLTDVVTETCmdeGQIAAVCRECLQ----ALEFLHSNQVIHRDIKSDNILLgMDGS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 166 crkVKLSDFGMTRRAGSPVKRVS---GTIPYTAPELCdTSKHDGFCVdystDVWAFGVLLFCMLTGNFPWEKAMPSDTFY 242
Cdd:cd06654 155 ---VKLTDFGFCAQITPEQSKRStmvGTPYWMAPEVV-TRKAYGPKV----DIWSLGIMAIEMIEGEPPYLNENPLRALY 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 243 -------EEFVRWQKrrtgaVPSQWRRFTDESLRMfrkllalEQERRCSVKEVFAH 291
Cdd:cd06654 227 liatngtPELQNPEK-----LSAIFRDFLNRCLEM-------DVEKRGSAKELLQH 270
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
38-282 3.17e-13

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: 69.91  E-value: 3.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLV----IHKIRGSKMALKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMfGIAFETDEYYVFAQEYAPSG 113
Cdd:cd05585   2 IGKGSFGKVMQVrkkdTSRIYALKTIRKAHIVSRSEVTHTLAERTV-LAQVDCPFIVPL-KFSFQSPEKLYLVLAFINGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAGSPVKRVS---GT 190
Cdd:cd05585  80 ELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILL--DYTGHIALCDFGLCKLNMKDDDKTNtfcGT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 191 IPYTAPELCDTSKHDGfCVDYstdvWAFGVLLFCMLTGNFPwekampsdtFYEEFVRWQKRRTGAVPSQWRRFTDESLR- 269
Cdd:cd05585 158 PEYLAPELLLGHGYTK-AVDW----WTLGVLLYEMLTGLPP---------FYDENTNEMYRKILQEPLRFPDGFDRDAKd 223
                       250
                ....*....|...
gi 75570321 270 MFRKLLALEQERR 282
Cdd:cd05585 224 LLIGLLNRDPTKR 236
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
74-235 3.43e-13

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: 69.18  E-value: 3.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  74 LREYSIsLYLSPCPFIINMFGIAFETdEYYVFAQEYAPSGDLFDIIPPQVGLPE---PVAKRCVHQVAIALEYLH--SKK 148
Cdd:cd14026  45 LKEAEI-LHKARFSYILPILGICNEP-EFLGIVTEYMTNGSLNELLHEKDIYPDvawPLRLRILYEIALGVNYLHnmSPP 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 149 LVHRDIKPENILIfDKECRkVKLSDFGM--------TRRAGSPVKRVSGTIPYTAPELCDTSKHDGFCVDYstDVWAFGV 220
Cdd:cd14026 123 LLHHDLKTQNILL-DGEFH-VKIADFGLskwrqlsiSQSRSSKSAPEGGTIIYMPPEEYEPSQKRRASVKH--DIYSYAI 198
                       170
                ....*....|....*
gi 75570321 221 LLFCMLTGNFPWEKA 235
Cdd:cd14026 199 IMWEVLSRKIPFEEV 213
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
89-232 3.49e-13

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: 69.61  E-value: 3.49e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFETDEYYVFAqEYAPSGDLFDII----PP--------------QVGLPEPVAkrCVHQVAIALEYLHSKKLV 150
Cdd:cd05099  80 IINLLGVCTQEGPLYVIV-EYAAKGNLREFLrarrPPgpdytfditkvpeeQLSFKDLVS--CAYQVARGMEYLESRRCI 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 151 HRDIKPENILIFDKECrkVKLSDFGMTRRAGSP---VKRVSGTIP--YTAPE-LCDTskhdgfCVDYSTDVWAFGVLLFC 224
Cdd:cd05099 157 HRDLAARNVLVTEDNV--MKIADFGLARGVHDIdyyKKTSNGRLPvkWMAPEaLFDR------VYTHQSDVWSFGILMWE 228

                ....*....
gi 75570321 225 MLT-GNFPW 232
Cdd:cd05099 229 IFTlGGSPY 237
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
114-291 4.69e-13

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: 68.79  E-value: 4.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPPQVGLPEpvAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTRRAGSPVKRVSG---T 190
Cdd:cd07843  94 SLMETMKQPFLQSE--VKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGI--LKICDFGLAREYGSPLKPYTQlvvT 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 191 IPYTAPELCDTSKHdgfcvdYST--DVWAFGVLLFCMLTGN--FPWEKAM------------PSDTFYEEFVR---WQKR 251
Cdd:cd07843 170 LWYRAPELLLGAKE------YSTaiDMWSVGCIFAELLTKKplFPGKSEIdqlnkifkllgtPTEKIWPGFSElpgAKKK 243
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75570321 252 -RTGAVPSQWR-RF-----TDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07843 244 tFTKYPYNQLRkKFpalslSDNGFDLLNRLLTYDPAKRISAEDALKH 290
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
32-288 5.14e-13

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: 68.55  E-value: 5.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALK--FLKKKSTKLKSFLREYSIslyLSPC--PFIINMFGIAFETDEYYVfAQ 107
Cdd:cd14046   8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKkiKLRSESKNNSRILREVML---LSRLnhQHVVRYYQAWIERANLYI-QM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIppQVGLPEPVAK--RCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAGSPVK 185
Cdd:cd14046  84 EYCEKSTLRDLI--DSGLFQDTDRlwRLFRQILEGLAYIHSQGIIHRDLKPVNIFL--DSNGNVKIGDFGLATSNKLNVE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 186 RVS---------------------GTIPYTAPELCD--TSKHDGfcvdySTDVWAFGVLLFcmltgnfpwEKAMPSDTFY 242
Cdd:cd14046 160 LATqdinkstsaalgssgdltgnvGTALYVAPEVQSgtKSTYNE-----KVDMYSLGIIFF---------EMCYPFSTGM 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 75570321 243 EEFVRWQKRR--TGAVPSQWRR-FTDESLRMFRKLLALEQERRCSVKEV 288
Cdd:cd14046 226 ERVQILTALRsvSIEFPPDFDDnKHSKQAKLIRWLLNHDPAKRPSAQEL 274
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
117-291 5.36e-13

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: 68.66  E-value: 5.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 117 DIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRAGSPVKRVSG---TIPY 193
Cdd:cd07836  89 DTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRG--ELKLADFGLARAFGIPVNTFSNevvTLWY 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 194 TAPELCDTSKhdgfcvDYST--DVWAFGVLLFCMLTG--------------------NFPWEKAMPSDTFYEEFVR-WQK 250
Cdd:cd07836 167 RAPDVLLGSR------TYSTsiDIWSVGCIMAEMITGrplfpgtnnedqllkifrimGTPTESTWPGISQLPEYKPtFPR 240
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 75570321 251 RRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07836 241 YPPQDLQQLFPHADPLGIDLLHRLLQLNPELRISAHDALQH 281
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
136-232 5.41e-13

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 68.90  E-value: 5.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENilIFDKECRKVKLSDFGM----TRRAGS-PVKRVSGTIPYTAPELCDTSKHDGFcvD 210
Cdd:cd14149 116 QTAQGMDYLHAKNIIHRDMKSNN--IFLHEGLTVKIGDFGLatvkSRWSGSqQVEQPTGSILWMAPEVIRMQDNNPF--S 191
                        90       100
                ....*....|....*....|..
gi 75570321 211 YSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd14149 192 FQSDVYSYGIVLYELMTGELPY 213
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
108-228 6.17e-13

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: 68.68  E-value: 6.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVG-LPEPVAKRC--VHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAGSPV 184
Cdd:cd14158  94 TYMPNGSLLDRLACLNDtPPLSWHMRCkiAQGTANGINYLHENNHIHRDIKSANILL--DETFVPKISDFGLARASEKFS 171
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 75570321 185 K-----RVSGTIPYTAPElcdTSKHDgfcVDYSTDVWAFGVLLFCMLTG 228
Cdd:cd14158 172 QtimteRIVGTTAYMAPE---ALRGE---ITPKSDIFSFGVVLLEIITG 214
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
32-231 6.59e-13

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: 68.92  E-value: 6.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKF--LKKKSTKLKSFLREYSIsLYLSPCPFIINMFGiAFETDEYYVFAQEY 109
Cdd:cd06649   7 FERISELGAGNGGVVTKVQHKPSGLIMARKLihLEIKPAIRNQIIRELQV-LHECNSPYIVGFYG-AFYSDGEISICMEH 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 110 APSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSK-KLVHRDIKPENILIFDKEcrKVKLSDFGMT-RRAGSPVKRV 187
Cdd:cd06649  85 MDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRG--EIKLCDFGVSgQLIDSMANSF 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 75570321 188 SGTIPYTAPElcdtsKHDGFCVDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:cd06649 163 VGTRSYMSPE-----RLQGTHYSVQSDIWSMGLSLVELAIGRYP 201
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
105-244 6.89e-13

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: 68.41  E-value: 6.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 105 FAQEYAPSGDLFDII-PPQ--VGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKV-KLSDFGMTR-- 178
Cdd:cd14039  73 LAMEYCSGGDLRKLLnKPEncCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVhKIIDLGYAKdl 152
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 179 RAGSPVKRVSGTIPYTAPELCDtSKHDGFCVDYstdvWAFGVLLFCMLTGNFPWEKAMPSDTFYEE 244
Cdd:cd14039 153 DQGSLCTSFVGTLQYLAPELFE-NKSYTVTVDY----WSFGTMVFECIAGFRPFLHNLQPFTWHEK 213
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
10-291 7.03e-13

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: 68.59  E-value: 7.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  10 DILEELQLYTAQNLEKlevnKYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFI 89
Cdd:cd06656   3 EILEKLRSIVSVGDPK----KKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  90 INMFGIAFETDEYYVfAQEYAPSGDLFDIIPPQV---GLPEPVAKRCVHqvaiALEYLHSKKLVHRDIKPENILI-FDKE 165
Cdd:cd06656  79 VNYLDSYLVGDELWV-VMEYLAGGSLTDVVTETCmdeGQIAAVCRECLQ----ALDFLHSNQVIHRDIKSDNILLgMDGS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 166 crkVKLSDFGMTRRAGSPVKRVS---GTIPYTAPELCdTSKHDGFCVdystDVWAFGVLLFCMLTGNFPWEKAMPSDTFY 242
Cdd:cd06656 154 ---VKLTDFGFCAQITPEQSKRStmvGTPYWMAPEVV-TRKAYGPKV----DIWSLGIMAIEMVEGEPPYLNENPLRALY 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 75570321 243 eefvrwqKRRTGAVP--SQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd06656 226 -------LIATNGTPelQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQH 269
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
88-287 7.10e-13

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


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 68.84  E-value: 7.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  88 FIINMfGIAFETDEYYVFAQEYAPSGDL-FDIIppQVGLPEPVAKRCVH---QVAIALEYLHSKKLVHRDIKPENILIFD 163
Cdd:cd05632  63 FVVNL-AYAYETKDALCLVLTIMNGGDLkFHIY--NMGNPGFEEERALFyaaEILCGLEDLHRENTVYRDLKPENILLDD 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 164 KEcrKVKLSDFGMTRR--AGSPVKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWeKAMPSDTF 241
Cdd:cd05632 140 YG--HIRISDLGLAVKipEGESIRGRVGTVGYMAPEVLNNQRY-----TLSPDYWGLGCLIYEMIEGQSPF-RGRKEKVK 211
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75570321 242 YEEFvrwQKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKE 287
Cdd:cd05632 212 REEV---DRRVLETEEVYSAKFSEEAKSICKMLLTKDPKQRLGCQE 254
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
33-239 8.07e-13

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: 68.14  E-value: 8.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  33 EVIRELGKGTYGKVDLVIHKiRGSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIAFETDEYYVFAqEYAPS 112
Cdd:cd05072  10 KLVKKLGAGQFGEVWMGYYN-NSTKVAVKTLKPGTMSVQAFLEEANLMKTLQH-DKLVRLYAVVTKEEPIYIIT-EYMAK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 113 GDLFDIIPPQVG----LPEPVAKRCvhQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR---------R 179
Cdd:cd05072  87 GSLLDFLKSDEGgkvlLPKLIDFSA--QIAEGMAYIERKNYIHRDLRAANVLV--SESLMCKIADFGLARviedneytaR 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75570321 180 AGS--PVKrvsgtipYTAPELCDTSkhdgfCVDYSTDVWAFGVLLFCMLT-GNFPWEKAMPSD 239
Cdd:cd05072 163 EGAkfPIK-------WTAPEAINFG-----SFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSD 213
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
32-250 9.53e-13

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: 68.91  E-value: 9.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSF---LREYSISLYLSPCPFIINMFgIAFETDEYYVFAQE 108
Cdd:cd05628   3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQvghIRAERDILVEADSLWVVKMF-YSFQDKLNLYLIME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGM------------ 176
Cdd:cd05628  82 FLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKG--HVKLSDFGLctglkkahrtef 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 177 ------------------TRRAGSPVKR--------VSGTIPYTAPELCDTSKHDGFCvdystDVWAFGVLLFCMLTGNF 230
Cdd:cd05628 160 yrnlnhslpsdftfqnmnSKRKAETWKRnrrqlafsTVGTPDYIAPEVFMQTGYNKLC-----DWWSLGVIMYEMLIGYP 234
                       250       260
                ....*....|....*....|
gi 75570321 231 PWEKAMPSDTfYEEFVRWQK 250
Cdd:cd05628 235 PFCSETPQET-YKKVMNWKE 253
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
136-232 1.04e-12

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: 67.78  E-value: 1.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENilIFDKECRKVKLSDFGM----TRRAGS-PVKRVSGTIPYTAPELCDTSKHDGFcvD 210
Cdd:cd14151 112 QTAQGMDYLHAKSIIHRDLKSNN--IFLHEDLTVKIGDFGLatvkSRWSGShQFEQLSGSILWMAPEVIRMQDKNPY--S 187
                        90       100
                ....*....|....*....|..
gi 75570321 211 YSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd14151 188 FQSDVYAFGIVLYELMTGQLPY 209
pknD PRK13184
serine/threonine-protein kinase PknD;
32-234 1.05e-12

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 69.80  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKF----LKKKSTKLKSFLREYSISLYLSPcPFIINMFGIAFETDE-YYV-- 104
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKiredLSENPLLKKRFLREAKIAADLIH-PGIVPVYSICSDGDPvYYTmp 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  105 FAQEYAPSgDLFDIIPPQVGLPEPVAK--------RCVHQVAIALEYLHSKKLVHRDIKPENIL--------IFD----- 163
Cdd:PRK13184  83 YIEGYTLK-SLLKSVWQKESLSKELAEktsvgaflSIFHKICATIEYVHSKGVLHRDLKPDNILlglfgevvILDwgaai 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75570321  164 -KECRKVKL--SDFGMTRRAGSPVK---RVSGTIPYTAPElcdtsKHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEK 234
Cdd:PRK13184 162 fKKLEEEDLldIDVDERNICYSSMTipgKIVGTPDYMAPE-----RLLGVPASESTDIYALGVILYQMLTLSFPYRR 233
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
87-242 1.10e-12

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; 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. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 67.93  E-value: 1.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEY---YVfaqeYAPSGDLFDIIPPQVGLPEPVAKRCVH---QVAIALEYLH--SKKLVHRDIKPEN 158
Cdd:cd14159  52 PNIVDLAGYSAQQGNYcliYV----YLPNGSLEDRLHCQVSCPCLSWSQRLHvllGTARAIQYLHsdSPSLIHGDVKSSN 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 159 ILIfdKECRKVKLSDFGM---TRRAGSPVKR--------VSGTIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLT 227
Cdd:cd14159 128 ILL--DAALNPKLGDFGLarfSRRPKQPGMSstlartqtVRGTLAYLPEEYVKTGT-----LSVEIDVYSFGVVLLELLT 200
                       170
                ....*....|....*
gi 75570321 228 GNFPWEKAMPSDTFY 242
Cdd:cd14159 201 GRRAMEVDSCSPTKY 215
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
136-241 1.16e-12

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 67.34  E-value: 1.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENILIFDKecrKVKLSDFGMTRRAGSPV---KRVSGTIPYTAPELCDTSKHDGfcvdyS 212
Cdd:cd13995 104 HVLKGLDFLHSKNIIHHDIKPSNIVFMST---KAVLVDFGLSVQMTEDVyvpKDLRGTEIYMSPEVILCRGHNT-----K 175
                        90       100
                ....*....|....*....|....*....
gi 75570321 213 TDVWAFGVLLFCMLTGNFPWEKAMPSDTF 241
Cdd:cd13995 176 ADIYSLGATIIHMQTGSPPWVRRYPRSAY 204
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
93-233 1.17e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 68.89  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   93 FGIA-----FETDEYYVFAQEYAPSGDLFDIIPPQVG--LP--EPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFD 163
Cdd:PTZ00267 125 FGIVkhfddFKSDDKLLLIMEYGSGGDLNKQIKQRLKehLPfqEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMP 204
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75570321  164 KECrkVKLSDFGMTRRAGSPV-----KRVSGTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWE 233
Cdd:PTZ00267 205 TGI--IKLGDFGFSKQYSDSVsldvaSSFCGTPYYLAPELWERKRYSK-----KADMWSLGVILYELLTLHRPFK 272
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
32-250 1.20e-12

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: 68.55  E-value: 1.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALK---FLKKKSTKLKSFLREYSISLYLSPCPFIINMFgIAFETDEYYVFAQE 108
Cdd:cd05627   4 FESLKVIGRGAFGEVRLVQKKDTGHIYAMKilrKADMLEKEQVAHIRAERDILVEADGAWVVKMF-YSFQDKRNLYLIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGM------------ 176
Cdd:cd05627  83 FLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKG--HVKLSDFGLctglkkahrtef 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 177 ------------------TRRAGSPVKR--------VSGTIPYTAPELCDTSKHDGFCvdystDVWAFGVLLFCMLTGNF 230
Cdd:cd05627 161 yrnlthnppsdfsfqnmnSKRKAETWKKnrrqlaysTVGTPDYIAPEVFMQTGYNKLC-----DWWSLGVIMYEMLIGYP 235
                       250       260
                ....*....|....*....|
gi 75570321 231 PWEKAMPSDTfYEEFVRWQK 250
Cdd:cd05627 236 PFCSETPQET-YRKVMNWKE 254
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
32-220 1.47e-12

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: 67.36  E-value: 1.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVdLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLyLSPCPF--IINMFGIAFETDEYYVfAQEY 109
Cdd:cd06646  11 YELIQRVGSGTYGDV-YKARNLHTGELAAVKIIKLEPGDDFSLIQQEIFM-VKECKHcnIVAYFGSYLSREKLWI-CMEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 110 APSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRAGSPV-KRVS 188
Cdd:cd06646  88 CGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNG--DVKLADFGVAAKITATIaKRKS 165
                       170       180       190
                ....*....|....*....|....*....|....
gi 75570321 189 --GTIPYTAPELCDTSKHDGFcvDYSTDVWAFGV 220
Cdd:cd06646 166 fiGTPYWMAPEVAAVEKNGGY--NQLCDIWAVGI 197
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
2-281 1.58e-12

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: 68.50  E-value: 1.58e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   2 SSSPVV-SRDILEELQLYT--AQNLEKLEVNKY-YEVIRELGKGTYGKVDLVIHKIRGSKMALKFL---KKKSTKLKSFL 74
Cdd:cd05623  40 SNSPLRrEKNILEYLEWAKpfTSKVKQMRLHKEdFEILKVIGRGAFGEVAVVKLKNADKVFAMKILnkwEMLKRAETACF 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  75 REYSISLYLSPCPFIINMFgIAFETDEYYVFAQEYAPSGDLFDIIPP-QVGLPEPVAKRCVHQVAIALEYLHSKKLVHRD 153
Cdd:cd05623 120 REERDVLVNGDSQWITTLH-YAFQDDNNLYLVMDYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRD 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 154 IKPENILIfDKECRkVKLSDFGMTRRA---GSPVKRVS-GTIPYTAPELCDTSKHDGFCVDYSTDVWAFGVLLFCMLTGN 229
Cdd:cd05623 199 IKPDNILM-DMNGH-IRLADFGSCLKLmedGTVQSSVAvGTPDYISPEILQAMEDGKGKYGPECDWWSLGVCMYEMLYGE 276
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 75570321 230 FPWEKAMPSDTfYEEFVRWQKRRTgaVPSQWRRFTDESLRMFRKLLALEQER 281
Cdd:cd05623 277 TPFYAESLVET-YGKIMNHKERFQ--FPTQVTDVSENAKDLIRRLICSREHR 325
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
83-237 1.83e-12

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: 67.00  E-value: 1.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  83 LSPC--PFIINMFGIAFETDEYYVFaQEYAPSGDLFDIIPPQvGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENIL 160
Cdd:cd06642  56 LSQCdsPYITRYYGSYLKGTKLWII-MEYLGGGSALDLLKPG-PLEETYIATILREILKGLDYLHSERKIHRDIKAANVL 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 161 IfdKECRKVKLSDFGMT-RRAGSPVKRVS--GTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWEKAMP 237
Cdd:cd06642 134 L--SEQGDVKLADFGVAgQLTDTQIKRNTfvGTPFWMAPEVIKQSAY-----DFKADIWSLGITAIELAKGEPPNSDLHP 206
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
38-240 2.16e-12

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: 66.52  E-value: 2.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGiAFETDEYYVFAQEYAPSGDLFD 117
Cdd:cd14115   1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQH-PQYITLHD-TYESPTSYILVLELMDDGRLLD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 118 IIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI-FDKECRKVKLSDFG--MTRRAGSPVKRVSGTIPYT 194
Cdd:cd14115  79 YLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIdLRIPVPRVKLIDLEdaVQISGHRHVHHLLGNPEFA 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75570321 195 APELCDtskhdGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDT 240
Cdd:cd14115 159 APEVIQ-----GTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEET 199
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
129-227 2.75e-12

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 66.77  E-value: 2.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  129 VAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRKVKLSDFGMTRRAGSPVKRVSG---TIPYTAPELCDTSKHd 205
Cdd:PLN00009 103 LIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLI-DRRTNALKLADFGLARAFGIPVRTFTHevvTLWYRAPEILLGSRH- 180
                         90       100
                 ....*....|....*....|....
gi 75570321  206 gfcvdYST--DVWAFGVLLFCMLT 227
Cdd:PLN00009 181 -----YSTpvDIWSVGCIFAEMVN 199
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
89-292 2.95e-12

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: 65.75  E-value: 2.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFETDEYYVfAQEYAPSGDLFDIIPPQVG--LPEPVAKRCVHQVAIALEYLHSK---KLVHRDIKPENILIFD 163
Cdd:cd14060  44 IIQFYGAILEAPNYGI-VTEYASYGSLFDYLNSNESeeMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAA 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 164 KECrkVKLSDFGMTRRAG-SPVKRVSGTIPYTAPELCDtskhdGFCVDYSTDVWAFGVLLFCMLTGNFPWEKampsdtfY 242
Cdd:cd14060 123 DGV--LKICDFGASRFHShTTHMSLVGTFPWMAPEVIQ-----SLPVSETCDTYSYGVVLWEMLTREVPFKG-------L 188
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 243 EEF-VRW---QKRRTGAVPSQW-RRFTDeslrMFRKLLALEQERRCSVKEVFAHL 292
Cdd:cd14060 189 EGLqVAWlvvEKNERPTIPSSCpRSFAE----LMRRCWEADVKERPSFKQIIGIL 239
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
95-241 3.37e-12

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: 65.91  E-value: 3.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  95 IAFETDEYYVFAQEYapsGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLS-- 172
Cdd:cd13976  54 IAGETKAYVFFERDH---GDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRLEsl 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 173 ---------DFGMTRRAGSPVkrvsgtipYTAPELCDTSKHdgfcvdYS---TDVWAFGVLLFCMLTGNFPWEKAMPSDT 240
Cdd:cd13976 131 edavilegeDDSLSDKHGCPA--------YVSPEILNSGAT------YSgkaADVWSLGVILYTMLVGRYPFHDSEPASL 196

                .
gi 75570321 241 F 241
Cdd:cd13976 197 F 197
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
27-226 3.45e-12

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: 67.01  E-value: 3.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  27 EVNKYYEVIRELGKGTYGKVDLVIHKIRGSKMA---LKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIaFET---- 99
Cdd:cd07855   2 DVGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAikkIPNAFDVVTTAKRTLRELKILRHFKH-DNIIAIRDI-LRPkvpy 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 100 ----DEYYVF-AQEyapsGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECrKVKLSDF 174
Cdd:cd07855  80 adfkDVYVVLdLME----SDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLV-NENC-ELKIGDF 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75570321 175 GMTRRA-GSPVKRVS------GTIPYTAPELCDTSKhdgfcvDYST--DVWAFGVLLFCML 226
Cdd:cd07855 154 GMARGLcTSPEEHKYfmteyvATRWYRAPELMLSLP------EYTQaiDMWSVGCIFAEML 208
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
32-227 3.76e-12

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: 66.29  E-value: 3.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKL---KSFLREYSISLYLSPcPFIINMFGIAFETDE-YYVFaq 107
Cdd:cd07861   2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEgvpSTAIREISLLKELQH-PNIVCLEDVLMQENRlYLVF-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYApSGDL---FDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTRRAGSPV 184
Cdd:cd07861  79 EFL-SMDLkkyLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGV--IKLADFGLARAFGIPV 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 75570321 185 KRVSG---TIPYTAPELCDTSKHdgfcvdYST--DVWAFGVLLFCMLT 227
Cdd:cd07861 156 RVYTHevvTLWYRAPEVLLGSPR------YSTpvDIWSIGTIFAEMAT 197
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
32-242 3.79e-12

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: 66.25  E-value: 3.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKV----DLVIHKIRGSKMALKFLKKKSTKLKSflREYSIslyLSPC--PFIINMFGIAFETDEYYVF 105
Cdd:cd06641   6 FTKLEKIGKGSFGEVfkgiDNRTQKVVAIKIIDLEEAEDEIEDIQ--QEITV---LSQCdsPYVTKYYGSYLKDTKLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 106 aQEYAPSGDLFDIIPPQvGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMT-RRAGSPV 184
Cdd:cd06641  81 -MEYLGGGSALDLLEPG-PLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLL--SEHGEVKLADFGVAgQLTDTQI 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 KR--VSGTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWEKAMPSDTFY 242
Cdd:cd06641 157 KRn*FVGTPFWMAPEVIKQSAYDS-----KADIWSLGITAIELARGEPPHSELHPMKVLF 211
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
89-232 3.83e-12

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: 66.58  E-value: 3.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFETDEYYVFAqEYAPSGDLFDII----PPQVG-------LPEPVAK-----RCVHQVAIALEYLHSKKLVHR 152
Cdd:cd05100  80 IINLLGACTQDGPLYVLV-EYASKGNLREYLrarrPPGMDysfdtckLPEEQLTfkdlvSCAYQVARGMEYLASQKCIHR 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 153 DIKPENILIFDKECrkVKLSDFGMTRRAGSP---VKRVSGTIP--YTAPE-LCDTskhdgfCVDYSTDVWAFGVLLFCML 226
Cdd:cd05100 159 DLAARNVLVTEDNV--MKIADFGLARDVHNIdyyKKTTNGRLPvkWMAPEaLFDR------VYTHQSDVWSFGVLLWEIF 230

                ....*..
gi 75570321 227 T-GNFPW 232
Cdd:cd05100 231 TlGGSPY 237
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
134-291 4.04e-12

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 66.55  E-value: 4.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 134 VHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRAGSPVKRVSG---TIPYTAPELCDTSKhdgfcvD 210
Cdd:cd07872 110 LYQILRGLAYCHRRKVLHRDLKPQNLLINERG--ELKLADFGLARAKSVPTKTYSNevvTLWYRPPDVLLGSS------E 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 211 YST--DVWAFGVLLFCMLTG--------------------NFPWEKAMPSDTFYEEFVRWQ--KRRTGAVPSQWRRFTDE 266
Cdd:cd07872 182 YSTqiDMWGVGCIFFEMASGrplfpgstvedelhlifrllGTPTEETWPGISSNDEFKNYNfpKYKPQPLINHAPRLDTE 261
                       170       180
                ....*....|....*....|....*
gi 75570321 267 SLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07872 262 GIELLTKFLQYESKKRISAEEAMKH 286
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
21-328 4.22e-12

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: 66.60  E-value: 4.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  21 QNLEKL--EVNKYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPF-----IINMF 93
Cdd:cd07877   6 QELNKTiwEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHenvigLLDVF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  94 GIAFETDEYY-VFAQEYAPSGDLFDIIPPQvGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECrKVKLS 172
Cdd:cd07877  86 TPARSLEEFNdVYLVTHLMGADLNNIVKCQ-KLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAV-NEDC-ELKIL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 173 DFGMTRRAGSPVKRVSGTIPYTAPELCDTSKHdgfcVDYSTDVWAFGVLLFCMLTGN--FPWE----------------- 233
Cdd:cd07877 163 DFGLARHTDDEMTGYVATRWYRAPEIMLNWMH----YNQTVDIWSVGCIMAELLTGRtlFPGTdhidqlklilrlvgtpg 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 234 ----KAMPSD---TFYEEFVRWQKRR-----TGAVPsqwrrftdESLRMFRKLLALEQERRCSVKEVFAHLGHRWMLDgT 301
Cdd:cd07877 239 aellKKISSEsarNYIQSLTQMPKMNfanvfIGANP--------LAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHD-P 309
                       330       340
                ....*....|....*....|....*..
gi 75570321 302 SGNHHQSVLNSSSEEDELLVDRMKQQT 328
Cdd:cd07877 310 DDEPVADPYDQSFESRDLLIDEWKSLT 336
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
108-276 4.31e-12

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, 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, like BMPR1, 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 BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 65.96  E-value: 4.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCvHQVAIALEYLHSK--------KLVHRDIKPENILIfdKECRKVKLSDFGMTRR 179
Cdd:cd14144  73 DYHENGSLYDFLRGNTLDTQSMLKLA-YSAACGLAHLHTEifgtqgkpAIAHRDIKSKNILV--KKNGTCCIADLGLAVK 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 180 AGSPVKRVS-------GTIPYTAPELCDTS-KHDGFCVDYSTDVWAFGVLLF-----CMLTG-----NFPWEKAMPSDTF 241
Cdd:cd14144 150 FISETNEVDlppntrvGTKRYMAPEVLDESlNRNHFDAYKMADMYSFGLVLWeiarrCISGGiveeyQLPYYDAVPSDPS 229
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 75570321 242 YEEFVR--WQKRRTGAVPSQWrrFTDESLRMFRKLLA 276
Cdd:cd14144 230 YEDMRRvvCVERRRPSIPNRW--SSDEVLRTMSKLMS 264
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
89-232 4.45e-12

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: 66.19  E-value: 4.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFETDEYYVFAqEYAPSGDLFDII----PPQVGLPEPVAK------------RCVHQVAIALEYLHSKKLVHR 152
Cdd:cd05101  92 IINLLGACTQDGPLYVIV-EYASKGNLREYLrarrPPGMEYSYDINRvpeeqmtfkdlvSCTYQLARGMEYLASQKCIHR 170
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 153 DIKPENILIfdKECRKVKLSDFGMTRRAGSP---VKRVSGTIP--YTAPE-LCDTskhdgfCVDYSTDVWAFGVLLFCML 226
Cdd:cd05101 171 DLAARNVLV--TENNVMKIADFGLARDINNIdyyKKTTNGRLPvkWMAPEaLFDR------VYTHQSDVWSFGVLMWEIF 242

                ....*..
gi 75570321 227 T-GNFPW 232
Cdd:cd05101 243 TlGGSPY 249
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
35-291 4.51e-12

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 65.81  E-value: 4.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  35 IRELGKGTYGKV-------DLVIHKIRGSKmalkFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGiAFETDEYYVFAQ 107
Cdd:cd14138  10 LEKIGSGEFGSVfkcvkrlDGCIYAIKRSK----KPLAGSVDEQNALREVYAHAVLGQHSHVVRYYS-AWAEDDHMLIQN 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVG----LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI-------------FDKECR--K 168
Cdd:cd14138  85 EYCNGGSLADAISENYRimsyFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFIsrtsipnaaseegDEDEWAsnK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 169 V--KLSDFGMTRRAGSPvKRVSGTIPYTAPELCDTskhdgfcvDYS----TDVWAFGVLLFCmltgnfpwekAMPSDTFY 242
Cdd:cd14138 165 VifKIGDLGHVTRVSSP-QVEEGDSRFLANEVLQE--------NYThlpkADIFALALTVVC----------AAGAEPLP 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 75570321 243 EEFVRWQKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14138 226 TNGDQWHEIRQGKLPRIPQVLSQEFLDLLKVMIHPDPERRPSAVALVKH 274
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
75-237 4.73e-12

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: 65.77  E-value: 4.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  75 REYSISLYLSPCPFIINMFG---IAFETDEYYVFA-QEYAPSGDLFDIIPP--QVGLPEPVAKRCVHQVAIALEYLHSKK 148
Cdd:cd14037  49 REIEIMKRLSGHKNIVGYIDssaNRSGNGVYEVLLlMEYCKGGGVIDLMNQrlQTGLTESEILKIFCDVCEAVAAMHYLK 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 149 --LVHRDIKPENILIFDKecRKVKLSDFGMTRRAGSPVKRVSG------------TIPYTAPELCDTskHDGFCVDYSTD 214
Cdd:cd14037 129 ppLIHRDLKVENVLISDS--GNYKLCDFGSATTKILPPQTKQGvtyveedikkytTLQYRAPEMIDL--YRGKPITEKSD 204
                       170       180
                ....*....|....*....|....*
gi 75570321 215 VWAFGVLLF--CMLTgnFPWEKAMP 237
Cdd:cd14037 205 IWALGCLLYklCFYT--TPFEESGQ 227
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
87-223 4.83e-12

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: 65.87  E-value: 4.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVFAqEYAPSGDLFDI---IPPQVGLPEPVAKR----CVHQVAIALEYLHSKKLVHRDIKPENI 159
Cdd:cd05036  69 PNIVRCIGVCFQRLPRFILL-ELMAGGDLKSFlreNRPRPEQPSSLTMLdllqLAQDVAKGCRYLEENHFIHRDIAARNC 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 160 LIFDKEC-RKVKLSDFGMTR------------RAGSPVKrvsgtipYTAPE-LCD---TSKhdgfcvdysTDVWAFGVLL 222
Cdd:cd05036 148 LLTCKGPgRVAKIGDFGMARdiyradyyrkggKAMLPVK-------WMPPEaFLDgifTSK---------TDVWSFGVLL 211

                .
gi 75570321 223 F 223
Cdd:cd05036 212 W 212
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
89-291 5.00e-12

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: 65.83  E-value: 5.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFETDEYYVfAQEYAPSGDLFDIIPPQVGLPEPVAKRCVhQVAIALEYLHSKKLVHRDIKPENILIFDKEcrK 168
Cdd:cd06658  81 VVDMYNSYLVGDELWV-VMEFLEGGALTDIVTHTRMNEEQIATVCL-SVLRALSYLHNQGVIHRDIKSDSILLTSDG--R 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 169 VKLSDFGMTRRAGSPV---KRVSGTIPYTAPELCDTskhdgfcVDYST--DVWAFGVLLFCMLTGNFPWekampsdtFYE 243
Cdd:cd06658 157 IKLSDFGFCAQVSKEVpkrKSLVGTPYWMAPEVISR-------LPYGTevDIWSLGIMVIEMIDGEPPY--------FNE 221
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75570321 244 EFVRWQKRRTGAVPSQWRRFTDES--LRMFRKL-LALEQERRCSVKEVFAH 291
Cdd:cd06658 222 PPLQAMRRIRDNLPPRVKDSHKVSsvLRGFLDLmLVREPSQRATAQELLQH 272
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
33-227 5.78e-12

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: 65.44  E-value: 5.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  33 EVIRELGKGTYGKV-----DLVIHKIRGSKMA--LKFLKKKSTKLKSFLREYSIsLYLSPCPFIINMFGIAFETDEYYVF 105
Cdd:cd05032   9 TLIRELGQGSFGMVyeglaKGVVKGEPETRVAikTVNENASMRERIEFLNEASV-MKEFNCHHVVRLLGVVSTGQPTLVV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 106 aQEYAPSGDLFDII----PPQV---GLPEPVAKRCVH---QVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFG 175
Cdd:cd05032  88 -MELMAKGDLKSYLrsrrPEAEnnpGLGPPTLQKFIQmaaEIADGMAYLAAKKFVHRDLAARNCMV--AEDLTVKIGDFG 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75570321 176 MTR--------RAGS----PVKrvsgtipYTAPElcdtSKHDGFCVDYStDVWAFGVLLFCMLT 227
Cdd:cd05032 165 MTRdiyetdyyRKGGkgllPVR-------WMAPE----SLKDGVFTTKS-DVWSFGVVLWEMAT 216
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
30-239 5.95e-12

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: 65.32  E-value: 5.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  30 KYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGiAFETDEYYVFAQEY 109
Cdd:cd14110   3 KTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQLVLREYQVLRRLSH-PRIAQLHS-AYLSPRHLVLIEEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 110 APSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFG----MTRRAGSPVK 185
Cdd:cd14110  81 CSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNL--LKIVDLGnaqpFNQGKVLMTD 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 75570321 186 RVSGTIPYTAPELCdtskhDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSD 239
Cdd:cd14110 159 KKGDYVETMAPELL-----EGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWE 207
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
89-227 6.21e-12

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: 65.52  E-value: 6.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFETDEYYVFAqEYAPSGDLFDII----PP----QVGLPEPVAKR--------CVHQVAIALEYLHSKKLVHR 152
Cdd:cd05053  79 IINLLGACTQDGPLYVVV-EYASKGNLREFLrarrPPgeeaSPDDPRVPEEQltqkdlvsFAYQVARGMEYLASKKCIHR 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 153 DIKPENILIFDKECrkVKLSDFGMTRRAGSP---VKRVSGTIPY--TAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLT 227
Cdd:cd05053 158 DLAARNVLVTEDNV--MKIADFGLARDIHHIdyyRKTTNGRLPVkwMAPEALFDRVY-----THQSDVWSFGVLLWEIFT 230
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
74-291 6.30e-12

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: 65.52  E-value: 6.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  74 LREYSI--SLYLSPCPFIINMFGiAFETDEYYVFAQEYAPSGDLfDIIPPQVG----LPEPVAKRCVHQVAIALEYLHSK 147
Cdd:cd14052  48 LEEVSIlrELTLDGHDNIVQLID-SWEYHGHLYIQTELCENGSL-DVFLSELGllgrLDEFRVWKILVELSLGLRFIHDH 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 148 KLVHRDIKPENILI-FDKecrKVKLSDFGMTRRAGSPVKR-VSGTIPYTAPELcdTSKHDgfcVDYSTDVWAFGVLLFcM 225
Cdd:cd14052 126 HFVHLDLKPANVLItFEG---TLKIGDFGMATVWPLIRGIeREGDREYIAPEI--LSEHM---YDKPADIFSLGLILL-E 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 226 LTGNFpwekAMPSDTfyeefVRWQKRRTG------------------------AVPSQWRRFTDESLRMFRKLLALEQER 281
Cdd:cd14052 197 AAANV----VLPDNG-----DAWQKLRSGdlsdaprlsstdlhsasspssnppPDPPNMPILSGSLDRVVRWMLSPEPDR 267
                       250
                ....*....|
gi 75570321 282 RCSVKEVFAH 291
Cdd:cd14052 268 RPTADDVLAT 277
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
86-239 6.53e-12

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: 65.54  E-value: 6.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  86 CPFIINMFgIAFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKE 165
Cdd:cd05606  57 CPFIVCMT-YAFQTPDKLCFILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILL--DE 133
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75570321 166 CRKVKLSDFGMT-----RRAGSPVkrvsGTIPYTAPELcdTSKhdGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSD 239
Cdd:cd05606 134 HGHVRISDLGLAcdfskKKPHASV----GTHGYMAPEV--LQK--GVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKD 204
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
136-236 6.55e-12

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 65.14  E-value: 6.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTR--RAGSPVKRVSGTIP--YTAPELCD----TSkhdgf 207
Cdd:cd05056 115 QLSTALAYLESKRFVHRDIAARNVLVSSPDC--VKLGDFGLSRymEDESYYKASKGKLPikWMAPESINfrrfTS----- 187
                        90       100
                ....*....|....*....|....*....
gi 75570321 208 cvdySTDVWAFGVllfCMltgnfpWEKAM 236
Cdd:cd05056 188 ----ASDVWMFGV---CM------WEILM 203
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
35-233 6.68e-12

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


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 64.97  E-value: 6.68e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  35 IRELGKGTYGkvdlVIHK---IRGSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIAFE-TDEYYVFaqEYA 110
Cdd:cd05112   9 VQEIGSGQFG----LVHLgywLNKDKVAIKTIREGAMSEEDFIEEAEVMMKLSH-PKLVQLYGVCLEqAPICLVF--EFM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGDLFDIIPPQVGL--PEPVAKRCVhQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR---------R 179
Cdd:cd05112  82 EHGCLSDYLRTQRGLfsAETLLGMCL-DVCEGMAYLEEASVIHRDLAARNCLV--GENQVVKVSDFGMTRfvlddqytsS 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75570321 180 AGS--PVKrvsgtipYTAPELCDTSKhdgfcvdYST--DVWAFGVLLFCMLT-GNFPWE 233
Cdd:cd05112 159 TGTkfPVK-------WSSPEVFSFSR-------YSSksDVWSFGVLMWEVFSeGKIPYE 203
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
32-220 6.98e-12

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: 65.45  E-value: 6.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIAFETDEYYVfAQEYAP 111
Cdd:cd06645  13 FELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWI-CMEFCG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 112 SGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRAGSPV-KRVS-- 188
Cdd:cd06645  92 GGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNG--HVKLADFGVSAQITATIaKRKSfi 169
                       170       180       190
                ....*....|....*....|....*....|..
gi 75570321 189 GTIPYTAPELCDTSKHDGFcvDYSTDVWAFGV 220
Cdd:cd06645 170 GTPYWMAPEVAAVERKGGY--NQLCDIWAVGI 199
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
141-231 7.61e-12

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: 65.48  E-value: 7.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 141 LEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAGSPVKRVSG---TIPYTAPELCDTSKhdgfcvDYST--DV 215
Cdd:cd07844 111 LAYCHQRRVLHRDLKPQNLLI--SERGELKLADFGLARAKSVPSKTYSNevvTLWYRPPDVLLGST------EYSTslDM 182
                        90
                ....*....|....*...
gi 75570321 216 WAFGVLLFCMLTGN--FP 231
Cdd:cd07844 183 WGVGCIFYEMATGRplFP 200
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
116-224 7.80e-12

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: 65.37  E-value: 7.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 116 FDIIPPQvGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTR-----RAGSPvkrVSGT 190
Cdd:cd07863  97 LDKVPPP-GLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGG--QVKLADFGLARiyscqMALTP---VVVT 170
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 75570321 191 IPYTAPELCDTSKhdgfcvdYST--DVWAFGVL---------LFC 224
Cdd:cd07863 171 LWYRAPEVLLQST-------YATpvDMWSVGCIfaemfrrkpLFC 208
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
96-291 7.85e-12

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: 66.22  E-value: 7.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  96 AFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFG 175
Cdd:cd05625  69 SFQDKDNLYFVMDYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILI-DRDGH-IKLTDFG 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 176 ---------------------------------------------MTRRAGSPVKR-----VSGTIPYTAPELCDTSKHD 205
Cdd:cd05625 147 lctgfrwthdskyyqsgdhlrqdsmdfsnewgdpencrcgdrlkpLERRAARQHQRclahsLVGTPNYIAPEVLLRTGYT 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 206 GFCvdystDVWAFGVLLFCMLTGNFPWEKAMPSDTfYEEFVRWQKrrTGAVPSQwRRFTDESLRMFRKLLALEQER--RC 283
Cdd:cd05625 227 QLC-----DWWSVGVILFEMLVGQPPFLAQTPLET-QMKVINWQT--SLHIPPQ-AKLSPEASDLIIKLCRGPEDRlgKN 297

                ....*...
gi 75570321 284 SVKEVFAH 291
Cdd:cd05625 298 GADEIKAH 305
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
136-233 8.33e-12

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: 64.61  E-value: 8.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTR---------RAGS--PVKrvsgtipYTAPElcdTSKH 204
Cdd:cd05034 100 QIASGMAYLESRNYIHRDLAARNILVGENNV--CKVADFGLARlieddeytaREGAkfPIK-------WTAPE---AALY 167
                        90       100       110
                ....*....|....*....|....*....|
gi 75570321 205 DGFCVdySTDVWAFGVLLFCMLT-GNFPWE 233
Cdd:cd05034 168 GRFTI--KSDVWSFGILLYEIVTyGRVPYP 195
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
37-234 9.33e-12

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: 64.97  E-value: 9.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  37 ELGKGTYGKVDLVIHKIRGSKM----ALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIAfeTDEYYVFAQEYAPS 112
Cdd:cd05115  11 ELGSGNFGCVKKGVYKMRKKQIdvaiKVLKQGNEKAVRDEMMREAQIMHQLDN-PYIVRMIGVC--EAEALMLVMEMASG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 113 GDLFDIIppqVGLPEPVAKRCV----HQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRAGSP----V 184
Cdd:cd05115  88 GPLNKFL---SGKKDEITVSNVvelmHQVSMGMKYLEEKNFVHRDLAARNVLLVNQH--YAKISDFGLSKALGADdsyyK 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 185 KRVSGTIP--YTAPElcdtskhdgfCVDY-----STDVWAFGVLLFCMLT-GNFPWEK 234
Cdd:cd05115 163 ARSAGKWPlkWYAPE----------CINFrkfssRSDVWSYGVTMWEAFSyGQKPYKK 210
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
87-291 9.88e-12

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: 65.13  E-value: 9.88e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVfAQEYAPSGDLFDIIPPQVGLPEPVAKRCvHQVAIALEYLHSKKLVHRDIKPENILIFDKEc 166
Cdd:cd06655  76 PNIVNFLDSFLVGDELFV-VMEYLAGGSLTDVVTETCMDEAQIAAVC-RECLQALEFLHANQVIHRDIKSDNVLLGMDG- 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 167 rKVKLSDFGMTRRAGSPVKRVS---GTIPYTAPELCdTSKHDGFCVdystDVWAFGVLLFCMLTGNFPWEKAMPSDTFY- 242
Cdd:cd06655 153 -SVKLTDFGFCAQITPEQSKRStmvGTPYWMAPEVV-TRKAYGPKV----DIWSLGIMAIEMVEGEPPYLNENPLRALYl 226
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 243 ------EEFVRWQKrrtgaVPSQWRRFTDESLRMfrkllalEQERRCSVKEVFAH 291
Cdd:cd06655 227 iatngtPELQNPEK-----LSPIFRDFLNRCLEM-------DVEKRGSAKELLQH 269
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
89-232 1.00e-11

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: 65.03  E-value: 1.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFETDEYYVFAqEYAPSGDLFDII----PPQVGL---PEPVAKR---------CVHQVAIALEYLHSKKLVHR 152
Cdd:cd05098  81 IINLLGACTQDGPLYVIV-EYASKGNLREYLqarrPPGMEYcynPSHNPEEqlsskdlvsCAYQVARGMEYLASKKCIHR 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 153 DIKPENILIfdKECRKVKLSDFGMTR---RAGSPVKRVSGTIP--YTAPE-LCDTskhdgfCVDYSTDVWAFGVLLFCML 226
Cdd:cd05098 160 DLAARNVLV--TEDNVMKIADFGLARdihHIDYYKKTTNGRLPvkWMAPEaLFDR------IYTHQSDVWSFGVLLWEIF 231

                ....*..
gi 75570321 227 T-GNFPW 232
Cdd:cd05098 232 TlGGSPY 238
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
108-227 1.23e-11

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: 64.54  E-value: 1.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPP-QVGLPEPVAkrCVHQVAIALEYLHSKKLVHRDIKPENILIfDKEcRKVKLSDFGMTRR--AGSPV 184
Cdd:cd05080  88 EYVPLGSLRDYLPKhSIGLAQLLL--FAQQICEGMAYLHSQHYIHRDLAARNVLL-DND-RLVKIGDFGLAKAvpEGHEY 163
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 75570321 185 KRVS--GTIP--YTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLT 227
Cdd:cd05080 164 YRVRedGDSPvfWYAPECLKEYK-----FYYASDVWSFGVTLYELLT 205
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
35-240 1.33e-11

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: 64.13  E-value: 1.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  35 IRELGKGTYGKV---------DLVIHKIRGSKMALKFLkkkstklksfLREYSISLYLSPcPFIINMFGIAfeTDEYYVF 105
Cdd:cd05113   9 LKELGTGQFGVVkygkwrgqyDVAIKMIKEGSMSEDEF----------IEEAKVMMNLSH-EKLVQLYGVC--TKQRPIF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 106 -AQEYAPSGDLFDIIPPQVGLPEPVA--KRCvHQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTRRA-- 180
Cdd:cd05113  76 iITEYMANGCLLNYLREMRKRFQTQQllEMC-KDVCEAMEYLESKQFLHRDLAARNCLVNDQGV--VKVSDFGLSRYVld 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75570321 181 GSPVKRVSGTIP--YTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLT-GNFPWEKAMPSDT 240
Cdd:cd05113 153 DEYTSSVGSKFPvrWSPPEVLMYSKFSS-----KSDVWAFGVLMWEVYSlGKMPYERFTNSET 210
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
87-223 1.40e-11

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


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 64.26  E-value: 1.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVfAQEYAPSGDLFDIIPPQVGlpEPVAKRCVH---QVAIALEYLHSKKLVHRDIKPENILIFD 163
Cdd:cd05085  53 PNIVKLIGVCTQRQPIYI-VMELVPGGDFLSFLRKKKD--ELKTKQLVKfslDAAAGMAYLESKNCIHRDLAARNCLVGE 129
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75570321 164 KECrkVKLSDFGMTRRAGSPVKRVSG----TIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLF 223
Cdd:cd05085 130 NNA--LKISDFGMSRQEDDGVYSSSGlkqiPIKWTAPEALNYGRYSS-----ESDVWSFGILLW 186
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
38-175 1.60e-11

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 61.30  E-value: 1.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFL-REYSISLYLS-PCPFIINMFGiAFETDEYYVFAQEYAPSGDL 115
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLeSEMDILRRLKgLELNIPKVLV-TEDVDGPNILLMELVKGGTL 79
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 116 FDIIPpQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFG 175
Cdd:cd13968  80 IAYTQ-EEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILL--SEDGNVKLIDFG 136
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
20-234 1.64e-11

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


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 63.85  E-value: 1.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  20 AQNLEKLEVnkyyevIRELGKGTYGkvDLVIHKIRGSKMALKFLKKKSTKLKSfLREYSISLYLSPcPFIINMFGIAFET 99
Cdd:cd05082   2 ALNMKELKL------LQTIGKGEFG--DVMLGDYRGNKVAVKCIKNDATAQAF-LAEASVMTQLRH-SNLVQLLGVIVEE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 100 DEYYVFAQEYAPSGDLFDIIPPQvGLPEPVAKRCVH---QVAIALEYLHSKKLVHRDIKPENILIFDKECRKVklSDFGM 176
Cdd:cd05082  72 KGGLYIVTEYMAKGSLVDYLRSR-GRSVLGGDCLLKfslDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKV--SDFGL 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75570321 177 TRRAGSPVKRVSGTIPYTAPELCDTSKhdgfcvdYST--DVWAFGVLLFCMLT-GNFPWEK 234
Cdd:cd05082 149 TKEASSTQDTGKLPVKWTAPEALREKK-------FSTksDVWSFGILLWEIYSfGRVPYPR 202
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
86-239 1.80e-11

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: 64.68  E-value: 1.80e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  86 CPFIINMfGIAFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKE 165
Cdd:cd14223  62 CPFIVCM-SYAFHTPDKLSFILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILL--DE 138
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 166 CRKVKLSDFGMTRRAGSPVKRVS-GTIPYTAPELCdtskHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSD 239
Cdd:cd14223 139 FGHVRISDLGLACDFSKKKPHASvGTHGYMAPEVL----QKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKD 209
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
136-241 1.83e-11

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


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 63.99  E-value: 1.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENILIFDKECRKVklSDFGMTRRAGSPVKRVSGT-IPY--TAPElcdTSKHDGFCVdyS 212
Cdd:cd05148 112 QVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKV--ADFGLARLIKEDVYLSSDKkIPYkwTAPE---AASHGTFST--K 184
                        90       100       110
                ....*....|....*....|....*....|
gi 75570321 213 TDVWAFGVLLFCMLT-GNFPWEKAMPSDTF 241
Cdd:cd05148 185 SDVWSFGILLYEMFTyGQVPYPGMNNHEVY 214
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
108-228 2.02e-11

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: 63.43  E-value: 2.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQ-VGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFD--KECRKV-KLSDFGMTR---RA 180
Cdd:cd14068  65 ELAPKGSLDALLQQDnASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTlyPNCAIIaKIADYGIAQyccRM 144
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 75570321 181 GspVKRVSGTIPYTAPELCdtskHDGFCVDYSTDVWAFGVLLFCMLTG 228
Cdd:cd14068 145 G--IKTSEGTPGFRAPEVA----RGNVIYNQQADVYSFGLLLYDILTC 186
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
87-223 2.06e-11

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: 63.83  E-value: 2.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAfeTDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEc 166
Cdd:cd05116  56 PYIVRMIGIC--EAESWMLVMEMAELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQH- 132
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 167 rKVKLSDFGMTRRAGSPVK----RVSGTIP--YTAPElcdtskhdgfCVDY-----STDVWAFGVLLF 223
Cdd:cd05116 133 -YAKISDFGLSKALRADENyykaQTHGKWPvkWYAPE----------CMNYykfssKSDVWSFGVLMW 189
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
137-234 2.27e-11

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: 63.35  E-value: 2.27e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 137 VAIALEYLHSKKLVHRDIKPENILIFDKECRKVklSDFGMTRRAGSPVKRVSGTIPYTAPElcdTSKHDGFCVdySTDVW 216
Cdd:cd05083 109 VAEGMEYLESKKLVHRDLAARNILVSEDGVAKI--SDFGLAKVGSMGVDNSRLPVKWTAPE---ALKNKKFSS--KSDVW 181
                        90
                ....*....|....*....
gi 75570321 217 AFGVLLFCMLT-GNFPWEK 234
Cdd:cd05083 182 SYGVLLWEVFSyGRAPYPK 200
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
32-231 2.90e-11

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: 63.49  E-value: 2.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIAFET-----DEYYVFA 106
Cdd:cd06636  18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKsppghDDQLWLV 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 107 QEYAPSGDLFDIIPPQVG--LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAGSPV 184
Cdd:cd06636  98 MEFCGAGSVTDLVKNTKGnaLKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLL--TENAEVKLVDFGVSAQLDRTV 175
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 KRVS---GTIPYTAPELCDTSKHDGFCVDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:cd06636 176 GRRNtfiGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPP 225
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
32-234 3.01e-11

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 63.05  E-value: 3.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLrEYSISLYLSPCPFIINMFGiAFETDEY-YVFAQEYA 110
Cdd:cd14017   2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPKQVLKM-EVAVLKKLQGKPHFCRLIG-CGRTERYnYIVMTLLG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PS-GDLFDIIPPQVgLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI--FDKECRKVKLSDFGMTRRAGSPVKRV 187
Cdd:cd14017  80 PNlAELRRSQPRGK-FSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIgrGPSDERTVYILDFGLARQYTNKDGEV 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 188 S----------GTIPY---TAPELCDTSKHDgfcvdystDVWAFGVLLFCMLTGNFPWEK 234
Cdd:cd14017 159 ErpprnaagfrGTVRYasvNAHRNKEQGRRD--------DLWSWFYMLIEFVTGQLPWRK 210
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
97-233 3.87e-11

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: 62.96  E-value: 3.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  97 FETDEYYVFAQEYAPSGDLFDIIPPQVG-LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKecRKVKLSDFG 175
Cdd:cd14186  70 FEDSNYVYLVLEMCHNGEMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRN--MNIKIADFG 147
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75570321 176 MTRRAGSPVKR---VSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd14186 148 LATQLKMPHEKhftMCGTPNYISPEIATRSAH-----GLESDVWSLGCMFYTLLVGRPPFD 203
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
32-291 4.11e-11

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: 63.71  E-value: 4.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFL---REYSISLYLSPCPFIINMFgIAFETDEYYVFAQE 108
Cdd:cd05629   3 FHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLahvKAERDVLAESDSPWVVSLY-YSFQDAQYLYLIME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGM------------ 176
Cdd:cd05629  82 FLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILI-DRGGH-IKLSDFGLstgfhkqhdsay 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 177 --------------TRRAGSPVKRVS------------------------GTIPYTAPELCDTSKHDGFCvdystDVWAF 218
Cdd:cd05629 160 yqkllqgksnknriDNRNSVAVDSINltmsskdqiatwkknrrlmaystvGTPDYIAPEIFLQQGYGQEC-----DWWSL 234
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 219 GVLLFCMLTGNFPWEKAMPSDTfYEEFVRWqkRRTGAVPSQWrRFTDESLRMFRKLLALEQER--RCSVKEVFAH 291
Cdd:cd05629 235 GAIMFECLIGWPPFCSENSHET-YRKIINW--RETLYFPDDI-HLSVEAEDLIRRLITNAENRlgRGGAHEIKSH 305
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
136-234 4.37e-11

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


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 62.75  E-value: 4.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENILIfdkECRKVKLSDFGM--------TRRAGSPVKRVSGTIPYTAPELC---DTSKH 204
Cdd:cd14063 105 QICQGMGYLHAKGIIHKDLKSKNIFL---ENGRVVITDFGLfslsgllqPGRREDTLVIPNGWLCYLAPEIIralSPDLD 181
                        90       100       110
                ....*....|....*....|....*....|..
gi 75570321 205 DGFCVDYS--TDVWAFGVLLFCMLTGNFPWEK 234
Cdd:cd14063 182 FEESLPFTkaSDVYAFGTVWYELLAGRWPFKE 213
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
32-231 5.13e-11

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: 62.81  E-value: 5.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIAFET-----DEYYVFA 106
Cdd:cd06637   8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKnppgmDDQLWLV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 107 QEYAPSGDLFDIIPPQVG--LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAGSPV 184
Cdd:cd06637  88 MEFCGAGSVTDLIKNTKGntLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLL--TENAEVKLVDFGVSAQLDRTV 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 75570321 185 KRVS---GTIPYTAPELCDTSKHDGFCVDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:cd06637 166 GRRNtfiGTPYWMAPEVIACDENPDATYDFKSDLWSLGITAIEMAEGAPP 215
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
108-233 5.48e-11

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 63.73  E-value: 5.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  108 EYAPSGDLFDIIPPQVGLPEPVAKrcvH-------QVAIALEYLHSKKLVHRDIKPENILIfdkeCRK--VKLSDFGMTR 178
Cdd:PTZ00283 119 DYANAGDLRQEIKSRAKTNRTFRE---HeagllfiQVLLAVHHVHSKHMIHRDIKSANILL----CSNglVKLGDFGFSK 191
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75570321  179 RAGSPV-----KRVSGTIPYTAPEL---CDTSKhdgfcvdySTDVWAFGVLLFCMLTGNFPWE 233
Cdd:PTZ00283 192 MYAATVsddvgRTFCGTPYYVAPEIwrrKPYSK--------KADMFSLGVLLYELLTLKRPFD 246
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
123-227 5.65e-11

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: 63.15  E-value: 5.65e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 123 VGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDK--ECRKVKLSDFGMTRRAGSPVKRVSGTIP------YT 194
Cdd:cd07868 119 VQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEgpERGRVKIADMGFARLFNSPLKPLADLDPvvvtfwYR 198
                        90       100       110
                ....*....|....*....|....*....|...
gi 75570321 195 APELCDTSKHdgfcVDYSTDVWAFGVLLFCMLT 227
Cdd:cd07868 199 APELLLGARH----YTKAIDIWAIGCIFAELLT 227
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
125-227 5.87e-11

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: 63.16  E-value: 5.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 125 LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDK--ECRKVKLSDFGMTRRAGSPVKRVSGTIP------YTAP 196
Cdd:cd07867 106 LPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEgpERGRVKIADMGFARLFNSPLKPLADLDPvvvtfwYRAP 185
                        90       100       110
                ....*....|....*....|....*....|.
gi 75570321 197 ELCDTSKHdgfcVDYSTDVWAFGVLLFCMLT 227
Cdd:cd07867 186 ELLLGARH----YTKAIDIWAIGCIFAELLT 212
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
98-291 6.30e-11

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: 61.99  E-value: 6.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  98 ETDEYYVFAQEYapsGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLS---DF 174
Cdd:cd14023  57 DTKAYVFFEKDF---GDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLRLEsleDT 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 175 GMTRRAGSPVKRVSGTIPYTAPELCDTSkhdGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFyeefvrwQKRRTG 254
Cdd:cd14023 134 HIMKGEDDALSDKHGCPAYVSPEILNTT---GTYSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALF-------SKIRRG 203
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 75570321 255 --AVPSQwrrFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14023 204 qfCIPDH---VSPKARCLIRSLLRREPSERLTAPEILLH 239
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
108-288 6.64e-11

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: 62.13  E-value: 6.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVgLPEPVAKRCVHQVAIALEYLHSKK--LVHRDIKPENILIFDKecRKVKLSDFGMTRRAGSPVK 185
Cdd:cd14025  73 EYMETGSLEKLLASEP-LPWELRFRIIHETAVGMNFLHCMKppLLHLDLKPANILLDAH--YHVKISDFGLAKWNGLSHS 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 186 R------VSGTIPYTAPElcdTSKHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEEFVRWQKRRTGAVPSQ 259
Cdd:cd14025 150 HdlsrdgLRGTIAYLPPE---RFKEKNRCPDTKHDVYSFAIVIWGILTQKKPFAGENNILHIMVKVVKGHRPSLSPIPRQ 226
                       170       180
                ....*....|....*....|....*....
gi 75570321 260 WRRFTDESLRMFRKLLALEQERRCSVKEV 288
Cdd:cd14025 227 RPSECQQMICLMKRCWDQDPRKRPTFQDI 255
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
38-232 7.19e-11

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: 62.71  E-value: 7.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISL----YLSPCPFIINMFGiAFETDEYYVFAQEYAPSG 113
Cdd:cd05088  15 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELevlcKLGHHPNIINLLG-ACEHRGYLYLAIEYAPHG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDII--------PPQVGLPEPVAKRCVHQ--------VAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMT 177
Cdd:cd05088  94 NLLDFLrksrvletDPAFAIANSTASTLSSQqllhfaadVARGMDYLSQKQFIHRDLAARNILV--GENYVAKIADFGLS 171
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 178 RRAGSPVKRVSGTIP--YTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLT-GNFPW 232
Cdd:cd05088 172 RGQEVYVKKTMGRLPvrWMAIESLNYSVYTT-----NSDVWSYGVLLWEIVSlGGTPY 224
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
114-291 7.39e-11

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 62.76  E-value: 7.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPPQvGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECrKVKLSDFGMTRRAGSPVKRVSGTIPY 193
Cdd:cd07878 105 DLNNIVKCQ-KLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAV-NEDC-ELRILDFGLARQADDEMTGYVATRWY 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 194 TAPELCDTSKHdgfcVDYSTDVWAFGVLLFCMLTGnfpweKAM-PSDTFYEEFVRWQKRRTGAVPSQWRRFTDESLR--- 269
Cdd:cd07878 182 RAPEIMLNWMH----YNQTVDIWSVGCIMAELLKG-----KALfPGNDYIDQLKRIMEVVGTPSPEVLKKISSEHARkyi 252
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75570321 270 -------------MFR-----------KLLALEQERRCSVKEVFAH 291
Cdd:cd07878 253 qslphmpqqdlkkIFRganplaidlleKMLVLDSDKRISASEALAH 298
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
32-291 7.70e-11

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: 62.88  E-value: 7.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKK---STKLKSFLREYSIsLYLSPCPFIINMFGIAFET------DEY 102
Cdd:cd07859   2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVfehVSDATRILREIKL-LRLLRHPDIVEIKHIMLPPsrrefkDIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 103 YVFaqEYAPSgDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECrKVKLSDFGMTRRAGS 182
Cdd:cd07859  81 VVF--ELMES-DLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILA-NADC-KLKICDFGLARVAFN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 183 PVKRVS------GTIPYTAPELCDTskhdgFCVDYST--DVWAFGVLLFCMLTGN--FPWEKAM-------------PSD 239
Cdd:cd07859 156 DTPTAIfwtdyvATRWYRAPELCGS-----FFSKYTPaiDIWSIGCIFAEVLTGKplFPGKNVVhqldlitdllgtpSPE 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75570321 240 TFYEefVRWQK--------RRTGAVP-SQWRRFTDE-SLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07859 231 TISR--VRNEKarrylssmRKKQPVPfSQKFPNADPlALRLLERLLAFDPKDRPTAEEALAD 290
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
32-226 8.14e-11

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: 62.36  E-value: 8.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLK----SFLREYSISLYLSPC--PFIINMFGIAF------ET 99
Cdd:cd07862   3 YECVAEIGEGAYGKVFKARDLKNGGRFVALKRVRVQTGEEgmplSTIREVAVLRHLETFehPNVVRLFDVCTvsrtdrET 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 100 DEYYVFAQEYAPSGDLFDIIPpQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR- 178
Cdd:cd07862  83 KLTLVFEHVDQDLTTYLDKVP-EPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILV--TSSGQIKLADFGLARi 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75570321 179 -RAGSPVKRVSGTIPYTAPELCDTSKhdgfcvdYST--DVWAFGVLLFCML 226
Cdd:cd07862 160 ySFQMALTSVVVTLWYRAPEVLLQSS-------YATpvDLWSVGCIFAEMF 203
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
30-291 8.62e-11

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: 61.85  E-value: 8.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  30 KYYEVIRELGKGTYGKVdlviHKIRGSKMAL------KFLKKKSTKLKSFLREYSISLYLSPCPFIINMFG--IAFETDE 101
Cdd:cd14131   1 KPYEILKQLGKGGSSKV----YKVLNPKKKIyalkrvDLEGADEQTLQSYKNEIELLKKLKGSDRIIQLYDyeVTDEDDY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 102 YYVfAQEYApSGDLFDIIppQVGLPEPVAKRCVH----QVAIALEYLHSKKLVHRDIKPENILIFDKecrKVKLSDFGMT 177
Cdd:cd14131  77 LYM-VMECG-EIDLATIL--KKKRPKPIDPNFIRyywkQMLEAVHTIHEEGIVHSDLKPANFLLVKG---RLKLIDFGIA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 178 RRAGS---PVKRVS--GTIPYTAPELC---DTSKHDGFC--VDYSTDVWAFGVLLFCMLTGNFPwekampsdtfyeeFVR 247
Cdd:cd14131 150 KAIQNdttSIVRDSqvGTLNYMSPEAIkdtSASGEGKPKskIGRPSDVWSLGCILYQMVYGKTP-------------FQH 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 75570321 248 WQK--RRTGAVPS-----QWRRFTDESL-RMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14131 217 ITNpiAKLQAIIDpnheiEFPDIPNPDLiDVMKRCLQRDPKKRPSIPELLNH 268
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
108-232 9.12e-11

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: 61.97  E-value: 9.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDII----PPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAGS- 182
Cdd:cd08228  82 ELADAGDLSQMIkyfkKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFI--TATGVVKLGDLGLGRFFSSk 159
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 75570321 183 --PVKRVSGTIPYTAPELCdtsKHDGFcvDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd08228 160 ttAAHSLVGTPYYMSPERI---HENGY--NFKSDIWSLGCLLYEMAALQSPF 206
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
126-244 9.63e-11

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 62.03  E-value: 9.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 126 PEPVAK--RCVHQVAIALEYLHS-KKLVHRDIKPENILIF-DKECrkVKLSDFGMTRR-------AGSPVKRVSGTIPYT 194
Cdd:cd14001 106 PFPAATilKVALSIARALEYLHNeKKILHGDIKSGNVLIKgDFES--VKLCDFGVSLPltenlevDSDPKAQYVGTEPWK 183
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 75570321 195 APELCDtskhDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYEE 244
Cdd:cd14001 184 AKEALE----EGGVITDKADIFAYGLVLWEMMTLSVPHLNLLDIEDDDED 229
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
86-239 9.68e-11

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: 62.39  E-value: 9.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  86 CPFIINMfGIAFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKE 165
Cdd:cd05633  67 CPFIVCM-TYAFHTPDKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL--DE 143
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 166 CRKVKLSDFGMTRRAGSPVKRVS-GTIPYTAPELCdtskHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSD 239
Cdd:cd05633 144 HGHVRISDLGLACDFSKKKPHASvGTHGYMAPEVL----QKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKD 214
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
38-231 9.94e-11

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: 61.74  E-value: 9.94e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSfLREYSISLYLSPcPFIINMFGIAFETDEYYvFAQEYAPSGDLFD 117
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSF-LKEVKLMRRLSH-PNILRFIGVCVKDNKLN-FITEYVNGGTLEE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 118 IIP-PQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI-FDKECRKVKLSDFGMTR-----RAGSPVKRVSGT 190
Cdd:cd14065  78 LLKsMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVrEANRGRNAVVADFGLARempdeKTKKPDRKKRLT 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 75570321 191 I---PY-TAPELCDTSKHDGfcvdySTDVWAFGVLLfCMLTGNFP 231
Cdd:cd14065 158 VvgsPYwMAPEMLRGESYDE-----KVDVFSFGIVL-CEIIGRVP 196
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
38-223 1.08e-10

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


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 61.67  E-value: 1.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIAFETDEYYVFAqEYAPSGDLFD 117
Cdd:cd05052  14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEEFLKEAAVMKEIKH-PNLVQLLGVCTREPPFYIIT-EFMPYGNLLD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 118 II--PPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR---------RAGS--PV 184
Cdd:cd05052  92 YLreCNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLV--GENHLVKVADFGLSRlmtgdtytaHAGAkfPI 169
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 75570321 185 KrvsgtipYTAPElcdTSKHDGFCVdySTDVWAFGVLLF 223
Cdd:cd05052 170 K-------WTAPE---SLAYNKFSI--KSDVWAFGVLLW 196
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
104-291 1.09e-10

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


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 61.66  E-value: 1.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 104 VFAQEYAPSGDL------FDIIPPQVglpepvAKRCVHQVAIALEYLHSKK--LVHRDIKPENILIfDKECRKVKLSDFG 175
Cdd:cd14031  89 VLVTELMTSGTLktylkrFKVMKPKV------LRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFI-TGPTGSVKIGDLG 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 176 M-TRRAGSPVKRVSGTIPYTAPELCDTSkhdgfcVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYeefvrwQKRRTG 254
Cdd:cd14031 162 LaTLMRTSFAKSVIGTPEFMAPEMYEEH------YDESVDVYAFGMCMLEMATSEYPYSECQNAAQIY------RKVTSG 229
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 75570321 255 AVPSQWRRFTDESLR-MFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14031 230 IKPASFNKVTDPEVKeIIEGCIRQNKSERLSIKDLLNH 267
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
38-228 1.14e-10

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: 61.75  E-value: 1.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSF-LREYSISLYLSPcPFIINMFGIAFEtDEYYVFAQEYAPSGDLF 116
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGEVMVMKELIRFDEEAQRNfLKEVKVMRSLDH-PNVLKFIGVLYK-DKKLNLITEYIPGGTLK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 117 DII-PPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR----------------- 178
Cdd:cd14154  79 DVLkDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLV--REDKTVVVADFGLARliveerlpsgnmspset 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 179 --RAGSPVKR----VSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLfCMLTG 228
Cdd:cd14154 157 lrHLKSPDRKkrytVVGNPYWMAPEMLNGRSY-----DEKVDIFSFGIVL-CEIIG 206
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
89-232 1.16e-10

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: 61.71  E-value: 1.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFETDEYY-VFaqEYAPSGDL----------------FDIIPPQVGLPEPVAkrCVHQVAIALEYLHSKKLVH 151
Cdd:cd05049  70 IVKFYGVCTEGDPLLmVF--EYMEHGDLnkflrshgpdaaflasEDSAPGELTLSQLLH--IAVQIASGMVYLASQHFVH 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 152 RDIKPENILIFDKECrkVKLSDFGMTRRAGSP-VKRVSGT----IPYTAPElcdTSKHDGFCVDysTDVWAFGVLLFCML 226
Cdd:cd05049 146 RDLATRNCLVGTNLV--VKIGDFGMSRDIYSTdYYRVGGHtmlpIRWMPPE---SILYRKFTTE--SDVWSFGVVLWEIF 218

                ....*..
gi 75570321 227 T-GNFPW 232
Cdd:cd05049 219 TyGKQPW 225
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
135-292 1.18e-10

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 62.73  E-value: 1.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 135 HQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR---RAGSPVKRVSGTIP--YTAPElcdtSKHDGFcv 209
Cdd:cd05105 244 YQVARGMEFLASKNCVHRDLAARNVLL--AQGKIVKICDFGLARdimHDSNYVSKGSTFLPvkWMAPE----SIFDNL-- 315
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 210 dYST--DVWAFGVLLFCMLT-GNFPWEKAMPSDTFYeefvrwQKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSvk 286
Cdd:cd05105 316 -YTTlsDVWSYGILLWEIFSlGGTPYPGMIVDSTFY------NKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPS-- 386

                ....*.
gi 75570321 287 evFAHL 292
Cdd:cd05105 387 --FLHL 390
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
135-247 1.20e-10

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta 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: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 62.72  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 135 HQVAIALEYLHSKKLVHRDIKPENILIFdkECRKVKLSDFGMTR---RAGSPVKRVSGTIP--YTAPELCdtskhdgFCV 209
Cdd:cd05107 246 YQVANGMEFLASKNCVHRDLAARNVLIC--EGKLVKICDFGLARdimRDSNYISKGSTFLPlkWMAPESI-------FNN 316
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 75570321 210 DYST--DVWAFGVLLFCMLT-GNFPWEKAMPSDTFYEEFVR 247
Cdd:cd05107 317 LYTTlsDVWSFGILLWEIFTlGGTPYPELPMNEQFYNAIKR 357
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
32-230 1.20e-10

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: 61.29  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKirgskmalkflKKKSTKLKSFLREYSISlYLSPC-----------------PFIINmFG 94
Cdd:cd08222   2 YRVVRKLGSGNFGTVYLVSDL-----------KATADEELKVLKEISVG-ELQPDetvdanreakllskldhPAIVK-FH 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  95 IAFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRCVH----QVAIALEYLHSKKLVHRDIKPENilIFDKEcRKVK 170
Cdd:cd08222  69 DSFVEKESFCIVTEYCEGGDLDDKISEYKKSGTTIDENQILdwfiQLLLAVQYMHERRILHRDLKAKN--IFLKN-NVIK 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 171 LSDFGMTR-RAGSP--VKRVSGTIPYTAPELCdtsKHDGFcvDYSTDVWAFGVLLF--CMLTGNF 230
Cdd:cd08222 146 VGDFGISRiLMGTSdlATTFTGTPYYMSPEVL---KHEGY--NSKSDIWSLGCILYemCCLKHAF 205
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
129-220 1.23e-10

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: 61.98  E-value: 1.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 129 VAKRCVHQVAIA---------LEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAgSPVKRVSGTIPYTAPELC 199
Cdd:cd06633 113 VHKKPLQEVEIAaithgalqgLAYLHSHNMIHRDIKAGNILL--TEPGQVKLADFGSASIA-SPANSFVGTPYWMAPEVI 189
                        90       100
                ....*....|....*....|....
gi 75570321 200 ---DTSKHDGfcvdySTDVWAFGV 220
Cdd:cd06633 190 lamDEGQYDG-----KVDIWSLGI 208
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
89-291 1.30e-10

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


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 61.58  E-value: 1.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFETDEYYVfAQEYAPSGDLFDIIPPQVGLPEPVAKRCVhQVAIALEYLHSKKLVHRDIKPENILIFDKEcrK 168
Cdd:cd06657  79 VVEMYNSYLVGDELWV-VMEFLEGGALTDIVTHTRMNEEQIAAVCL-AVLKALSVLHAQGVIHRDIKSDSILLTHDG--R 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 169 VKLSDFGMTRRAGSPVKR---VSGTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWekampsdtFYEEF 245
Cdd:cd06657 155 VKLSDFGFCAQVSKEVPRrksLVGTPYWMAPELISRLPYGP-----EVDIWSLGIMVIEMVDGEPPY--------FNEPP 221
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 75570321 246 VRWQKRRTGAVPSQWRRF--TDESLRMF-RKLLALEQERRCSVKEVFAH 291
Cdd:cd06657 222 LKAMKMIRDNLPPKLKNLhkVSPSLKGFlDRLLVRDPAQRATAAELLKH 270
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
129-291 1.43e-10

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: 61.17  E-value: 1.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 129 VAKRCVHQVAIALEYLHSK--KLVHRDIKPENILIfDKECRKVKLSDFGM-TRRAGSPVKRVSGTIPYTAPELCDTSkhd 205
Cdd:cd14033 105 LLQRWSRQILKGLHFLHSRcpPILHRDLKCDNIFI-TGPTGSVKIGDLGLaTLKRASFAKSVIGTPEFMAPEMYEEK--- 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 206 gfcVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYeefvrwQKRRTGAVPSQWRRFTDESLR-MFRKLLALEQERRCS 284
Cdd:cd14033 181 ---YDEAVDVYAFGMCILEMATSEYPYSECQNAAQIY------RKVTSGIKPDSFYKVKVPELKeIIEGCIRTDKDERFT 251

                ....*..
gi 75570321 285 VKEVFAH 291
Cdd:cd14033 252 IQDLLEH 258
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
124-228 1.49e-10

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: 61.79  E-value: 1.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 124 GLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGmtrrAGSPVkrvsGTIPYT--------A 195
Cdd:cd14210 112 GLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSSIKVIDFG----SSCFE----GEKVYTyiqsrfyrA 183
                        90       100       110
                ....*....|....*....|....*....|....*
gi 75570321 196 PELCdtskhdgFCVDYST--DVWAFGVLLFCMLTG 228
Cdd:cd14210 184 PEVI-------LGLPYDTaiDMWSLGCILAELYTG 211
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
125-228 1.68e-10

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 62.36  E-value: 1.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  125 LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRKVKLSDFGMTRRAGSPVKRVSGTIP--YTAPELCDTS 202
Cdd:PTZ00036 167 LPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLI-DPNTHTLKLCDFGSAKNLLAGQRSVSYICSrfYRAPELMLGA 245
                         90       100
                 ....*....|....*....|....*...
gi 75570321  203 khdgfcVDYST--DVWAFGVLLFCMLTG 228
Cdd:PTZ00036 246 ------TNYTThiDLWSLGCIIAEMILG 267
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
134-291 1.93e-10

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: 61.51  E-value: 1.93e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 134 VHQVAIALEYLHSKKLVHRDIKPENILIfDKECrKVKLSDFGMTRRAGSPVKRVSGTIPYTAPELCDTSKHdgfcVDYST 213
Cdd:cd07880 124 VYQMLKGLKYIHAAGIIHRDLKPGNLAV-NEDC-ELKILDFGLARQTDSEMTGYVVTRWYRAPEVILNWMH----YTQTV 197
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 214 DVWAFGVLLFCMLTGNFPWEKAMPSDTFYE----------EFV----------------RWQKRRTGAVpsqWRRFTDES 267
Cdd:cd07880 198 DIWSVGCIMAEMLTGKPLFKGHDHLDQLMEimkvtgtpskEFVqklqsedaknyvkklpRFRKKDFRSL---LPNANPLA 274
                       170       180
                ....*....|....*....|....
gi 75570321 268 LRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07880 275 VNVLEKMLVLDAESRITAAEALAH 298
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
32-230 2.13e-10

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


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 61.22  E-value: 2.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIR---GSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIAFETDEYYVFAQE 108
Cdd:cd13981   2 YVISKELGEGGYASVYLAKDDDEqsdGSLVALKVEKPPSIWEFYICDQLHSRLKNSRLRESISGAHSAHLFQDESILVMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 109 YAPSGDLFDII-----PPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEC-------------RKVK 170
Cdd:cd13981  82 YSSQGTLLDVVnkmknKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLRLEICadwpgegengwlsKGLK 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 171 LSDFGmtrRA--------GSPVKRVSGTIPYTAPELcdtskHDGFCVDYSTDVWAFGVLLFCMLTGNF 230
Cdd:cd13981 162 LIDFG---RSidmslfpkNQSFKADWHTDSFDCIEM-----REGRPWTYQIDYFGIAATIHVMLFGKY 221
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
32-231 2.14e-10

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: 61.13  E-value: 2.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLK--SFLREYSISLYLSPCPfIINMFGIaFETDEYYVFAQEY 109
Cdd:cd07870   2 YLNLEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVpfTAIREASLLKGLKHAN-IVLLHDI-IHTKETLTFVFEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 110 APSgDLFDIIPPQVGLPEPVAKRC-VHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAGSPVKRVS 188
Cdd:cd07870  80 MHT-DLAQYMIQHPGGLHPYNVRLfMFQLLRGLAYIHGQHILHRDLKPQNLLI--SYLGELKLADFGLARAKSIPSQTYS 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 75570321 189 G---TIPYTAPELCDTSkhdgfcVDYST--DVWAFGVLLFCMLTGN--FP 231
Cdd:cd07870 157 SevvTLWYRPPDVLLGA------TDYSSalDIWGAGCIFIEMLQGQpaFP 200
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
131-230 2.21e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 62.02  E-value: 2.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  131 KRCVHQVAIALEYLHSKKLVHRDIKPENILIfdkECR-KVKLSDFGMTRRAGSPvkRVS------GTIPYTAPELCdtsK 203
Cdd:PHA03210 270 RAIMKQLLCAVEYIHDKKLIHRDIKLENIFL---NCDgKIVLGDFGTAMPFEKE--REAfdygwvGTVATNSPEIL---A 341
                         90       100
                 ....*....|....*....|....*..
gi 75570321  204 HDGFCvdYSTDVWAFGVLLFCMLTGNF 230
Cdd:PHA03210 342 GDGYC--EITDIWSCGLILLDMLSHDF 366
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
136-293 2.37e-10

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 61.15  E-value: 2.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTR---RAGSPVKRVSGTIP--YTAPELCdtskhdgFCVD 210
Cdd:cd05103 187 QVAKGMEFLASRKCIHRDLAARNILLSENNV--VKICDFGLARdiyKDPDYVRKGDARLPlkWMAPETI-------FDRV 257
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 211 YST--DVWAFGVLLFCMLT-GNFPWekamPSDTFYEEFVRWQKRRTgavpsQWRRFTDESLRMFRKLLAL---EQERRCS 284
Cdd:cd05103 258 YTIqsDVWSFGVLLWEIFSlGASPY----PGVKIDEEFCRRLKEGT-----RMRAPDYTTPEMYQTMLDCwhgEPSQRPT 328

                ....*....
gi 75570321 285 VKEVFAHLG 293
Cdd:cd05103 329 FSELVEHLG 337
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
34-223 2.51e-10

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: 60.75  E-value: 2.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  34 VIRELGKGTYGKVDLVIHK--IRG---SKMALKFLKKKSTKLKSF--LREYSISLYLSpCPFIINMFGIAFETDEYYVfA 106
Cdd:cd05061  10 LLRELGQGSFGMVYEGNARdiIKGeaeTRVAVKTVNESASLRERIefLNEASVMKGFT-CHHVVRLLGVVSKGQPTLV-V 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 107 QEYAPSGDLFDII---------PPqvGLPEPVAKRCVH---QVAIALEYLHSKKLVHRDIKPENILIFDKecRKVKLSDF 174
Cdd:cd05061  88 MELMAHGDLKSYLrslrpeaenNP--GRPPPTLQEMIQmaaEIADGMAYLNAKKFVHRDLAARNCMVAHD--FTVKIGDF 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75570321 175 GMTR--------RAGSpvkrvSGTIP--YTAPElcdtSKHDGFCVDYStDVWAFGVLLF 223
Cdd:cd05061 164 GMTRdiyetdyyRKGG-----KGLLPvrWMAPE----SLKDGVFTTSS-DMWSFGVVLW 212
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
33-232 2.61e-10

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: 60.29  E-value: 2.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  33 EVIRELGKGTYGKVDLVIHKiRGSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIAfeTDEYYVFAQEYAPS 112
Cdd:cd05067  10 KLVERLGAGQFGEVWMGYYN-GHTKVAIKSLKQGSMSPDAFLAEANLMKQLQH-QRLVRLYAVV--TQEPIYIITEYMEN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 113 GDLFDIIPPQVGLPEPVAK--RCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTR---------RAG 181
Cdd:cd05067  86 GSLVDFLKTPSGIKLTINKllDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLS--CKIADFGLARliedneytaREG 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75570321 182 S--PVKrvsgtipYTAPElcdtskhdgfCVDYST-----DVWAFGVLLFCMLT-GNFPW 232
Cdd:cd05067 164 AkfPIK-------WTAPE----------AINYGTftiksDVWSFGILLTEIVThGRIPY 205
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
27-291 2.68e-10

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: 60.85  E-value: 2.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  27 EVNKYyEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKL---KSFLREYSIsLYLSPCPFIINMFGIA------- 96
Cdd:cd07865  10 EVSKY-EKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMENEKEgfpITALREIKI-LQLLKHENVVNLIEICrtkatpy 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  97 --FETDEYYVFA-QEYAPSGDLFDiipPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKEcRKVKLSD 173
Cdd:cd07865  88 nrYKGSIYLVFEfCEHDLAGLLSN---KNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILI-TKD-GVLKLAD 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 174 FGMTR-----RAGSPVK---RVSgTIPYTAPELCDTSKHDGFCVdystDVWAFGVLLFCMltgnfpWEKA--MPSDT--- 240
Cdd:cd07865 163 FGLARafslaKNSQPNRytnRVV-TLWYRPPELLLGERDYGPPI----DMWGAGCIMAEM------WTRSpiMQGNTeqh 231
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 241 ---------------FYEEFVRWQKRRTGAVPSQWRRFTDESLRMF----------RKLLALEQERRCSVKEVFAH 291
Cdd:cd07865 232 qltlisqlcgsitpeVWPGVDKLELFKKMELPQGQKRKVKERLKPYvkdpyaldliDKLLVLDPAKRIDADTALNH 307
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
136-244 2.89e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 61.05  E-value: 2.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  136 QVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRragSPVKR-----VSGTIPYTAPELCDTSKHDGfcvd 210
Cdd:PHA03209 165 QILEGLRYLHAQRIIHRDVKTENIFINDVD--QVCIGDLGAAQ---FPVVApaflgLAGTVETNAPEVLARDKYNS---- 235
                         90       100       110
                 ....*....|....*....|....*....|....
gi 75570321  211 ySTDVWAFGVLLFCMLtgnfpwekAMPSDTFYEE 244
Cdd:PHA03209 236 -KADIWSAGIVLFEML--------AYPSTIFEDP 260
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
98-291 3.43e-10

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: 60.27  E-value: 3.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  98 ETDEYYVFAQ-EYAPSGDLFDIIPPQVGLPEPVAKRCVH---QVAIALEYLHSKKLVHRDIKPENILiFDKEcRKVKLSD 173
Cdd:cd14048  84 KMDEVYLYIQmQLCRKENLKDWMNRRCTMESRELFVCLNifkQIASAVEYLHSKGLIHRDLKPSNVF-FSLD-DVVKVGD 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 174 FGMTRRA--GSPVKRVS-------------GTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLtgnFPWEKAMps 238
Cdd:cd14048 162 FGLVTAMdqGEPEQTVLtpmpayakhtgqvGTRLYMSPEQIHGNQY-----SEKVDIFALGLILFELI---YSFSTQM-- 231
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 75570321 239 dtfyEEFVRWQKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14048 232 ----ERIRTLTDVRKLKFPALFTNKYPEERDMVQQMLSPSPSERPEAHEVIEH 280
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
136-253 4.12e-10

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR 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: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 60.20  E-value: 4.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTR---RAGSPVKRVSGTIP--YTAPElcdtSKHDGFCVD 210
Cdd:cd05054 146 QVARGMEFLASRKCIHRDLAARNILLSENNV--VKICDFGLARdiyKDPDYVRKGDARLPlkWMAPE----SIFDKVYTT 219
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 75570321 211 YStDVWAFGVLLF-CMLTGNFPWekamPSDTFYEEFVRWQKRRT 253
Cdd:cd05054 220 QS-DVWSFGVLLWeIFSLGASPY----PGVQMDEEFCRRLKEGT 258
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
136-232 4.55e-10

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: 59.73  E-value: 4.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTR----------RAGS--PVKrvsgtipYTAPELCDTSK 203
Cdd:cd05068 112 QVASGMAYLESQNYIHRDLAARNVLVGENNI--CKVADFGLARvikvedeyeaREGAkfPIK-------WTAPEAANYNR 182
                        90       100       110
                ....*....|....*....|....*....|
gi 75570321 204 hdgFCVdySTDVWAFGVLLFCMLT-GNFPW 232
Cdd:cd05068 183 ---FSI--KSDVWSFGILLTEIVTyGRIPY 207
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
104-291 5.63e-10

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: 59.71  E-value: 5.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 104 VFAQEYAPSGDL------FDIIPPQVglpepvAKRCVHQVAIALEYLHSKK--LVHRDIKPENILIfDKECRKVKLSDFG 175
Cdd:cd14032  80 VLVTELMTSGTLktylkrFKVMKPKV------LRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFI-TGPTGSVKIGDLG 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 176 M-TRRAGSPVKRVSGTIPYTAPELCDTSkhdgfcVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYeefvrwQKRRTG 254
Cdd:cd14032 153 LaTLKRASFAKSVIGTPEFMAPEMYEEH------YDESVDVYAFGMCMLEMATSEYPYSECQNAAQIY------RKVTCG 220
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 75570321 255 AVPSQWRRFTDESLR-MFRKLLALEQERRCSVKEVFAH 291
Cdd:cd14032 221 IKPASFEKVTDPEIKeIIGECICKNKEERYEIKDLLSH 258
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
140-260 6.82e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 60.01  E-value: 6.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  140 ALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMtrrAGSPVKRV-------SGTIPYTAPELCDTSKHDGfcvdyS 212
Cdd:PHA03212 194 AIQYLHENRIIHRDIKAENIFI--NHPGDVCLGDFGA---ACFPVDINankyygwAGTIATNAPELLARDPYGP-----A 263
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 75570321  213 TDVWAFGVLLFCMLTG-NFPWEK-AMPSDTFYEEFVRWQKRRTGAVPSQW 260
Cdd:PHA03212 264 VDIWSAGIVLFEMATChDSLFEKdGLDGDCDSDRQIKLIIRRSGTHPNEF 313
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
129-220 7.08e-10

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: 59.00  E-value: 7.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 129 VAKRCVHQVAIA---------LEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAgSPVKRVSGTIPYTAPELC 199
Cdd:cd06607  93 VHKKPLQEVEIAaichgalqgLAYLHSHNRIHRDVKAGNILL--TEPGTVKLADFGSASLV-CPANSFVGTPYWMAPEVI 169
                        90       100
                ....*....|....*....|....
gi 75570321 200 ---DTSKHDGfcvdySTDVWAFGV 220
Cdd:cd06607 170 lamDEGQYDG-----KVDVWSLGI 188
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
35-233 8.36e-10

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


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 59.00  E-value: 8.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  35 IRELGKGTYGKVDLviHKIRGS-KMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIAFETDEYYVfAQEYAPSG 113
Cdd:cd05059   9 LKELGSGQFGVVHL--GKWRGKiDVAIKMIKEGSMSEDDFIEEAKVMMKLSH-PKLVQLYGVCTKQRPIFI-VTEYMANG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPPQVGL--PEPVAKRCVhQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTR---------RAGS 182
Cdd:cd05059  85 CLLNYLRERRGKfqTEQLLEMCK-DVCEAMEYLESNGFIHRDLAARNCLVGEQNV--VKVSDFGLARyvlddeytsSVGT 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 183 --PVKrvsgtipYTAPELCDTSKhdgfcvdYS--TDVWAFGVLLFCMLT-GNFPWE 233
Cdd:cd05059 162 kfPVK-------WSPPEVFMYSK-------FSskSDVWSFGVLMWEVFSeGKMPYE 203
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
31-222 8.62e-10

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: 59.34  E-value: 8.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  31 YYEVIRELGKGTYGKVDLVIHKIR--GSKMALKFLK---KKSTKLKSFLREYSISLYLSPCPFIINMFG--IAFET--DE 101
Cdd:cd07857   1 RYELIKELGQGAYGIVCSARNAETseEETVAIKKITnvfSKKILAKRALRELKLLRHFRGHKNITCLYDmdIVFPGnfNE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 102 YYVFAQ--EYapsgDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECrKVKLSDFGMTRR 179
Cdd:cd07857  81 LYLYEElmEA----DLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLV-NADC-ELKICDFGLARG 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 75570321 180 AGSPVKRVSG-------TIPYTAPELCDTSKhdgfcvDYST--DVWAFGVLL 222
Cdd:cd07857 155 FSENPGENAGfmteyvaTRWYRAPEIMLSFQ------SYTKaiDVWSVGCIL 200
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
114-291 8.97e-10

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: 59.76  E-value: 8.97e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAgSPVKRVSGTIP- 192
Cdd:cd07853  89 DLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLV-NSNCV-LKICDFGLARVE-EPDESKHMTQEv 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 193 ----YTAPELCDTSKHdgfcvdYST--DVWAFGVLLFCMLTGNFPWEKAMP----------------SDTFY--EEFVRW 248
Cdd:cd07853 166 vtqyYRAPEILMGSRH------YTSavDIWSVGCIFAELLGRRILFQAQSPiqqldlitdllgtpslEAMRSacEGARAH 239
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 75570321 249 QKRRTGAVPSQWRRF------TDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07853 240 ILRGPHKPPSLPVLYtlssqaTHEAVHLLCRMLVFDPDKRISAADALAH 288
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
36-276 9.48e-10

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, 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, like BMPR1a, 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 BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 58.90  E-value: 9.48e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  36 RELGKGTYGKVDLviHKIRGSKMALKFLKKKSTKL---------KSFLREYSISLYLSPcpfiiNMFGIAFETDEYYVfa 106
Cdd:cd14220   1 RQIGKGRYGEVWM--GKWRGEKVAVKVFFTTEEASwfreteiyqTVLMRHENILGFIAA-----DIKGTGSWTQLYLI-- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 107 QEYAPSGDLFDIIPPQVgLPEPVAKRCVHQVAIALEYLHSK--------KLVHRDIKPENILIfdKECRKVKLSDFGMTR 178
Cdd:cd14220  72 TDYHENGSLYDFLKCTT-LDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILI--KKNGTCCIADLGLAV 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 179 RAGS-------PVKRVSGTIPYTAPELCDTS-KHDGFCVDYSTDVWAFGVLLFCM----LTG------NFPWEKAMPSDT 240
Cdd:cd14220 149 KFNSdtnevdvPLNTRVGTKRYMAPEVLDESlNKNHFQAYIMADIYSFGLIIWEMarrcVTGgiveeyQLPYYDMVPSDP 228
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 75570321 241 FYEEF--VRWQKRRTGAVPSQWRrfTDESLRMFRKLLA 276
Cdd:cd14220 229 SYEDMreVVCVKRLRPTVSNRWN--SDECLRAVLKLMS 264
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
32-235 9.71e-10

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 60.52  E-value: 9.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321    32 YEVIRELGKGTYGKVDLVIHK------------IRGSKMALKFLKKKSTKLKSFLREYSISLYlspcpfiINMFgIAFET 99
Cdd:PTZ00266   15 YEVIKKIGNGRFGEVFLVKHKrtqeffcwkaisYRGLKEREKSQLVIEVNVMRELKHKNIVRY-------IDRF-LNKAN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   100 DEYYVFaQEYAPSGDLFDIIPPQVGLPEPVAKRCV----HQVAIALEYLHS-------KKLVHRDIKPENILIFD--KEC 166
Cdd:PTZ00266   87 QKLYIL-MEFCDAGDLSRNIQKCYKMFGKIEEHAIvditRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTgiRHI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321   167 RKV-------------KLSDFGMTRRAG--SPVKRVSGTIPYTAPELCdtsKHDGFCVDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:PTZ00266  166 GKItaqannlngrpiaKIGDFGLSKNIGieSMAHSCVGTPYYWSPELL---LHETKSYDDKSDMWALGCIIYELCSGKTP 242

                  ....
gi 75570321   232 WEKA 235
Cdd:PTZ00266  243 FHKA 246
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
99-241 1.25e-09

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: 57.97  E-value: 1.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  99 TDEYYVFAQeyAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRKVKL------- 171
Cdd:cd14024  57 QDRAYAFFS--RHYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLvnledsc 134
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75570321 172 ----SDFGMTRRAGSPVkrvsgtipYTAPELCdTSKHdgfcvDYS---TDVWAFGVLLFCMLTGNFPWEKAMPSDTF 241
Cdd:cd14024 135 plngDDDSLTDKHGCPA--------YVGPEIL-SSRR-----SYSgkaADVWSLGVCLYTMLLGRYPFQDTEPAALF 197
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
27-336 1.35e-09

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: 59.15  E-value: 1.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  27 EVNKYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPF-----IINMFGIAFETDE 101
Cdd:cd07879  12 ELPERYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHenvigLLDVFTSAVSGDE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 102 YYVFaqeYAPSGDLFDIIPPQVGLP--EPVAKRCVHQVAIALEYLHSKKLVHRDIKPENiLIFDKECrKVKLSDFGMTRR 179
Cdd:cd07879  92 FQDF---YLVMPYMQTDLQKIMGHPlsEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGN-LAVNEDC-ELKILDFGLARH 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 180 AGSPVKRVSGTIPYTAPELCDTSKHdgfcVDYSTDVWAFGVLLFCMLTGNFPWE--------------KAMPSDTFYEEF 245
Cdd:cd07879 167 ADAEMTGYVVTRWYRAPEVILNWMH----YNQTVDIWSVGCIMAEMLTGKTLFKgkdyldqltqilkvTGVPGPEFVQKL 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 246 -VRWQKRRTGAVPSQWR--------RFTDESLRMFRKLLALEQERRCSVKEVFAHLGHRWMLDGTSGNHHQSvLNSSSEE 316
Cdd:cd07879 243 eDKAAKSYIKSLPKYPRkdfstlfpKASPQAVDLLEKMLELDVDKRLTATEALEHPYFDSFRDADEETEQQP-YDDSLEN 321
                       330       340
                ....*....|....*....|
gi 75570321 317 DELLVDRMKQQTLSPTANTS 336
Cdd:cd07879 322 EKLSVDEWKKHIYKEVKSFS 341
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
87-231 1.59e-09

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: 58.25  E-value: 1.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVFAQEYAPSGDLFDIIPPQVGlpEPVAKRCVH---QVAIALEYLHSKKLVHRDIKPENILIfd 163
Cdd:cd05058  56 PNVLSLLGICLPSEGSPLVVLPYMKHGDLRNFIRSETH--NPTVKDLIGfglQVAKGMEYLASKKFVHRDLAARNCML-- 131
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 164 KECRKVKLSDFGMTR-----RAGSPVKRVSGTIP--YTAPELCDTSKhdgFCVdySTDVWAFGVLLFCMLTGNFP 231
Cdd:cd05058 132 DESFTVKVADFGLARdiydkEYYSVHNHTGAKLPvkWMALESLQTQK---FTT--KSDVWSFGVLLWELMTRGAP 201
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
38-228 1.61e-09

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: 58.04  E-value: 1.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSF-LREYSISLYLSPcPFIINMFGIAFEtDEYYVFAQEYAPSGDLF 116
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRTfLKEVKVMRCLEH-PNVLKFIGVLYK-DKRLNFITEYIKGGTLR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 117 DIIPpQVGLPEPVAKRC--VHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR-------------RAG 181
Cdd:cd14221  79 GIIK-SMDSHYPWSQRVsfAKDIASGMAYLHSMNIIHRDLNSHNCLV--RENKSVVVADFGLARlmvdektqpeglrSLK 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75570321 182 SPVKRVSGTI---PY-TAPELCdtskhDGFCVDYSTDVWAFGVLLfCMLTG 228
Cdd:cd14221 156 KPDRKKRYTVvgnPYwMAPEMI-----NGRSYDEKVDVFSFGIVL-CEIIG 200
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
75-232 1.87e-09

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: 58.14  E-value: 1.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  75 REYSISLYLSPcPFIINMFG-IAFETDEYYVFAqEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKK--LVH 151
Cdd:cd14040  59 REYRIHKELDH-PRIVKLYDyFSLDTDTFCTVL-EYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIH 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 152 RDIKPENILIFD-KECRKVKLSDFGMTRRAGSPVKRV---------SGTIPYTAPElCDTSKHDGFCVDYSTDVWAFGVL 221
Cdd:cd14040 137 YDLKPGNILLVDgTACGEIKITDFGLSKIMDDDSYGVdgmdltsqgAGTYWYLPPE-CFVVGKEPPKISNKVDVWSVGVI 215
                       170
                ....*....|.
gi 75570321 222 LFCMLTGNFPW 232
Cdd:cd14040 216 FFQCLYGRKPF 226
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
83-268 2.37e-09

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


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 57.75  E-value: 2.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  83 LSPC--PFIINMFGIAFETDEYYVFaQEYAPSGDLFDIIppQVG-LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENI 159
Cdd:cd06640  56 LSQCdsPYVTKYYGSYLKGTKLWII-MEYLGGGSALDLL--RAGpFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANV 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 160 LIfdKECRKVKLSDFGMT-RRAGSPVKRVS--GTIPYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGNFPWEKAM 236
Cdd:cd06640 133 LL--SEQGDVKLADFGVAgQLTDTQIKRNTfvGTPFWMAPEVIQQSAYDS-----KADIWSLGITAIELAKGEPPNSDMH 205
                       170       180       190
                ....*....|....*....|....*....|..
gi 75570321 237 PSDTFYEEFVRWQKRRTGAVPSQWRRFTDESL 268
Cdd:cd06640 206 PMRVLFLIPKNNPPTLVGDFSKPFKEFIDACL 237
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
141-233 2.64e-09

Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 porphyrin-binding domain [Signal transduction mechanisms];


Pssm-ID: 444462 [Multi-domain]  Cd Length: 466  Bit Score: 58.48  E-value: 2.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 141 LEYLHSKKLVHRDIKPENIlIFDKECRKVKLSDFGMTRRAGSPVKRVSGTI----PYTAPElcdtsKHDGfCVDYSTDVW 216
Cdd:COG5752 151 LQFIHSRNVIHRDIKPANI-IRRRSDGKLVLIDFGVAKLLTITALLQTGTIigtpEYMAPE-----QLRG-KVFPASDLY 223
                        90
                ....*....|....*..
gi 75570321 217 AFGVLLFCMLTGNFPWE 233
Cdd:COG5752 224 SLGVTCIYLLTGVSPFD 240
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
74-226 2.76e-09

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


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 57.64  E-value: 2.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  74 LREYSISLYLSPcPFIINMFGIAFETDEYYVFAqEYAPSGDL----------------FDIIPPQVGLPEPVAKRCVH-- 135
Cdd:cd05096  67 LKEVKILSRLKD-PNIIRLLGVCVDEDPLCMIT-EYMENGDLnqflsshhlddkeengNDAVPPAHCLPAISYSSLLHva 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 -QVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRR--AGSpVKRVSG----TIPYTAPELCDTSKhdgfc 208
Cdd:cd05096 145 lQIASGMKYLSSLNFVHRDLATRNCLV--GENLTIKIADFGMSRNlyAGD-YYRIQGravlPIRWMAWECILMGK----- 216
                       170
                ....*....|....*...
gi 75570321 209 VDYSTDVWAFGVLLFCML 226
Cdd:cd05096 217 FTTASDVWAFGVTLWEIL 234
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
134-231 2.80e-09

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: 57.97  E-value: 2.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 134 VHQVAIALEYLHSKKLVHRDIKPENILIfDKECrKVKLSDFGMTRRAGSPVKRVSGTIPYTAPELCDTSKHdgfcVDYST 213
Cdd:cd07856 114 LYQILRGLKYVHSAGVIHRDLKPSNILV-NENC-DLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQK----YDVEV 187
                        90       100
                ....*....|....*....|
gi 75570321 214 DVWAFGVLLFCMLTGN--FP 231
Cdd:cd07856 188 DIWSAGCIFAEMLEGKplFP 207
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
94-228 2.85e-09

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: 57.87  E-value: 2.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  94 GIAFETDEYYVfAQEYAPSgDLFDIIPpQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECRKVKLSD 173
Cdd:cd07854  83 GSLTELNSVYI-VQEYMET-DLANVLE-QGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFI-NTEDLVLKIGD 158
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75570321 174 FGMTR-------RAGSPVKRVSgTIPYTAPELCDTSKHdgfcVDYSTDVWAFGVLLFCMLTG 228
Cdd:cd07854 159 FGLARivdphysHKGYLSEGLV-TKWYRSPRLLLSPNN----YTKAIDMWAAGCIFAEMLTG 215
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
134-223 2.94e-09

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


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 57.72  E-value: 2.94e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 134 VHQVAIALEYLHSKKLVHRDIKPENILIFDKecRKVKLSDFGMTRR--AGSPVKRVSGT---IPYTAPELCDTSKhdgFC 208
Cdd:cd05091 131 VTQIAAGMEYLSSHHVVHKDLATRNVLVFDK--LNVKISDLGLFREvyAADYYKLMGNSllpIRWMSPEAIMYGK---FS 205
                        90
                ....*....|....*
gi 75570321 209 VDysTDVWAFGVLLF 223
Cdd:cd05091 206 ID--SDIWSYGVVLW 218
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
30-227 3.33e-09

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


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 57.21  E-value: 3.33e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  30 KYYEVIRELGKGTYGKVDLV----IHKIRGSKMALKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGIAFETDEY-YV 104
Cdd:cd05081   4 RHLKYISQLGKGNFGSVELCrydpLGDNTGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGRRsLR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 105 FAQEYAPSGDLFDIIPPQVGLPEPVAKRC-VHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTR----R 179
Cdd:cd05081  84 LVMEYLPSGCLRDFLQRHRARLDASRLLLySSQICKGMEYLGSRRCVHRDLAARNILVESEA--HVKIADFGLAKllplD 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75570321 180 AGSPVKRVSGTIP--YTAPE-LCDTskhdgfCVDYSTDVWAFGVLLFCMLT 227
Cdd:cd05081 162 KDYYVVREPGQSPifWYAPEsLSDN------IFSRQSDVWSFGVVLYELFT 206
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
128-231 3.46e-09

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: 57.44  E-value: 3.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 128 PVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRAGSPVKRVSG---TIPYTAPELCDTSKh 204
Cdd:cd07839  99 EIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNG--ELKLADFGLARAFGIPVRCYSAevvTLWYRPPDVLFGAK- 175
                        90       100
                ....*....|....*....|....*..
gi 75570321 205 dgfCVDYSTDVWAFGVLLFCMLTGNFP 231
Cdd:cd07839 176 ---LYSTSIDMWSAGCIFAELANAGRP 199
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
129-282 3.48e-09

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 57.13  E-value: 3.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 129 VAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrKVKLSDFG---------------MTRRAGSPVKRVSGTIPY 193
Cdd:cd14049 121 VTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDI-HVRIGDFGlacpdilqdgndsttMSRLNGLTHTSGVGTCLY 199
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 194 TAPELCDTSKHdgfcvDYSTDVWAFGVLLFcmltgnfpwEKAMPSDTFYEEFVRWQKRRTGAVPSQWRRFTDESLRMFRK 273
Cdd:cd14049 200 AAPEQLEGSHY-----DFKSDMYSIGVILL---------ELFQPFGTEMERAEVLTQLRNGQIPKSLCKRWPVQAKYIKL 265

                ....*....
gi 75570321 274 LLALEQERR 282
Cdd:cd14049 266 LTSTEPSER 274
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
135-220 3.63e-09

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: 57.37  E-value: 3.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 135 HQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAgSPVKRVSGTIPYTAPELC---DTSKHDGfcvdy 211
Cdd:cd06635 132 HGALQGLAYLHSHNMIHRDIKAGNILL--TEPGQVKLADFGSASIA-SPANSFVGTPYWMAPEVIlamDEGQYDG----- 203

                ....*....
gi 75570321 212 STDVWAFGV 220
Cdd:cd06635 204 KVDVWSLGI 212
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
136-227 3.67e-09

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


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 57.33  E-value: 3.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTR-----RAGSPVKRvSGTIP--YTAPELCDTSKhdgFC 208
Cdd:cd14205 116 QICKGMEYLGTKRYIHRDLATRNILV-ENENR-VKIGDFGLTKvlpqdKEYYKVKE-PGESPifWYAPESLTESK---FS 189
                        90
                ....*....|....*....
gi 75570321 209 VdySTDVWAFGVLLFCMLT 227
Cdd:cd14205 190 V--ASDVWSFGVVLYELFT 206
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
35-234 4.69e-09

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


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 56.79  E-value: 4.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  35 IRELGKGTYGKVDL---------VIHKIRGSKMALKFLkkkstklksfLREYSISLYLSPcPFIINMFGIAFETDEYYVf 105
Cdd:cd05114   9 MKELGSGLFGVVRLgkwraqykvAIKAIREGAMSEEDF----------IEEAKVMMKLTH-PKLVQLYGVCTQQKPIYI- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 106 AQEYAPSGDLFDIIPPQVG-LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTRR----- 179
Cdd:cd05114  77 VTEFMENGCLLNYLRQRRGkLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGV--VKVSDFGMTRYvlddq 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75570321 180 ------AGSPVKrvsgtipYTAPELCDTSKHDGfcvdySTDVWAFGVLLFCMLT-GNFPWEK 234
Cdd:cd05114 155 ytsssgAKFPVK-------WSPPEVFNYSKFSS-----KSDVWSFGVLMWEVFTeGKMPFES 204
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
140-290 4.90e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 57.55  E-value: 4.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  140 ALEYLHSKKLVHRDIKPENilIFDKECRKVKLSDFGMTRRAGSPVKRV-----SGTIPYTAPELcdtSKHDGFCVdySTD 214
Cdd:PHA03207 197 ALAYLHGRGIIHRDVKTEN--IFLDEPENAVLGDFGAACKLDAHPDTPqcygwSGTLETNSPEL---LALDPYCA--KTD 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  215 VWAFGVLLFCMLTGNFP-WEKAMPSD------------------------TFYEEFVRW--QKRRTGAVPSQWRRFTdes 267
Cdd:PHA03207 270 IWSAGLVLFEMSVKNVTlFGKQVKSSssqlrsiircmqvhplefpqngstNLCKHFKQYaiVLRPPYTIPPVIRKYG--- 346
                        170       180
                 ....*....|....*....|....*...
gi 75570321  268 LRM-----FRKLLALEQERRCSVKEVFA 290
Cdd:PHA03207 347 MHMdveylIAKMLTFDQEFRPSAQDILS 374
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
32-291 5.08e-09

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: 56.94  E-value: 5.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKL---KSFLREYSISLYLSPcPFIINMFGIAFETDE------- 101
Cdd:cd07866  10 YEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNEKDgfpITALREIKILKKLKH-PNVVPLIDMAVERPDkskrkrg 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 102 --YYVFA-QEYAPSGDLFDiipPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTR 178
Cdd:cd07866  89 svYMVTPyMDHDLSGLLEN---PSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQG--ILKIADFGLAR 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 179 ----------RAGSPVKR----VSGTIPYTAPELCDTSKHdgfcvdYST--DVWAFGVLLFCMLTGN------------- 229
Cdd:cd07866 164 pydgpppnpkGGGGGGTRkytnLVVTRWYRPPELLLGERR------YTTavDIWGIGCVFAEMFTRRpilqgksdidqlh 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75570321 230 --F-----PWEKAMPSDTFYE--EFVRWQKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07866 238 liFklcgtPTEETWPGWRSLPgcEGVHSFTNYPRTLEERFGKLGPEGLDLLSKLLSLDPYKRLTASDALEH 308
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
30-227 5.22e-09

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: 56.86  E-value: 5.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  30 KYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKS------TKLKSFLREYSI--SLYLSPcpfIINMFGIAFE-TD 100
Cdd:cd05079   4 RFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLkpesggNHIADLKKEIEIlrNLYHEN---IVKYKGICTEdGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 101 EYYVFAQEYAPSGDLFDIIP---PQVGLPEPVakRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMT 177
Cdd:cd05079  81 NGIKLIMEFLPSGSLKEYLPrnkNKINLKQQL--KYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH--QVKIGDFGLT 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75570321 178 R-----RAGSPVK-RVSGTIPYTAPELCDTSKhdgFCVdySTDVWAFGVLLFCMLT 227
Cdd:cd05079 157 KaietdKEYYTVKdDLDSPVFWYAPECLIQSK---FYI--ASDVWSFGVTLYELLT 207
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
131-250 5.34e-09

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


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 56.91  E-value: 5.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 131 KRCVHQVAI----ALEYLHSKKLVHRDIKPENILI-FDKECRKVKLSDFGMTRR----------AGSPVKRVSGTIPYTA 195
Cdd:cd14015 126 EKTVLQLALrildVLEYIHENGYVHADIKASNLLLgFGKNKDQVYLVDYGLASRycpngkhkeyKEDPRKAHNGTIEFTS 205
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 196 PELcdtskHDGFCVDYSTDvwaFGVLLFCM---LTGNFPWEKAMPSdtfyEEFVRWQK 250
Cdd:cd14015 206 RDA-----HKGVAPSRRGD---LEILGYNMlqwLCGKLPWEDNLKN----PEYVQKQK 251
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
87-232 5.58e-09

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: 56.96  E-value: 5.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVFAqEYAPSGDLFDII----PPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIf 162
Cdd:cd08229  84 PNVIKYYASFIEDNELNIVL-ELADAGDLSRMIkhfkKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFI- 161
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75570321 163 dKECRKVKLSDFGMTRRAGS---PVKRVSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLFCMLTGNFPW 232
Cdd:cd08229 162 -TATGVVKLGDLGLGRFFSSkttAAHSLVGTPYYMSPERIHENGY-----NFKSDIWSLGCLLYEMAALQSPF 228
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
114-231 5.61e-09

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: 56.92  E-value: 5.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPPQVgLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECrKVKLSDFGMTRRAGSPVKRVSGTIPY 193
Cdd:cd07851 105 DLNNIVKCQK-LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAV-NEDC-ELKILDFGLARHTDDEMTGYVATRWY 181
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 75570321 194 TAPELCDTSKHdgfcvdY--STDVWAFGVLLFCMLTGN--FP 231
Cdd:cd07851 182 RAPEIMLNWMH------YnqTVDIWSVGCIMAELLTGKtlFP 217
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
38-228 5.98e-09

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 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: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 56.49  E-value: 5.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSISLY--------LSPCPFIINmFGIAFETDEYyVFAQEY 109
Cdd:cd05078   7 LGQGTFTKIFKGIRREVGDYGQLHETEVLLKVLDKAHRNYSESFFeaasmmsqLSHKHLVLN-YGVCVCGDEN-ILVQEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 110 APSGDLFDIIPPQVGLPEPVAKRCV-HQVAIALEYLHSKKLVHRDIKPENILIFDKECRK------VKLSDFGMTRRAgS 182
Cdd:cd05078  85 VKFGSLDTYLKKNKNCINILWKLEVaKQLAWAMHFLEEKTLVHGNVCAKNILLIREEDRKtgnppfIKLSDPGISITV-L 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75570321 183 PVKRVSGTIPYTAPELCDTSKHdgfcVDYSTDVWAFGVLLFCMLTG 228
Cdd:cd05078 164 PKDILLERIPWVPPECIENPKN----LSLATDKWSFGTTLWEICSG 205
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
136-253 7.00e-09

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 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: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 56.91  E-value: 7.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR---RAGSPVKRVSGTIP--YTAPElcdtSKHDGFcvd 210
Cdd:cd05102 180 QVARGMEFLASRKCIHRDLAARNILL--SENNVVKICDFGLARdiyKDPDYVRKGSARLPlkWMAPE----SIFDKV--- 250
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 75570321 211 YST--DVWAFGVLLFCMLT-GNFPWekamPSDTFYEEFVRWQKRRT 253
Cdd:cd05102 251 YTTqsDVWSFGVLLWEIFSlGASPY----PGVQINEEFCQRLKDGT 292
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
136-223 7.07e-09

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 56.93  E-value: 7.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR---RAGSPVKRVSGTIP--YTAPElcdtSKHDGFcvd 210
Cdd:cd14207 188 QVARGMEFLSSRKCIHRDLAARNILL--SENNVVKICDFGLARdiyKNPDYVRKGDARLPlkWMAPE----SIFDKI--- 258
                        90
                ....*....|....*
gi 75570321 211 YST--DVWAFGVLLF 223
Cdd:cd14207 259 YSTksDVWSYGVLLW 273
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
75-238 8.24e-09

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: 56.00  E-value: 8.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  75 REYSISLYLSPcPFIINMFGIAFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAK-RCVHQVAIALEYLH--SKKLVH 151
Cdd:cd14064  40 REVSILCRLNH-PCVIQFVGACLDDPSQFAIVTQYVSGGSLFSLLHEQKRVIDLQSKlIIAVDVAKGMEYLHnlTQPIIH 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 152 RDIKPENILIFdkECRKVKLSDFGMTR----RAGSPVKRVSGTIPYTAPELCDTskhdgfCVDYS--TDVWAFGVLLFCM 225
Cdd:cd14064 119 RDLNSHNILLY--EDGHAVVADFGESRflqsLDEDNMTKQPGNLRWMAPEVFTQ------CTRYSikADVFSYALCLWEL 190
                       170
                ....*....|...
gi 75570321 226 LTGNFPWEKAMPS 238
Cdd:cd14064 191 LTGEIPFAHLKPA 203
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
131-228 1.01e-08

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


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 56.10  E-value: 1.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 131 KRCVHQVAIALEYLHSKKLVHRDIKPENIL-IFDKECrkVKLSDFGMTRRAGSPVKRVSGTIPYTAP--ELCDTSKHDGF 207
Cdd:cd14020 113 QHCARDVLEALAFLHHEGYVHADLKPRNILwSAEDEC--FKLIDFGLSFKEGNQDVKYIQTDGYRAPeaELQNCLAQAGL 190
                        90       100
                ....*....|....*....|....*
gi 75570321 208 CVD----YSTDVWAFGVLLFCMLTG 228
Cdd:cd14020 191 QSEtectSAVDLWSLGIVLLEMFSG 215
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
140-291 1.01e-08

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: 55.39  E-value: 1.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 140 ALEYLHSKKLVHRDIKPENILI-FDKECrkvKLSDFGMT---RRAGspVKRVS-GTIPYTAPELCDTSkhdgfcVDYSTD 214
Cdd:cd14050 112 GLKHLHDHGLIHLDIKPANIFLsKDGVC---KLGDFGLVvelDKED--IHDAQeGDPRYMAPELLQGS------FTKAAD 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 215 VWAFGVLLFcMLTGNFPWEKAMPSdtfyeefvrWQKRRTGAVPSqwrRFTDESLRMFRKLLAL----EQERRCSVKEVFA 290
Cdd:cd14050 181 IFSLGITIL-ELACNLELPSGGDG---------WHQLRQGYLPE---EFTAGLSPELRSIIKLmmdpDPERRPTAEDLLA 247

                .
gi 75570321 291 H 291
Cdd:cd14050 248 L 248
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
32-228 1.29e-08

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: 55.85  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLK--SFLREYSISLYLSPCPFIinMFGIAFETDEYYVFAQEY 109
Cdd:cd07869   7 YEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTpfTAIREASLLKGLKHANIV--LLHDIIHTKETLTLVFEY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 110 APSgDLFDIIPPQVGLPEP-VAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRAGSPVKRVS 188
Cdd:cd07869  85 VHT-DLCQYMDKHPGGLHPeNVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTG--ELKLADFGLARAKSVPSHTYS 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 75570321 189 G---TIPYTAPELCDTSKHDGFCVdystDVWAFGVLLFCMLTG 228
Cdd:cd07869 162 NevvTLWYRPPDVLLGSTEYSTCL----DMWGVGCIFVEMIQG 200
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
76-266 1.45e-08

Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 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. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal 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: 271029 [Multi-domain]  Cd Length: 277  Bit Score: 55.19  E-value: 1.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  76 EYSISLYLSPCPFIINMFGIAFETDEYYVFAQEYAPS-GDLFDIIPPQVGLPEPV--AKRCVHQVaialEYLHSKKLVHR 152
Cdd:cd14127  45 EYRTYKLLAGCPGIPNVYYFGQEGLHNILVIDLLGPSlEDLFDLCGRKFSVKTVVmvAKQMLTRV----QTIHEKNLIYR 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 153 DIKPENILI---FDKECRKVKLSDFGMTRRAGSPVKRVSgtIPY-TAPELCDTSKH----DGFCVDYS--TDVWAFGVLL 222
Cdd:cd14127 121 DIKPDNFLIgrpGTKNANVIHVVDFGMAKQYRDPKTKQH--IPYrEKKSLSGTARYmsinTHLGREQSrrDDLEALGHVF 198
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75570321 223 FCMLTGNFPWE--KAMPSDTFYEEFVrwQKRRTGAVPSQWRRFTDE 266
Cdd:cd14127 199 MYFLRGSLPWQglKAATNKQKYEKIG--EKKQSTPIRDLCEGFPEE 242
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
75-288 1.57e-08

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: 55.45  E-value: 1.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  75 REYSISLYLSPcPFIINMFG-IAFETDEYYVFAqEYAPSGDLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKK--LVH 151
Cdd:cd14041  59 REYRIHKELDH-PRIVKLYDyFSLDTDSFCTVL-EYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIH 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 152 RDIKPENILIFD-KECRKVKLSDFGMTRRAGSP----------VKRVSGTIPYTAPElCDTSKHDGFCVDYSTDVWAFGV 220
Cdd:cd14041 137 YDLKPGNILLVNgTACGEIKITDFGLSKIMDDDsynsvdgmelTSQGAGTYWYLPPE-CFVVGKEPPKISNKVDVWSVGV 215
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 221 LLFCMLTGNFPWEKAMPSDTFYEEFVRWQKRRTGAVPSQwrRFTDESLRMFRKLLALEQERRCSVKEV 288
Cdd:cd14041 216 IFYQCLYGRKPFGHNQSQQDILQENTILKATEVQFPPKP--VVTPEAKAFIRRCLAYRKEDRIDVQQL 281
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
87-234 1.59e-08

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: 55.16  E-value: 1.59e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVFAqEYAPSGDL--FDII---------PPQVGLPEPVAkrCVHQVAIALEYLHSKKLVHRDIK 155
Cdd:cd05046  68 KNVVRLLGLCREAEPHYMIL-EYTDLGDLkqFLRAtkskdeklkPPPLSTKQKVA--LCTQIALGMDHLSNARFVHRDLA 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 156 PENILIFDKecRKVKLSDFGMTRRAGSP--VKRVSGTIP--YTAPElcdtskhdgfCV---DYST--DVWAFGVLLFCML 226
Cdd:cd05046 145 ARNCLVSSQ--REVKVSLLSLSKDVYNSeyYKLRNALIPlrWLAPE----------AVqedDFSTksDVWSFGVLMWEVF 212

                ....*....
gi 75570321 227 T-GNFPWEK 234
Cdd:cd05046 213 TqGELPFYG 221
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
113-233 1.64e-08

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: 55.21  E-value: 1.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 113 GDLFDIIPpQVGLPEPVAKRCV----HQVAIALEYLHSKK--LVHRDIKPENILIFDKecRKVKLSDFG-MTRRAGSP-- 183
Cdd:cd14036  90 GQLVDFVK-KVEAPGPFSPDTVlkifYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQ--GQIKLCDFGsATTEAHYPdy 166
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75570321 184 ----VKR-------VSGTIP-YTAPELCDTskHDGFCVDYSTDVWAFGVLLFCMLTGNFPWE 233
Cdd:cd14036 167 swsaQKRslvedeiTRNTTPmYRTPEMIDL--YSNYPIGEKQDIWALGCILYLLCFRKHPFE 226
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
108-275 1.85e-08

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, 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 TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 55.14  E-value: 1.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 108 EYAPSGDLFDIIPPQVGLPEPVAKRCVhQVAIALEYLHSK--------KLVHRDIKPENILIfdKECRKVKLSDFGMTRR 179
Cdd:cd14143  73 DYHEHGSLFDYLNRYTVTVEGMIKLAL-SIASGLAHLHMEivgtqgkpAIAHRDLKSKNILV--KKNGTCCIADLGLAVR 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 180 AGS--------PVKRVsGTIPYTAPE-LCDTSKHDGFCVDYSTDVWAFGVLLF-----CMLTG-----NFPWEKAMPSDT 240
Cdd:cd14143 150 HDSatdtidiaPNHRV-GTKRYMAPEvLDDTINMKHFESFKRADIYALGLVFWeiarrCSIGGihedyQLPYYDLVPSDP 228
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 75570321 241 FYEEF---VRWQKRRTGaVPSQWRrfTDESLRMFRKLL 275
Cdd:cd14143 229 SIEEMrkvVCEQKLRPN-IPNRWQ--SCEALRVMAKIM 263
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
96-161 2.11e-08

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 54.72  E-value: 2.11e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  96 AFETDEYYVFAQEYAPSGDLFDIIPP--QVG--LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILI 161
Cdd:cd14051  68 AWAEDDHMIIQNEYCNGGSLADAISEneKAGerFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFI 137
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
103-223 2.48e-08

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They 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. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. 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 serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 54.41  E-value: 2.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 103 YVFAQEYAPSGDLFDIIPPQVGLPEPVAK-RCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECRK----VKLSDFGMT 177
Cdd:cd05037  76 NIMVQEYVRYGPLDKYLRRMGNNVPLSWKlQVAKQLASALHYLEDKKLIHGNVRGRNILLAREGLDGyppfIKLSDPGVP 155
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 75570321 178 RRAGSPVKRVSgTIPYTAPELCdtsKHDGFCVDYSTDVWAFGVLLF 223
Cdd:cd05037 156 ITVLSREERVD-RIPWIAPECL---RNLQANLTIAADKWSFGTTLW 197
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
101-175 2.57e-08

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 54.75  E-value: 2.57e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 101 EYYVFAQEYAPsgdlfdiiPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENIlIFDKECRKVKLSDFG 175
Cdd:cd14013 101 EPIIFGRVLIP--------PRGPKRENVIIKSIMRQILVALRKLHSTGIVHRDVKPQNI-IVSEGDGQFKIIDLG 166
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
38-231 2.94e-08

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


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 54.06  E-value: 2.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIrGSKMALKFLKKKSTKLKSFLREYSISLYLSPcPFIINMFGIAFETDEYYVFAqEYAPSGDLFD 117
Cdd:cd14156   1 IGSGFFSKVYKVTHGA-TGKVMVVKIYKNDVDQHKIVREISLLQKLSH-PNIVRYLGICVKDEKLHPIL-EYVSGGCLEE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 118 IIPPQ---VGLPEPVAKRCvhQVAIALEYLHSKKLVHRDIKPENILIFDK-ECRKVKLSDFGMTRRAG-----SPVKRVS 188
Cdd:cd14156  78 LLAREelpLSWREKVELAC--DISRGMVYLHSKNIYHRDLNSKNCLIRVTpRGREAVVTDFGLAREVGempanDPERKLS 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 75570321 189 --GTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLfCMLTGNFP 231
Cdd:cd14156 156 lvGSAFWMAPEMLRGEPY-----DRKVDVFSFGIVL-CEILARIP 194
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
136-244 3.77e-08

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; 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 domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 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: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 54.15  E-value: 3.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENILIFDKECRK-----VKLSDFGMTRRAGSPVKRVSgTIPYTAPELCDTskhdGFCVD 210
Cdd:cd05076 124 QLASALSYLENKNLVHGNVCAKNILLARLGLEEgtspfIKLSDPGVGLGVLSREERVE-RIPWIAPECVPG----GNSLS 198
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 75570321 211 YSTDVWAFG-VLLFCMLTGNFPWEKAMPSDT--FYEE 244
Cdd:cd05076 199 TAADKWGFGaTLLEICFNGEAPLQSRTPSEKerFYQR 235
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
114-250 3.85e-08

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271028 [Multi-domain]  Cd Length: 288  Bit Score: 54.35  E-value: 3.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPPQVGLpepvakRCVHQVAIAL----EYLHSKKLVHRDIKPENILIFDKECRK---VKLSDFGMTRRAGSPV-- 184
Cdd:cd14126  84 DLFDLCDRTFSL------KTVLMIAIQLisriEYVHSKHLIYRDVKPENFLIGRQSTKKqhvIHIIDFGLAKEYIDPEtn 157
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75570321 185 --------KRVSGTIPYTApelcdTSKHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEkAMPSDTFYEefvRWQK 250
Cdd:cd14126 158 khipyrehKSLTGTARYMS-----INTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQ-GLKADTLKE---RYQK 222
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
135-242 4.31e-08

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 54.47  E-value: 4.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 135 HQVAIALEYLHSKKLVHRDIKPENILIFDKecRKVKLSDFGMTR------------RAGSPVKrvsgtipYTAPElcdtS 202
Cdd:cd05106 219 SQVAQGMDFLASKNCIHRDVAARNVLLTDG--RVAKICDFGLARdimndsnyvvkgNARLPVK-------WMAPE----S 285
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 75570321 203 KHDgfCVdYS--TDVWAFGVLLFCMLT-GNFPWEKAMPSDTFY 242
Cdd:cd05106 286 IFD--CV-YTvqSDVWSYGILLWEIFSlGKSPYPGILVNSKFY 325
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
96-259 4.31e-08

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: 53.88  E-value: 4.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  96 AFETDEYYVFAQEYAPSGDLFDIIPPQVGLPEPVAKRC--VHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSD 173
Cdd:cd05073  73 AVVTKEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLIdfSAQIAEGMAFIEQRNYIHRDLRAANILV--SASLVCKIAD 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 174 FGMTR--RAGSPVKRVSGTIP--YTAPELCDtskHDGFCVdySTDVWAFGVLLFCMLT-GNFPWEKAMPSDTFYEEFVRW 248
Cdd:cd05073 151 FGLARviEDNEYTAREGAKFPikWTAPEAIN---FGSFTI--KSDVWSFGILLMEIVTyGRIPYPGMSNPEVIRALERGY 225
                       170
                ....*....|.
gi 75570321 249 QKRRTGAVPSQ 259
Cdd:cd05073 226 RMPRPENCPEE 236
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
89-232 4.56e-08

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


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 53.38  E-value: 4.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFETDEYYVfaQEYAPSGDLFDIIPPQVG----LPEPVAKRCvhQVAIALEYLHSKKLVHRDIKPENILIFDK 164
Cdd:cd14203  52 LVQLYAVVSEEPIYIV--TEFMSKGSLLDFLKDGEGkylkLPQLVDMAA--QIASGMAYIERMNYIHRDLRAANILVGDN 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 165 -ECrkvKLSDFGMTR---------RAGS--PVKrvsgtipYTAPElcdTSKHDGFCVdySTDVWAFGVLLFCMLT-GNFP 231
Cdd:cd14203 128 lVC---KIADFGLARliedneytaRQGAkfPIK-------WTAPE---AALYGRFTI--KSDVWSFGILLTELVTkGRVP 192

                .
gi 75570321 232 W 232
Cdd:cd14203 193 Y 193
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
136-233 5.13e-08

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: 53.57  E-value: 5.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR---RAGSPVKRVSGTIP--YTAPElcdtSKHDGfcvD 210
Cdd:cd05057 117 QIAKGMSYLEEKRLVHRDLAARNVLV--KTPNHVKITDFGLAKlldVDEKEYHAEGGKVPikWMALE----SIQYR---I 187
                        90       100
                ....*....|....*....|....*.
gi 75570321 211 YS--TDVWAFGVLLFCMLT-GNFPWE 233
Cdd:cd05057 188 YThkSDVWSYGVTVWELMTfGAKPYE 213
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
37-222 5.51e-08

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


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 53.53  E-value: 5.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  37 ELGKGTYGKV---DLVIHKIRGSKMALKFLKKKSTKLKSFLREY--SISLYLS-PCPFIINMFGIAFeTDEYYVFAQEYA 110
Cdd:cd05048  12 ELGEGAFGKVykgELLGPSSEESAISVAIKTLKENASPKTQQDFrrEAELMSDlQHPNIVCLLGVCT-KEQPQCMLFEYM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 111 PSGDLFDII--------PPQVGLPEPVAKRCVH--------QVAIALEYLHSKKLVHRDIKPENILIFDKecRKVKLSDF 174
Cdd:cd05048  91 AHGDLHEFLvrhsphsdVGVSSDDDGTASSLDQsdflhiaiQIAAGMEYLSSHHYVHRDLAARNCLVGDG--LTVKISDF 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 75570321 175 GMTRRA-GSPVKRVSGT----IPYTAPELCDTSKhdgFCVDysTDVWAFGVLL 222
Cdd:cd05048 169 GLSRDIySSDYYRVQSKsllpVRWMPPEAILYGK---FTTE--SDVWSFGVVL 216
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
87-266 6.77e-08

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: 53.46  E-value: 6.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFeTDEYYVFAQEYAPSGDLFDIIP---PQVGLPEPVAKRCVH---------QVAIALEYLHSKKLVHRDI 154
Cdd:cd05095  79 PNIIRLLAVCI-TDDPLCMITEYMENGDLNQFLSrqqPEGQLALPSNALTVSysdlrfmaaQIASGMKYLSSLNFVHRDL 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 155 KPENILIfdKECRKVKLSDFGMTRRAGS-PVKRVSG----TIPYTAPELCDTSKhdgfcVDYSTDVWAFGVLLFCMLT-- 227
Cdd:cd05095 158 ATRNCLV--GKNYTIKIADFGMSRNLYSgDYYRIQGravlPIRWMSWESILLGK-----FTTASDVWAFGVTLWETLTfc 230
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75570321 228 GNFPWEKaMPSDTFYE---EFVRWQKRRT-----GAVP--------SQWRRFTDE 266
Cdd:cd05095 231 REQPYSQ-LSDEQVIEntgEFFRDQGRQTylpqpALCPdsvyklmlSCWRRDTKD 284
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
105-232 6.88e-08

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: 53.43  E-value: 6.88e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 105 FAQEYAPSGDLFD----IIPPQVGLPEPVAkrCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRA 180
Cdd:cd05092  97 FLRSHGPDAKILDggegQAPGQLTLGQMLQ--IASQIASGMVYLASLHFVHRDLATRNCLV--GQGLVVKIGDFGMSRDI 172
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 181 GSP-VKRVSG----TIPYTAPELCDTSKhdgFCVDysTDVWAFGVLLFCMLT-GNFPW 232
Cdd:cd05092 173 YSTdYYRVGGrtmlPIRWMPPESILYRK---FTTE--SDIWSFGVVLWEIFTyGKQPW 225
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
135-231 7.35e-08

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: 53.38  E-value: 7.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 135 HQVAIALEYLHSKKLVHRDIKPENILIfdKECRKV-KLSDFGMTRRAG----SP--VKRVsgtipYTAPELCdtskhDGF 207
Cdd:cd14135 112 QQLFLALKHLKKCNILHADIKPDNILV--NEKKNTlKLCDFGSASDIGeneiTPylVSRF-----YRAPEII-----LGL 179
                        90       100
                ....*....|....*....|....*.
gi 75570321 208 CVDYSTDVWAFGVLLFCMLTGN--FP 231
Cdd:cd14135 180 PYDYPIDMWSVGCTLYELYTGKilFP 205
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
132-275 7.67e-08

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


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 53.21  E-value: 7.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 132 RCVHQVAIALEYLHSK---------KLVHRDIKPENILI-FDKECrkvKLSDFGMTRR--------AGSPVKRVsGTIPY 193
Cdd:cd13998  96 RLALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNILVkNDGTC---CIADFGLAVRlspstgeeDNANNGQV-GTKRY 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 194 TAPELCDTskhdgfCVDYS-------TDVWAFGVLLFCM---LTGNF--------PWEKAMPSDTFYEEF----VRWQKR 251
Cdd:cd13998 172 MAPEVLEG------AINLRdfesfkrVDIYAMGLVLWEMasrCTDLFgiveeykpPFYSEVPNHPSFEDMqevvVRDKQR 245
                       170       180
                ....*....|....*....|....
gi 75570321 252 RTgaVPSQWrrFTDESLRMFRKLL 275
Cdd:cd13998 246 PN--IPNRW--LSHPGLQSLAETI 265
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
24-198 8.61e-08

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 53.01  E-value: 8.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  24 EKLEVNKyyevireLGKGTYGKVDLVIHKIRGSKMA---LKFLKKKSTKLKSFLREYSISLYLSPCPFIINMFGiAFETD 100
Cdd:cd14139   1 EFLELEK-------IGVGEFGSVYKCIKRLDGCVYAikrSMRPFAGSSNEQLALHEVYAHAVLGHHPHVVRYYS-AWAED 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 101 EYYVFAQEYAPSGDLFDIIPPQVGL----PEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdkeCRKVKLSDFGM 176
Cdd:cd14139  73 DHMIIQNEYCNGGSLQDAISENTKSgnhfEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFI----CHKMQSSSGVG 148
                       170       180
                ....*....|....*....|..
gi 75570321 177 TRRAGSPVKRVSGTIPYTAPEL 198
Cdd:cd14139 149 EEVSNEEDEFLSANVVYKIGDL 170
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
133-233 1.23e-07

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: 52.72  E-value: 1.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 133 CVhQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTRRAGSPVKRV---SGTIP--YTAPE--LCDTSKHd 205
Cdd:cd05108 115 CV-QIAKGMNYLEDRRLVHRDLAARNVLV--KTPQHVKITDFGLAKLLGAEEKEYhaeGGKVPikWMALEsiLHRIYTH- 190
                        90       100
                ....*....|....*....|....*....
gi 75570321 206 gfcvdySTDVWAFGVLLFCMLT-GNFPWE 233
Cdd:cd05108 191 ------QSDVWSYGVTVWELMTfGSKPYD 213
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
89-232 1.28e-07

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: 52.74  E-value: 1.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFETDEYyVFAQEYAPSGDLFDII-------------PPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIK 155
Cdd:cd05093  69 IVKFYGVCVEGDPL-IMVFEYMKHGDLNKFLrahgpdavlmaegNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLA 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 156 PENILIfdKECRKVKLSDFGMTRRAGSP-VKRVSG----TIPYTAPElcdTSKHDGFCVDysTDVWAFGVLLFCMLT-GN 229
Cdd:cd05093 148 TRNCLV--GENLLVKIGDFGMSRDVYSTdYYRVGGhtmlPIRWMPPE---SIMYRKFTTE--SDVWSLGVVLWEIFTyGK 220

                ...
gi 75570321 230 FPW 232
Cdd:cd05093 221 QPW 223
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
134-291 1.44e-07

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: 52.80  E-value: 1.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 134 VHQVAIALEYLHSKKLVHRDIKPENILIFDkECrKVKLSDFGMTRRAG-----SP--VKRVsgtipYTAPELCdtskhdg 206
Cdd:cd07850 108 LYQMLCGIKHLHSAGIIHRDLKPSNIVVKS-DC-TLKILDFGLARTAGtsfmmTPyvVTRY-----YRAPEVI------- 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 207 FCVDYS--TDVWAFGVLLFCMLTGN--FP-------WEK-----AMPSDTFYEE-------FVRWQKRRTG--------- 254
Cdd:cd07850 174 LGMGYKenVDIWSVGCIMGEMIRGTvlFPgtdhidqWNKiieqlGTPSDEFMSRlqptvrnYVENRPKYAGysfeelfpd 253
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 75570321 255 -----AVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07850 254 vlfppDSEEHNKLKASQARDLLSKMLVIDPEKRISVDDALQH 295
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
135-220 1.47e-07

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: 52.72  E-value: 1.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 135 HQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGmTRRAGSPVKRVSGTIPYTAPELC---DTSKHDGfcvdy 211
Cdd:cd06634 122 HGALQGLAYLHSHNMIHRDVKAGNILL--TEPGLVKLGDFG-SASIMAPANSFVGTPYWMAPEVIlamDEGQYDG----- 193

                ....*....
gi 75570321 212 STDVWAFGV 220
Cdd:cd06634 194 KVDVWSLGI 202
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
141-243 1.74e-07

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 51.98  E-value: 1.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 141 LEYLHSKKLVHRDIKPENILI-FDKECRKVKLSDFGMTRRAGSPVKRVSgtIPY--------TApELCDTSKHDGFCVDY 211
Cdd:cd14125 109 IEYVHSKNFIHRDIKPDNFLMgLGKKGNLVYIIDFGLAKKYRDPRTHQH--IPYrenknltgTA-RYASINTHLGIEQSR 185
                        90       100       110
                ....*....|....*....|....*....|....
gi 75570321 212 STDVWAFGVLLFCMLTGNFPWE--KAMPSDTFYE 243
Cdd:cd14125 186 RDDLESLGYVLMYFNRGSLPWQglKAATKKQKYE 219
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
135-222 1.75e-07

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: 51.99  E-value: 1.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 135 HQVAIALEYLHSKKLVHRDIKPENILIfDKECRkVKLSDFGMTRRAGSP---VKRVSGTIP--YTAPElcdTSKHDGFCV 209
Cdd:cd05033 113 RGIASGMKYLSEMNYVHRDLAARNILV-NSDLV-CKVSDFGLSRRLEDSeatYTTKGGKIPirWTAPE---AIAYRKFTS 187
                        90
                ....*....|...
gi 75570321 210 dySTDVWAFGVLL 222
Cdd:cd05033 188 --ASDVWSFGIVM 198
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
114-291 2.04e-07

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: 52.37  E-value: 2.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 114 DLFDIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfDKECrKVKLSDFGMTRRAGSPVKRVSG---T 190
Cdd:cd07858  94 DLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLL-NANC-DLKICDFGLARTTSEKGDFMTEyvvT 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 191 IPYTAPELCDTskhdgfCVDYST--DVWAFGVLLFCMLTGN--FPWEKAM------------PSDTfYEEFVRWQK---- 250
Cdd:cd07858 172 RWYRAPELLLN------CSEYTTaiDVWSVGCIFAELLGRKplFPGKDYVhqlklitellgsPSEE-DLGFIRNEKarry 244
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75570321 251 -RRTGAVPSQ-----WRRFTDESLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07858 245 iRSLPYTPRQsfarlFPHANPLAIDLLEKMLVFDPSKRITVEEALAH 291
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
38-239 2.09e-07

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 51.87  E-value: 2.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  38 LGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSF-LREYSISLYLSPcPFIINMFGIAFEtDEYYVFAQEYAPSGDLF 116
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTfLTEVKVMRSLDH-PNVLKFIGVLYK-DKRLNLLTEFIEGGTLK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 117 DIIPPQVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR-----RAGSPVKR----- 186
Cdd:cd14222  79 DFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLI--KLDKTVVVADFGLSRliveeKKKPPPDKpttkk 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 187 -------------VSGTIPYTAPELCDTSKHdgfcvDYSTDVWAFGVLLfCMLTGN-------FP------------WEK 234
Cdd:cd14222 157 rtlrkndrkkrytVVGNPYWMAPEMLNGKSY-----DEKVDIFSFGIVL-CEIIGQvyadpdcLPrtldfglnvrlfWEK 230

                ....*
gi 75570321 235 AMPSD 239
Cdd:cd14222 231 FVPKD 235
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
32-291 2.35e-07

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: 51.73  E-value: 2.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKL---KSFLREYSISLYLSPcPFIINMFGIA--------FETD 100
Cdd:cd07864   9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEgfpITAIREIKILRQLNH-RSVVNLKEIVtdkqdaldFKKD 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 101 E---YYVFaqEYApSGDLFDIIPPQ-VGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGM 176
Cdd:cd07864  88 KgafYLVF--EYM-DHDLMGLLESGlVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKG--QIKLADFGL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 177 TRRAGSPVKRVSG----TIPYTAPELCDTSKHDGfcvdYSTDVWAFGVLLFCMLTGN--FPWEKAM------------PS 238
Cdd:cd07864 163 ARLYNSEESRPYTnkviTLWYRPPELLLGEERYG----PAIDVWSCGCILGELFTKKpiFQANQELaqlelisrlcgsPC 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75570321 239 DTFYEEFVRWQKRRTGAVPSQWRRFTDE--------SLRMFRKLLALEQERRCSVKEVFAH 291
Cdd:cd07864 239 PAVWPDVIKLPYFNTMKPKKQYRRRLREefsfiptpALDLLDHMLTLDPSKRCTAEQALNS 299
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
122-228 2.35e-07

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: 51.78  E-value: 2.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 122 QVGLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRAGSPVKRVSGTIPYTAPELCDT 201
Cdd:cd05576 107 RFYIPEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRG--HIQLTYFSRWSEVEDSCDSDAIENMYCAPEVGGI 184
                        90       100
                ....*....|....*....|....*..
gi 75570321 202 SKHDGFCvdystDVWAFGVLLFCMLTG 228
Cdd:cd05576 185 SEETEAC-----DWWSLGALLFELLTG 206
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
132-234 2.38e-07

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 51.59  E-value: 2.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 132 RCVHQVAIALEYLHSKKLVHRDIKPENILI--FDKECRKVKLSDFGMTR---------RAGSPVKRVSGTIPYTApelcd 200
Cdd:cd14129 101 RLGRQILESIESIHSVGFLHRDIKPSNFAMgrFPSTCRKCYMLDFGLARqftnscgdvRPPRAVAGFRGTVRYAS----- 175
                        90       100       110
                ....*....|....*....|....*....|....
gi 75570321 201 TSKHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEK 234
Cdd:cd14129 176 INAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRK 209
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
129-291 2.45e-07

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 51.59  E-value: 2.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 129 VAKRCVHQVAIALEYLHSKK--LVHRDIKPENILIfDKECRKVKLSDFGM-TRRAGSPVKRVSGTIPYTAPELCDTSkhd 205
Cdd:cd14030 129 VLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFI-TGPTGSVKIGDLGLaTLKRASFAKSVIGTPEFMAPEMYEEK--- 204
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 206 gfcVDYSTDVWAFGVLLFCMLTGNFPWEKAMPSDTFYeefvrwQKRRTGAVPSQWRRFT-DESLRMFRKLLALEQERRCS 284
Cdd:cd14030 205 ---YDESVDVYAFGMCMLEMATSEYPYSECQNAAQIY------RRVTSGVKPASFDKVAiPEVKEIIEGCIRQNKDERYA 275

                ....*..
gi 75570321 285 VKEVFAH 291
Cdd:cd14030 276 IKDLLNH 282
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
121-233 2.70e-07

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: 51.54  E-value: 2.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 121 PQVGLPEPVaKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKECrkVKLSDFGMTRR--AGSPVKRVS--GTIPYTAP 196
Cdd:cd07848  94 PNGVPPEKV-RSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDV--LKLCDFGFARNlsEGSNANYTEyvATRWYRSP 170
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 75570321 197 ELCDTSKHDGfcvdySTDVWAFGVLLFCMLTGN--FPWE 233
Cdd:cd07848 171 ELLLGAPYGK-----AVDMWSVGCILGELSDGQplFPGE 204
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
136-226 2.85e-07

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: 51.79  E-value: 2.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 136 QVAIALEYLHSKKLVHRDIKPENILIFDKECRK-VKLSDFGMTR----RAGSPVKRVS----------GTIPYTAPELCD 200
Cdd:cd13977 142 QLSSALAFLHRNQIVHRDLKPDNILISHKRGEPiLKVADFGLSKvcsgSGLNPEEPANvnkhflssacGSDFYMAPEVWE 221
                        90       100
                ....*....|....*....|....*....
gi 75570321 201 ---TSKhdgfcvdysTDVWAFGVLLFCML 226
Cdd:cd13977 222 ghyTAK---------ADIFALGIIIWAMV 241
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
141-244 3.00e-07

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 51.35  E-value: 3.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 141 LEYLHSKKLVHRDIKPENILI-FDKECRKVKLSDFGMTRRAGSPvkRVSGTIPYTAPE-LCDTSK------HDGFCVDYS 212
Cdd:cd14128 109 IEYVHNKNFIHRDIKPDNFLMgIGRHCNKLFLIDFGLAKKYRDS--RTRQHIPYREDKnLTGTARyasinaHLGIEQSRR 186
                        90       100       110
                ....*....|....*....|....*....|....
gi 75570321 213 TDVWAFGVLLFCMLTGNFPWE--KAMPSDTFYEE 244
Cdd:cd14128 187 DDMESLGYVLMYFNRGSLPWQglKAATKKQKYEK 220
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
136-175 3.39e-07

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 52.10  E-value: 3.39e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 75570321  136 QVAIALEYLHSKKLVHRDIKPENIlIFDKECRKVKLSDFG 175
Cdd:PLN03225 263 QILFALDGLHSTGIVHRDVKPQNI-IFSEGSGSFKIIDLG 301
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
74-293 3.62e-07

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: 51.33  E-value: 3.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  74 LREYSISLYLSPCPFIINMFGIAFETDEYYVFAqEYAPSGDLFDII--PPQVGLPEPVAKRCVHQVAIALEYLHSKKLVH 151
Cdd:cd05055  86 MSELKIMSHLGNHENIVNLLGACTIGGPILVIT-EYCCYGDLLNFLrrKRESFLTLEDLLSFSYQVAKGMAFLASKNCIH 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 152 RDIKPENILIfdKECRKVKLSDFGMTRRAGSP---VKRVSGTIP--YTAPElcdtSKHDGFcvdYST--DVWAFGVLLFC 224
Cdd:cd05055 165 RDLAARNVLL--THGKIVKICDFGLARDIMNDsnyVVKGNARLPvkWMAPE----SIFNCV---YTFesDVWSYGILLWE 235
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 225 MLT-GNFPWEKAMPSDTFYeefvrwQKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCSVKEVFAHLG 293
Cdd:cd05055 236 IFSlGSNPYPGMPVDSKFY------KLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLIG 299
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
135-243 3.72e-07

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 51.44  E-value: 3.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 135 HQVAIALEYLHSKKLVHRDIKPENILIfdKECRKVKLSDFGMTR------------RAGSPVKrvsgtipYTAPELCDTs 202
Cdd:cd05104 221 YQVAKGMEFLASKNCIHRDLAARNILL--THGRITKICDFGLARdirndsnyvvkgNARLPVK-------WMAPESIFE- 290
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 75570321 203 khdgfCV-DYSTDVWAFGVLLFCMLT-GNFPWeKAMPSDT-FYE 243
Cdd:cd05104 291 -----CVyTFESDVWSYGILLWEIFSlGSSPY-PGMPVDSkFYK 328
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
32-307 4.25e-07

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 51.17  E-value: 4.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  32 YEVIRELGKGTYGKV-DLVIHKIRGSKMALKFLKkkstklksflreySISLYLSPCPFIINMFGIAFETD---------- 100
Cdd:cd14215  14 YEIVSTLGEGTFGRVvQCIDHRRGGARVALKIIK-------------NVEKYKEAARLEINVLEKINEKDpenknlcvqm 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 101 -EYYVFAQEYAPSGDL-----FDIIPPQVGLPEPV--AKRCVHQVAIALEYLHSKKLVHRDIKPENILIF---------- 162
Cdd:cd14215  81 fDWFDYHGHMCISFELlglstFDFLKENNYLPYPIhqVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVnsdyeltynl 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 163 ----DKECRK---VKLSDFGMTRRAGSPVKRVSGTIPYTAPELCDTSKHDGFCvdystDVWAFGVLLFCMLTGnFPWEKA 235
Cdd:cd14215 161 ekkrDERSVKstaIRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPC-----DVWSIGCIIFEYYVG-FTLFQT 234
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75570321 236 MPSdtfyEEFVRWQKRRTGAVPSQWRRFTDESLRMFRKLLALEQERRCS--VKEVFAHLgHRWMLDGTSgNHHQ 307
Cdd:cd14215 235 HDN----REHLAMMERILGPIPSRMIRKTRKQKYFYHGRLDWDENTSAGryVRENCKPL-RRYLTSEAE-EHHQ 302
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
125-228 4.41e-07

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: 51.18  E-value: 4.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 125 LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFD--KECRKVKLSDFGmtrRAGSPVKRVSGTIP----YTAPEL 198
Cdd:cd14229  99 LPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDpvRQPYRVKVIDFG---SASHVSKTVCSTYLqsryYRAPEI 175
                        90       100       110
                ....*....|....*....|....*....|
gi 75570321 199 CDTSKhdgFCvdYSTDVWAFGVLLFCMLTG 228
Cdd:cd14229 176 ILGLP---FC--EAIDMWSLGCVIAELFLG 200
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
124-161 4.57e-07

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 51.17  E-value: 4.57e-07
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 75570321 124 GLPEPVAKRCVHQVAIALEYLHSK-KLVHRDIKPENILI 161
Cdd:cd14218 115 GLPLPCVKSILRQVLQGLDYLHTKcKIIHTDIKPENILM 153
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
124-198 5.01e-07

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK2 mediates neuronal cell cycle and cell death through regulation of nuclear cyclin D1. It has also been found to promote leukemia cell proliferation by regulating cyclin A1. SRPK2 also plays a role in regulating pre-mRNA splicing and is required for spliceosomal B complex formation. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271119 [Multi-domain]  Cd Length: 366  Bit Score: 51.18  E-value: 5.01e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75570321 124 GLPEPVAKRCVHQVAIALEYLHSK-KLVHRDIKPENIL--IFDKECRKVKlSDFGMTRRAGSPVKrvSGTIPYTAPEL 198
Cdd:cd14217 117 GLPIRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILmcVDDAYVRRMA-AEATEWQKAGAPPP--SGSAVSTAPDL 191
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
136-223 5.08e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 51.43  E-value: 5.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  136 QVAIALEYLHSKKLVHRDIKPENILIFDKEcrKVKLSDFGMTRRA----GSPVKR-VSGTIPYTAPELCDTSKHDGfcvd 210
Cdd:PHA03211 268 QLLSAIDYIHGEGIIHRDIKTENVLVNGPE--DICLGDFGAACFArgswSTPFHYgIAGTVDTNAPEVLAGDPYTP---- 341
                         90
                 ....*....|...
gi 75570321  211 ySTDVWAFGVLLF 223
Cdd:PHA03211 342 -SVDIWSAGLVIF 353
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
89-232 5.48e-07

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: 50.46  E-value: 5.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  89 IINMFGIAFETDEYYVfaQEYAPSGDLFDIIPPQVG--LPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIFDKEC 166
Cdd:cd05071  66 LVQLYAVVSEEPIYIV--TEYMSKGSLLDFLKGEMGkyLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLV 143
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75570321 167 RKVklSDFGMTR--RAGSPVKRVSGTIP--YTAPElcdTSKHDGFCVdySTDVWAFGVLLFCMLT-GNFPW 232
Cdd:cd05071 144 CKV--ADFGLARliEDNEYTARQGAKFPikWTAPE---AALYGRFTI--KSDVWSFGILLTELTTkGRVPY 207
PK_VRK3 cd14124
Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to ...
125-238 6.11e-07

Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK3 is an inactive pseudokinase that is unable to bind ATP. It achieves its regulatory function through protein-protein interactions. It negatively regulates ERK signaling by binding directly and enhancing the activity of the MAPK phosphatase VHR (vaccinia H1-related), which dephosphorylates and inactivates ERK. The VRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271026 [Multi-domain]  Cd Length: 298  Bit Score: 50.61  E-value: 6.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 125 LPEpvakRCVHQVAI----ALEYLHSKKLVHRDIKPENILIFDKECRKVKLSDFGMTRR---AGSPVKRVSG--TIPYTA 195
Cdd:cd14124 119 LSE----KAVLQLACrlldALEFIHENEYVHGDITAENIFVDPEDQSEVYLAGYGFAFRycpGGKHVEYREGsrSPHEGD 194
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 75570321 196 PELCDTSKHDGFCVDYSTDVWAFGVLLFCMLTGNFPWEKAMPS 238
Cdd:cd14124 195 IEFISLDSHKGAGPSRRSDLQSLGYCMLKWLTGSLPWSNLLHN 237
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
129-223 6.39e-07

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 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: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 50.32  E-value: 6.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 129 VAKrcvhQVAIALEYLHSKKLVHRDIKPENILI----FDKECRK-VKLSDFGMTRRAGSPVKRVSgTIPYTAPELCDTSK 203
Cdd:cd05077 114 VAK----QLASALSYLEDKDLVHGNVCTKNILLaregIDGECGPfIKLSDPGIPITVLSRQECVE-RIPWIAPECVEDSK 188
                        90       100
                ....*....|....*....|
gi 75570321 204 HdgfcVDYSTDVWAFGVLLF 223
Cdd:cd05077 189 N----LSIAADKWSFGTTLW 204
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
13-326 6.49e-07

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: 50.80  E-value: 6.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  13 EELQLYTAQNLEK-LEVNKYYEVIRELGKGTYGKVDLVIHKIRGSKMALKFLKKKSTKLKSFLREYSiSLYLSPCP---- 87
Cdd:cd07876   3 EDSQFYSVQVADStFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYR-ELVLLKCVnhkn 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  88 --FIINMFGIAFETDEYyvfaQEYAPSGDLFDIIPPQV---GLPEPVAKRCVHQVAIALEYLHSKKLVHRDIKPENILIf 162
Cdd:cd07876  82 iiSLLNVFTPQKSLEEF----QDVYLVMELMDANLCQVihmELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVV- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 163 DKECrKVKLSDFGMTRRAGSPVKRVSGTIP--YTAPELCdtskhDGFCVDYSTDVWAFGVLLFCMLTGNF---------P 231
Cdd:cd07876 157 KSDC-TLKILDFGLARTACTNFMMTPYVVTryYRAPEVI-----LGMGYKENVDIWSVGCIMGELVKGSVifqgtdhidQ 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 232 WEK----------------------------AMPSDTFYEEFVRWqkrrtgAVPSQWRR---FTDESLRMFRKLLALEQE 280
Cdd:cd07876 231 WNKvieqlgtpsaefmnrlqptvrnyvenrpQYPGISFEELFPDW------IFPSESERdklKTSQARDLLSKMLVIDPD 304
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 75570321 281 RRCSVKEVFAH-LGHRWMLDGTSGNHHQSVLNSSSEEDELLVDRMKQ 326
Cdd:cd07876 305 KRISVDEALRHpYITVWYDPAEAEAPPPQIYDAQLEEREHAIEEWKE 351
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
124-161 6.65e-07

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 50.80  E-value: 6.65e-07
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 75570321 124 GLPEPVAKRCVHQVAIALEYLHSK-KLVHRDIKPENILI 161
Cdd:cd14216 115 GLPLPCVKKIIRQVLQGLDYLHTKcRIIHTDIKPENILL 153
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
87-233 7.06e-07

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) 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. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 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: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 50.41  E-value: 7.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321  87 PFIINMFGIAFETDEYYVfaQEYAPSGDLFDIIPPQVGL--PEPVAKRCVhQVAIALEYLHSKKLVHRDIKPENILIfdK 164
Cdd:cd05109  69 PYVCRLLGICLTSTVQLV--TQLMPYGCLLDYVRENKDRigSQDLLNWCV-QIAKGMSYLEEVRLVHRDLAARNVLV--K 143
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75570321 165 ECRKVKLSDFGMTRRAGSPVKRV---SGTIPYTAPELcDTSKHDGFCvdYSTDVWAFGVLLFCMLT-GNFPWE 233
Cdd:cd05109 144 SPNHVKITDFGLARLLDIDETEYhadGGKVPIKWMAL-ESILHRRFT--HQSDVWSYGVTVWELMTfGAKPYD 213
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
137-233 7.85e-07

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


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 49.97  E-value: 7.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75570321 137 VAIALEYLHSKKLVHRDIKPENILIFDK-ECrkvKLSDFGMTR----RAGSPVKRVSGTIP--YTAPELCDTSKHDGfcv 209
Cdd:cd05063 116 IAAGMKYLSDMNYVHRDLAARNILVNSNlEC---KVSDFGLSRvledDPEGTYTTSGGKIPirWTAPEAIAYRKFTS--- 189
                        90       100
                ....*....|....*....|....*.
gi 75570321 210 dySTDVWAFGVLLF-CMLTGNFP-WE 233
Cdd:cd05063 190 --ASDVWSFGIVMWeVMSFGERPyWD 213
 
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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