NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|20986497|ref|NP_002740|]
View 

mitogen-activated protein kinase 7 isoform 1 [Homo sapiens]

Protein Classification

mitogen-activated protein kinase( domain architecture ID 10167618)

mitogen-activated protein kinase (MAPK) is a serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; similar to MAPK7/ERK5 that is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
49-384 0e+00

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: 687.56  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  49 FDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYG 128
Cdd:cd07855   1 FDVGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRTLRELKILRHFKHDNIIAIRDILRPKVPYA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLC 208
Cdd:cd07855  81 DFKDVYVVLDLMESDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQA 288
Cdd:cd07855 161 TSPEEHKYFMTEYVATRWYRAPELMLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVLGTPSQAVINA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 289 VGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCAPPFDFAFD 368
Cdd:cd07855 241 IGADRVRRYIQNLPNKQPVPWETLYPKADQQALDLLSQMLRFDPSERITVAEALQHPFLAKYHDPDDEPDCAPPFDFDFD 320
                       330
                ....*....|....*.
gi 20986497 369 REALTRERIKEAIVAE 384
Cdd:cd07855 321 AEALTREALKEAIVNE 336
 
Name Accession Description Interval E-value
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
49-384 0e+00

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: 687.56  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  49 FDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYG 128
Cdd:cd07855   1 FDVGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRTLRELKILRHFKHDNIIAIRDILRPKVPYA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLC 208
Cdd:cd07855  81 DFKDVYVVLDLMESDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQA 288
Cdd:cd07855 161 TSPEEHKYFMTEYVATRWYRAPELMLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVLGTPSQAVINA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 289 VGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCAPPFDFAFD 368
Cdd:cd07855 241 IGADRVRRYIQNLPNKQPVPWETLYPKADQQALDLLSQMLRFDPSERITVAEALQHPFLAKYHDPDDEPDCAPPFDFDFD 320
                       330
                ....*....|....*.
gi 20986497 369 REALTRERIKEAIVAE 384
Cdd:cd07855 321 AEALTREALKEAIVNE 336
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
55-347 4.13e-90

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 284.42  E-value: 4.13e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497     55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVvTNAKRTLRELKILKHFKHDNIIAIKDILRptvpygEFKSVY 134
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIK-KDRERILREIKILKKLKHPNIVRLYDVFE------DEDKLY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497    135 VVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLctspaE 213
Cdd:smart00220  74 LVMEYCEgGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQL-----D 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497    214 HQYFMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhQLQLIMMVLGTPspaviqavgaer 293
Cdd:smart00220 149 PGEKLTTFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGDD---QLLELFKKIGKP------------ 212
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 20986497    294 vrayiqslPPRQPVPWETVYPgadrQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:smart00220 213 --------KPPFPPPEWDISP----EAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
61-365 2.42e-69

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 232.34  E-value: 2.42e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   61 IGNGAYGVVSSARRRLTGQQVAIKKIPN---AFDVVTNAKR---------TLRELKILKHFKHDNIIAIKDIlrptvpYG 128
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAIKKVKIieiSNDVTKDRQLvgmcgihftTLRELKIMNEIKHENIMGLVDV------YV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  129 EFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLC 208
Cdd:PTZ00024  91 EGDFINLVMDIMASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRYG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  209 TSPAEHQYF----------MTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVL 278
Cdd:PTZ00024 171 YPPYSDTLSkdetmqrreeMTSKVVTLWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIFELL 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  279 GTPSPAVIQAvgAERVRAYIQsLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHpflaKYHDPDDEPd 358
Cdd:PTZ00024 251 GTPNEDNWPQ--AKKLPLYTE-FTPRKPKDLKTIFPNASDDAIDLLQSLLKLNPLERISAKEALKH----EYFKSDPLP- 322
                        330
                 ....*....|
gi 20986497  359 CAP---PFDF 365
Cdd:PTZ00024 323 CDPsqlPFNF 332
Pkinase pfam00069
Protein kinase domain;
55-347 1.18e-48

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 171.27  E-value: 1.18e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497    55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDIlrptvpYGEFKSVY 134
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDA------FEDKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   135 VVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLkymhsaqvihrdlkpsnllvnencelkigdfgmarglctspaE 213
Cdd:pfam00069  75 LVLEYVEgGSLFDLLSEKGAFSEREAKFIMKQILEGL------------------------------------------E 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   214 HQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMmvlgtpspaviqavgaer 293
Cdd:pfam00069 113 SGSSLTTFVGTPWYMAPEV-LGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELII------------------ 173
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 20986497   294 vrayiqslppRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:pfam00069 174 ----------DQPYAFPELPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
51-344 1.50e-41

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 159.02  E-value: 1.50e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  51 VGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKI-PNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDilrptvpYGE 129
Cdd:COG0515   5 LLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLrPELAADPEARERFRREARALARLNHPNIVRVYD-------VGE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSV-YVVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL 207
Cdd:COG0515  78 EDGRpYLVMEYVEgESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 CTSPAEHQYFMteyVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhQLQLIMMVLgtpspaviq 287
Cdd:COG0515 158 GGATLTQTGTV---VGTPGYMAPEQARG-EPVDPRSDVYSLGVTLYELLTGRPPFDGDS---PAELLRAHL--------- 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 288 avgaervrayiqslpPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRH 344
Cdd:COG0515 222 ---------------REPPPPPSELRPDLPPALDAIVLRALAKDPEERYQSAAELAA 263
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
52-264 8.81e-17

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 84.46  E-value: 8.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   52 GDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdvvtnakrTLR-EL----KILKHFK----------HDNIIA 116
Cdd:NF033483   6 GGRYEIGERIGRGGMAEVYLAKDTRLDRDVAVK--------------VLRpDLardpEFVARFRreaqsaaslsHPNIVS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  117 IKDIlrptvpyGEFKSV-YVVldlME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVN 191
Cdd:NF033483  72 VYDV-------GEDGGIpYIV---MEyvdgRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILIT 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  192 ENCELKIGDFGMARGLCTSPAEH--------QYFmteyvatrwyrAPElmlslheytQA--------IDLWSVGCIFGEM 255
Cdd:NF033483 142 KDGRVKVTDFGIARALSSTTMTQtnsvlgtvHYL-----------SPE---------QArggtvdarSDIYSLGIVLYEM 201

                 ....*....
gi 20986497  256 LARRQLFPG 264
Cdd:NF033483 202 LTGRPPFDG 210
 
Name Accession Description Interval E-value
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
49-384 0e+00

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: 687.56  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  49 FDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYG 128
Cdd:cd07855   1 FDVGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRTLRELKILRHFKHDNIIAIRDILRPKVPYA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLC 208
Cdd:cd07855  81 DFKDVYVVLDLMESDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQA 288
Cdd:cd07855 161 TSPEEHKYFMTEYVATRWYRAPELMLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVLGTPSQAVINA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 289 VGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCAPPFDFAFD 368
Cdd:cd07855 241 IGADRVRRYIQNLPNKQPVPWETLYPKADQQALDLLSQMLRFDPSERITVAEALQHPFLAKYHDPDDEPDCAPPFDFDFD 320
                       330
                ....*....|....*.
gi 20986497 369 REALTRERIKEAIVAE 384
Cdd:cd07855 321 AEALTREALKEAIVNE 336
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
55-384 0e+00

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: 574.86  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYgEFKSVY 134
Cdd:cd07834   2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNVFDDLIDAKRILREIKILRHLKHENIIGLLDILRPPSPE-EFNDVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAeh 214
Cdd:cd07834  81 IVTELMETDLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGVDPDED-- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 215 QYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGAERV 294
Cdd:cd07834 159 KGFLTEYVVTRWYRAPELLLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEVLGTPSEEDLKFISSEKA 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 295 RAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCAPPFDFA-FDREALT 373
Cdd:cd07834 239 RNYLKSLPKKPKKPLSEVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQLHDPEDEPVAKPPFDFPfFDDEELT 318
                       330
                ....*....|.
gi 20986497 374 RERIKEAIVAE 384
Cdd:cd07834 319 IEELKELIYEE 329
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
49-389 1.26e-169

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: 493.04  E-value: 1.26e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  49 FDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPtVPYG 128
Cdd:cd07858   1 FEVDTKYVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIANAFDNRIDAKRTLREIKLLRHLDHENVIAIKDIMPP-PHRE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglc 208
Cdd:cd07858  80 AFNDVYIVYELMDTDLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLAR--- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAEHQyFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQA 288
Cdd:cd07858 157 TTSEKGD-FMTEYVVTRWYRAPELLLNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGSPSEEDLGF 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 289 VGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCAPPFDFAFD 368
Cdd:cd07858 236 IRNEKARRYIRSLPYTPRQSFARLFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYLASLHDPSDEPVCQTPFSFDFE 315
                       330       340
                ....*....|....*....|.
gi 20986497 369 REALTRERIKEAIVAEIEDFH 389
Cdd:cd07858 316 EDALTEEDIKELIYNEMLAYH 336
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
49-385 4.06e-168

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: 489.12  E-value: 4.06e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  49 FDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTvPYG 128
Cdd:cd07849   1 FDVGPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKI-SPFEHQTYCLRTLREIKILLRFKHENIIGILDIQRPP-TFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMESDLHQIIhSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARgLC 208
Cdd:cd07849  79 SFKDVYIVQELMETDLYKLI-KTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLAR-IA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQA 288
Cdd:cd07849 157 DPEHDHTGFLTEYVATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGILGTPSQEDLNC 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 289 VGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCAPPFDFAFD 368
Cdd:cd07849 237 IISLKARNYIKSLPFKPKVPWNKLFPNADPKALDLLDKMLTFNPHKRITVEEALAHPYLEQYHDPSDEPVAEEPFPFDME 316
                       330
                ....*....|....*...
gi 20986497 369 R-EALTRERIKEAIVAEI 385
Cdd:cd07849 317 LfDDLPKEKLKELIFEEI 334
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
48-388 9.43e-149

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: 439.81  E-value: 9.43e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  48 TFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPY 127
Cdd:cd07851  10 VWEVPDRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPASSL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 128 GEFKSVYVVLDLMESDLHQIIhSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARgl 207
Cdd:cd07851  90 EDFQDVYLVTHLMGADLNNIV-KCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLAR-- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 ctsPAEHQyfMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQ 287
Cdd:cd07851 167 ---HTDDE--MTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNLVGTPDEELLK 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 288 AVGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDcAPPFDFAF 367
Cdd:cd07851 242 KISSESARNYIQSLPQMPKKDFKEVFSGANPLAIDLLEKMLVLDPDKRITAAEALAHPYLAEYHDPEDEPV-APPYDQSF 320
                       330       340
                ....*....|....*....|.
gi 20986497 368 DREALTRERIKEAIVAEIEDF 388
Cdd:cd07851 321 ESRDLTVDEWKELVYDEIMNF 341
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
55-385 3.24e-147

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: 435.68  E-value: 3.24e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSAR--RRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFK-HDNIIAIKDIlrPTVPYGEFK 131
Cdd:cd07857   2 YELIKELGQGAYGIVCSARnaETSEEETVAIKKITNVFSKKILAKRALRELKLLRHFRgHKNITCLYDM--DIVFPGNFN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSP 211
Cdd:cd07857  80 ELYLYEELMEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFSENP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 212 AEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGA 291
Cdd:cd07857 160 GENAGFMTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQVLGTPDEETLSRIGS 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 292 ERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCAPPFDFAFDREA 371
Cdd:cd07857 240 PKAQNYIRSLPNIPKKPFESIFPNANPLALDLLEKLLAFDPTKRISVEEALEHPYLAIWHDPDDEPVCQKPFDFSFESED 319
                       330
                ....*....|....
gi 20986497 372 lTRERIKEAIVAEI 385
Cdd:cd07857 320 -SMEELRDMIIEEV 332
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
55-389 8.87e-134

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: 401.08  E-value: 8.87e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYgEFKSVY 134
Cdd:cd07859   2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLPPSRR-EFKDIY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARgLCTSPAEH 214
Cdd:cd07859  81 VVFELMESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLAR-VAFNDTPT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 215 QYFMTEYVATRWYRAPELMLSLH-EYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGAER 293
Cdd:cd07859 160 AIFWTDYVATRWYRAPELCGSFFsKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDLLGTPSPETISRVRNEK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 294 VRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCAP--PFDFAFDREA 371
Cdd:cd07859 240 ARRYLSSMRKKQPVPFSQKFPNADPLALRLLERLLAFDPKDRPTAEEALADPYFKGLAKVEREPSAQPitKLEFEFERRR 319
                       330
                ....*....|....*...
gi 20986497 372 LTRERIKEAIVAEIEDFH 389
Cdd:cd07859 320 LTKEDVRELIYREILEYH 337
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
55-385 6.49e-123

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: 373.05  E-value: 6.49e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFK-HDNIIAIKDILRPTvpygEFKSV 133
Cdd:cd07852   9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKKIFDAFRNATDAQRTFREIMFLQELNdHPNIIKLLNVIRAE----NDKDI 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMESDLHQIIHSSqplTLE--HVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSP 211
Cdd:cd07852  85 YLVFEYMETDLHAVIRAN---ILEdiHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQLE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 212 AEHQY-FMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVG 290
Cdd:cd07852 162 EDDENpVLTDYVATRWYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGKPLFPGTSTLNQLEKIIEVIGRPSAEDIESIQ 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 291 AERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCA----PPFDfa 366
Cdd:cd07852 242 SPFAATMLESLPPSRPKSLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQFHNPADEPSLPgpivIPLD-- 319
                       330
                ....*....|....*....
gi 20986497 367 fDREALTRERIKEAIVAEI 385
Cdd:cd07852 320 -DNKKLTVDEYRNRLYEEI 337
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
49-388 1.25e-120

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: 367.45  E-value: 1.25e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  49 FDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYG 128
Cdd:cd07878  11 WEVPERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVFTPATSIE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMESDLHQIIhSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglc 208
Cdd:cd07878  91 NFNEVYLVTNLMGADLNNIV-KCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLAR--- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 tsPAEHQyfMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQA 288
Cdd:cd07878 167 --QADDE--MTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVGTPSPEVLKK 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 289 VGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDcAPPFDFAFD 368
Cdd:cd07878 243 ISSEHARKYIQSLPHMPQQDLKKIFRGANPLAIDLLEKMLVLDSDKRISASEALAHPYFSQYHDPEDEPE-AEPYDESPE 321
                       330       340
                ....*....|....*....|
gi 20986497 369 REALTRERIKEAIVAEIEDF 388
Cdd:cd07878 322 NKERTIEEWKELTYEEVSSF 341
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
49-388 1.07e-119

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: 365.13  E-value: 1.07e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  49 FDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYG 128
Cdd:cd07877  13 WEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMESDLHQIIhSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLC 208
Cdd:cd07877  93 EFNDVYLVTHLMGADLNNIV-KCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTD 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSpaehqyfMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQA 288
Cdd:cd07877 172 DE-------MTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAELLKK 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 289 VGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDcAPPFDFAFD 368
Cdd:cd07877 245 ISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPV-ADPYDQSFE 323
                       330       340
                ....*....|....*....|
gi 20986497 369 REALTRERIKEAIVAEIEDF 388
Cdd:cd07877 324 SRDLLIDEWKSLTYDEVISF 343
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
45-384 8.98e-117

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: 356.88  E-value: 8.98e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  45 FDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDI-LRP 123
Cdd:cd07856   2 FGTVFEITTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIfISP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 124 tvpygeFKSVYVVLDLMESDLHQIIhSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGM 203
Cdd:cd07856  82 ------LEDIYFVTELLGTDLHRLL-TSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 204 ARglCTSPAehqyfMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSP 283
Cdd:cd07856 155 AR--IQDPQ-----MTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPD 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 284 AVIQAVGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCAPPF 363
Cdd:cd07856 228 DVINTICSENTLRFVQSLPKRERVPFSEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLAPYHDPTDEPVADEKF 307
                       330       340
                ....*....|....*....|.
gi 20986497 364 DFAFDREALTRERIKEAIVAE 384
Cdd:cd07856 308 DWSFNDADLPVDTWKVMMYSE 328
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
54-390 7.08e-110

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: 340.57  E-value: 7.08e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPyGEFKSV 133
Cdd:cd07853   1 DVEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHI-DPFEEI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglCTSPAE 213
Cdd:cd07853  80 YVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLAR--VEEPDE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 214 HQYfMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSpavIQAVGA-- 291
Cdd:cd07853 158 SKH-MTQEVVTQYYRAPEILMGSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPS---LEAMRSac 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 292 ERVRAYIQSLPPRQPVPWETVY--PGADRQALSLLGRMLRFEPSARISAAAALRHPFLA----KYHD------------- 352
Cdd:cd07853 234 EGARAHILRGPHKPPSLPVLYTlsSQATHEAVHLLCRMLVFDPDKRISAADALAHPYLDegrlRYHTcmckccyttsggr 313
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 20986497 353 ---PDDEPDCAPPFDFAFDREALTRERIKEAIVAEIEDFHA 390
Cdd:cd07853 314 vytSDFEPSANPPFDDEYEKNLTSVRQVKEELHQFILEQQQ 354
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
55-347 1.69e-105

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: 325.59  E-value: 1.69e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIP--NAFDVVTNAkrTLRELKILKHFKHDNIIAIKDIlrptvpYGEFKS 132
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRldNEEEGIPST--ALREISLLKELKHPNIVKLLDV------IHTENK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMESDLHQIIHS-SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARgLCTSP 211
Cdd:cd07829  73 LYLVFEYCDQDLKKYLDKrPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLAR-AFGIP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 212 aEHQYfmTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQavGA 291
Cdd:cd07829 152 -LRTY--THEVVTLWYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQILGTPTEESWP--GV 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 292 ERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd07829 227 TKLPDYKPTFPKWPKNDLEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
49-388 1.02e-103

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: 323.39  E-value: 1.02e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  49 FDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYG 128
Cdd:cd07879  11 WELPERYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVSGD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMESDLHQIIhsSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglc 208
Cdd:cd07879  91 EFQDFYLVMPYMQTDLQKIM--GHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLAR--- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAEhqyfMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQA 288
Cdd:cd07879 166 HADAE----MTGYVVTRWYRAPEVILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGPEFVQK 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 289 VGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDcAPPFDFAFD 368
Cdd:cd07879 242 LEDKAAKSYIKSLPKYPRKDFSTLFPKASPQAVDLLEKMLELDVDKRLTATEALEHPYFDSFRDADEETE-QQPYDDSLE 320
                       330       340
                ....*....|....*....|
gi 20986497 369 REALTRERIKEAIVAEIEDF 388
Cdd:cd07879 321 NEKLSVDEWKKHIYKEVKSF 340
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
49-388 4.70e-103

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: 321.90  E-value: 4.70e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  49 FDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYG 128
Cdd:cd07880  11 WEVPDRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMESDLHQIIHSSQpLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglc 208
Cdd:cd07880  91 RFHDFYLVMPFMGTDLGKLMKHEK-LSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLAR--- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAEhqyfMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQA 288
Cdd:cd07880 167 QTDSE----MTGYVVTRWYRAPEVILNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSKEFVQK 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 289 VGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDcAPPFDFAFD 368
Cdd:cd07880 243 LQSEDAKNYVKKLPRFRKKDFRSLLPNANPLAVNVLEKMLVLDAESRITAAEALAHPYFEEFHDPEDETE-APPYDDSFD 321
                       330       340
                ....*....|....*....|
gi 20986497 369 REALTRERIKEAIVAEIEDF 388
Cdd:cd07880 322 EVDQSLEEWKRLTFTEILSF 341
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
55-385 4.34e-97

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: 305.88  E-value: 4.34e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFKSVY 134
Cdd:cd07850   2 YQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKLSRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFTPQKSLEEFQDVY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMESDLHQIIHssqpLTLEHVR--YFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSpa 212
Cdd:cd07850  82 LVMELMDANLCQVIQ----MDLDHERmsYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTS-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 213 ehqYFMTEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGaE 292
Cdd:cd07850 156 ---FMMTPYVVTRYYRAPEVILGM-GYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIEQLGTPSDEFMSRLQ-P 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 293 RVRAYIQSLPPRQPVPWETVYP------GADR-------QALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDC 359
Cdd:cd07850 231 TVRNYVENRPKYAGYSFEELFPdvlfppDSEEhnklkasQARDLLSKMLVIDPEKRISVDDALQHPYINVWYDPSEVEAP 310
                       330       340
                ....*....|....*....|....*..
gi 20986497 360 AP-PFDFAFDREALTRERIKEAIVAEI 385
Cdd:cd07850 311 PPaPYDHSIDEREHTVEEWKELIYKEV 337
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
55-347 3.03e-91

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: 287.21  E-value: 3.03e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVvtnAKRTLRELKILKHFK----HDNIIAIKDILRPtvpyGEF 130
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRH---PKAALREIKLLKHLNdvegHPNIVKLLDVFEH----RGG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVLDLMESDLHQII-HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVN-ENCELKIGDFGMARglc 208
Cdd:cd05118  74 NHLCLVFELMGMNLYELIkDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLADFGLAR--- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 tspAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPspaviqa 288
Cdd:cd05118 151 ---SFTSPPYTPYVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLGTP------- 220
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 289 vgaervrayiqslpprqpvpwetvypgadrQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd05118 221 ------------------------------EALDLLSKMLKYDPAKRITASQALAHPYF 249
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
55-347 4.13e-90

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 284.42  E-value: 4.13e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497     55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVvTNAKRTLRELKILKHFKHDNIIAIKDILRptvpygEFKSVY 134
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIK-KDRERILREIKILKKLKHPNIVRLYDVFE------DEDKLY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497    135 VVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLctspaE 213
Cdd:smart00220  74 LVMEYCEgGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQL-----D 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497    214 HQYFMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhQLQLIMMVLGTPspaviqavgaer 293
Cdd:smart00220 149 PGEKLTTFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGDD---QLLELFKKIGKP------------ 212
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 20986497    294 vrayiqslPPRQPVPWETVYPgadrQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:smart00220 213 --------KPPFPPPEWDISP----EAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
55-346 4.95e-89

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: 283.31  E-value: 4.95e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKI-----PNAFDVVtnAKRTLRELKILKHFKHDNIIAIKDIlrptvpYGE 129
Cdd:cd07841   2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIklgerKEAKDGI--NFTALREIKLLQELKHPNIIGLLDV------FGH 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDLMESDLHQIIHS-SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARgLC 208
Cdd:cd07841  74 KSNINLVFEFMETDLEKVIKDkSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLAR-SF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAEHqyfMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQa 288
Cdd:cd07841 153 GSPNRK---MTHQVVTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALGTPTEENWP- 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 289 vGAERVRAYIQsLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd07841 229 -GVTSLPDYVE-FKPFPPTPLKQIFPAASDDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
49-363 7.32e-89

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: 284.36  E-value: 7.32e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  49 FDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnafdVVTNA---KRTLRELKILKHFKHDNIIAIKDILRP-- 123
Cdd:cd07854   1 FDLGSRYMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKI-----VLTDPqsvKHALREIKIIRRLDHDNIVKVYEVLGPsg 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 124 ---TVPYG---EFKSVYVVLDLMESDLHQIIHSsQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVN-ENCEL 196
Cdd:cd07854  76 sdlTEDVGsltELNSVYIVQEYMETDLANVLEQ-GPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINtEDLVL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 197 KIGDFGMARgLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIM- 275
Cdd:cd07854 155 KIGDFGLAR-IVDPHYSHKGYLSEGLVTKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILe 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 276 --MVLGTPSPAVIQAVGAERVRAYIQSlpPRQPVpwETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDP 353
Cdd:cd07854 234 svPVVREEDRNELLNVIPSFVRNDGGE--PRRPL--RDLLPGVNPEALDFLEQILTFNPMDRLTAEEALMHPYMSCYSCP 309
                       330
                ....*....|
gi 20986497 354 DDEPDCAPPF 363
Cdd:cd07854 310 FDEPVSLHPF 319
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
51-346 8.28e-86

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: 274.38  E-value: 8.28e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  51 VGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNafdvVTNAKRtlRELKILKHFKHDNIIAIKDILrpTVPYGEF 130
Cdd:cd14137   2 VEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQ----DKRYKN--RELQIMRRLKHPNIVKLKYFF--YSSGEKK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVY--VVLDLMESDLHQIIHS----SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVN-ENCELKIGDFGM 203
Cdd:cd14137  74 DEVYlnLVMEYMPETLYRVIRHysknKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDpETGVLKLCDFGS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 204 ARGLctSPAEHQyfmTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSP 283
Cdd:cd14137 154 AKRL--VPGEPN---VSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTPTR 228
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 284 AVIQAVgaeRVRAYIQSLPPRQPVPWETVYP-GADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd14137 229 EQIKAM---NPNYTEFKFPQIKPHPWEKVFPkRTPPDAIDLLSKILVYNPSKRLTALEALAHPF 289
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
54-347 3.57e-85

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: 272.67  E-value: 3.57e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIP--NAFDVVtnAKRTLRELKILKHFK-HDNIIAIKDILrptvPYGEf 130
Cdd:cd07832   1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVAlrKLEGGI--PNQALREIKALQACQgHPYVVKLRDVF----PHGT- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 kSVYVVLDLMESDLHQIIHSSQ-PLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARgLCT 209
Cdd:cd07832  74 -GFVLVFEYMLSSLSEVLRDEErPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLAR-LFS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 210 SPAEHQYfmTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAV 289
Cdd:cd07832 152 EEDPRLY--SHQVATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRTLGTPNEKTWPEL 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 290 gAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd07832 230 -TSLPDYNKITFPESKGIRLEEIFPDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
53-347 1.53e-84

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: 271.11  E-value: 1.53e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDIlrptvpygeFKS 132
Cdd:cd07833   1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEA---------FRR 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 ---VYVVLDLMESDLHQIIHSSQP-LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLC 208
Cdd:cd07833  72 kgrLYLVFEYVERTLLELLEASPGgLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALT 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAEHqyfMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQA 288
Cdd:cd07833 152 ARPASP---LTDYVATRWYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKCLGPLPPSHQEL 228
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 289 VGAERVRAYIQSLPPRQPVPWETVYPGA-DRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd07833 229 FSSNPRFAGVAFPEPSQPESLERRYPGKvSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
55-346 1.08e-83

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: 268.66  E-value: 1.08e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKI-----PNAFDVVTnakrtLRELKILKHFKHDNIIAIKDILRPTVPYGE 129
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIrmeneKEGFPITA-----IREIKLLQKLDHPNVVRLKEIVTSKGSAKY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDLMESDLHQIIHS-SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglC 208
Cdd:cd07840  76 KGSIYMVFEYMDHDLTGLLDNpEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLAR--P 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAEHQYFmTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAviQA 288
Cdd:cd07840 154 YTKENNADY-TNRVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELCGSPTEE--NW 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 289 VGAERVRAYIQSLPPRQPVPWE-TVYPGA-DRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd07840 231 PGVSDLPWFENLKPKKPYKRRLrEVFKNViDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
53-346 5.68e-83

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: 267.17  E-value: 5.68e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPN-----AFDVVTnakrtLRELKILKHFKHDNIIAIKDIlrptVPY 127
Cdd:cd07843   5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKMekekeGFPITS-----LREINILLKLQHPNIVTVKEV----VVG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 128 GEFKSVYVVLDLMESDLHQII-HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARg 206
Cdd:cd07843  76 SNLDKIYMVMEYVEHDLKSLMeTMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAR- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 207 LCTSPAEHqyfMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPS---- 282
Cdd:cd07843 155 EYGSPLKP---YTQLVVTLWYRAPELLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLLGTPTekiw 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 283 PAVIQAVGAERVRayiqslPPRQPV-PWETVYP--GADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd07843 232 PGFSELPGAKKKT------FTKYPYnQLRKKFPalSLSDNGFDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
55-347 1.72e-81

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: 262.86  E-value: 1.72e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAF---DVVTNakrtLRELKILKHFK-HDNIIAIKDILRptvpygEF 130
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKFyswEECMN----LREVKSLRKLNeHPNIVKLKEVFR------EN 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVLDLMESDLHQII--HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLC 208
Cdd:cd07830  71 DELYFVFEYMEGNLYQLMkdRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREIR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAehqYfmTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQA 288
Cdd:cd07830 151 SRPP---Y--TDYVSTRWYRAPEILLRSTSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKICSVLGTPTKQDWPE 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 289 vGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd07830 226 -GYKLASKLGFRFPQFAPTSLHQLIPNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
46-387 7.43e-80

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: 261.12  E-value: 7.43e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  46 DVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTV 125
Cdd:cd07876  14 DSTFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQK 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 PYGEFKSVYVVLDLMESDLHQIIHssqpLTLEHVR--YFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGM 203
Cdd:cd07876  94 SLEEFQDVYLVMELMDANLCQVIH----MELDHERmsYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 204 ARGLCTSpaehqYFMTEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSP 283
Cdd:cd07876 170 ARTACTN-----FMMTPYVVTRYYRAPEVILGM-GYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIEQLGTPSA 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 284 AVIQAVgAERVRAYIQSLPPRQPVPWETVYPG------------ADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYH 351
Cdd:cd07876 244 EFMNRL-QPTVRNYVENRPQYPGISFEELFPDwifpseserdklKTSQARDLLSKMLVIDPDKRISVDEALRHPYITVWY 322
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 20986497 352 DPdDEPDCAPP--FDFAFDREALTRERIKEAIVAEIED 387
Cdd:cd07876 323 DP-AEAEAPPPqiYDAQLEEREHAIEEWKELIYKEVMD 359
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
55-347 1.12e-78

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: 255.29  E-value: 1.12e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILrptvpYGEFKsVY 134
Cdd:cd07835   1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETEDEGVPSTAIREISLLKELNHPNIVRLLDVV-----HSENK-LY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMESDLHQII--HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLcTSPA 212
Cdd:cd07835  75 LVFEFLDLDLKKYMdsSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAF-GVPV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 213 EhQYfmTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQavGAE 292
Cdd:cd07835 154 R-TY--THEVVTLWYRAPEILLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTLGTPDEDVWP--GVT 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 293 RVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd07835 229 SLPDYKPTFPKWARQDLSKVVPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
53-346 4.11e-77

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: 252.24  E-value: 4.11e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnafdVVTNAKR-----TLRELKILKHFKHDNIIAIKD--ILRPTV 125
Cdd:cd07866   8 RDYEILGKLGEGTFGEVYKARQIKTGRVVALKKI-----LMHNEKDgfpitALREIKILKKLKHPNVVPLIDmaVERPDK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 PYGEFKSVYVVLDLMESDLHQIIHS-SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA 204
Cdd:cd07866  83 SKRKRGSVYMVTPYMDHDLSGLLENpSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RGLCTSP---------AEHQYfmTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIM 275
Cdd:cd07866 163 RPYDGPPpnpkgggggGTRKY--TNLVVTRWYRPPELLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLIF 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 276 MVLGTPSPAVIQavGAervrayiQSLPPRQPVPWETVYPGA--------DRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd07866 241 KLCGTPTEETWP--GW-------RSLPGCEGVHSFTNYPRTleerfgklGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
46-385 1.58e-76

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 252.32  E-value: 1.58e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  46 DVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTV 125
Cdd:cd07874  10 DSTFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQK 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 PYGEFKSVYVVLDLMESDLHQIIHssQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd07874  90 SLEEFQDVYLVMELMDANLCQVIQ--MELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 206 GLCTSpaehqYFMTEYVATRWYRAPELMLSLHeYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAV 285
Cdd:cd07874 168 TAGTS-----FMMTPYVVTRYYRAPEVILGMG-YKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEF 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 286 IQAVgAERVRAYIQSLPPRQPVPWETVYPG----AD--------RQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDP 353
Cdd:cd07874 242 MKKL-QPTVRNYVENRPKYAGLTFPKLFPDslfpADsehnklkaSQARDLLSKMLVIDPAKRISVDEALQHPYINVWYDP 320
                       330       340       350
                ....*....|....*....|....*....|....
gi 20986497 354 dDEPDCAPP--FDFAFDREALTRERIKEAIVAEI 385
Cdd:cd07874 321 -AEVEAPPPqiYDKQLDEREHTIEEWKELIYKEV 353
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
46-388 6.33e-75

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 248.42  E-value: 6.33e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  46 DVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTV 125
Cdd:cd07875  17 DSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQK 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 PYGEFKSVYVVLDLMESDLHQIIHssqpLTLEHVR--YFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGM 203
Cdd:cd07875  97 SLEEFQDVYIVMELMDANLCQVIQ----MELDHERmsYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGL 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 204 ARGLCTSpaehqYFMTEYVATRWYRAPELMLSLHeYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSP 283
Cdd:cd07875 173 ARTAGTS-----FMMTPYVVTRYYRAPEVILGMG-YKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQLGTPCP 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 284 AVIQAVgAERVRAYIQSLPPRQPVPWETVYPG----AD--------RQALSLLGRMLRFEPSARISAAAALRHPFLAKYH 351
Cdd:cd07875 247 EFMKKL-QPTVRTYVENRPKYAGYSFEKLFPDvlfpADsehnklkaSQARDLLSKMLVIDASKRISVDEALQHPYINVWY 325
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 20986497 352 DPdDEPDCAPPF--DFAFDREALTRERIKEAIVAEIEDF 388
Cdd:cd07875 326 DP-SEAEAPPPKipDKQLDEREHTIEEWKELIYKEVMDL 363
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
55-346 2.02e-74

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: 243.95  E-value: 2.02e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTvpygefKSVY 134
Cdd:cd07860   2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTE------NKLY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMESDLHQIIHSSQP--LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR--GLCTS 210
Cdd:cd07860  76 LVFEFLHQDLKKFMDASALtgIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARafGVPVR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 211 PAEHQyfmteyVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQavG 290
Cdd:cd07860 156 TYTHE------VVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWP--G 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 291 AERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd07860 228 VTSMPDYKPSFPKWARQDFSKVVPPLDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
55-346 6.40e-74

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: 242.56  E-value: 6.40e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRtLRELKILKHFK-HDNIIAIKDIL--RPTvpygefK 131
Cdd:cd07831   1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQVNN-LREIQALRRLSpHPNILRLIEVLfdRKT------G 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQIIHS-SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCeLKIGDFGMARGLCTS 210
Cdd:cd07831  74 RLALVFELMDMNLYELIKGrKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDI-LKLADFGSCRGIYSK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 211 PAehqyfMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVG 290
Cdd:cd07831 153 PP-----YTEYISTRWYRAPECLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIHDVLGTPDAEVLKKFR 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 291 AERVRAYiqSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd07831 228 KSRHMNY--NFPSKKGTGLRKLLPNASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
55-347 1.48e-72

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: 239.10  E-value: 1.48e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKI--PNAFDVVTNAkrTLRE---LKILKHFKHDNIIAIKDILRpTVPYGE 129
Cdd:cd07838   1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVrvPLSEEGIPLS--TIREialLKQLESFEHPNVVRLLDVCH-GPRTDR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDLMESDLHQII--HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL 207
Cdd:cd07838  78 ELKLTLVFEHVDQDLATYLdkCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARIY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 CTSPAehqyfMTEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSpaviQ 287
Cdd:cd07838 158 SFEMA-----LTSVVVTLWYRAPEVLLQS-SYATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFDVIGLPS----E 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 288 AVGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd07838 228 EEWPRNSALPRSSFPSYTPRPFKSFVPEIDEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
55-346 5.51e-70

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: 231.99  E-value: 5.51e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnAFDVVTNAKRT-LRELKILKHFKHDNIIAIKDILrptvpYGEFKSV 133
Cdd:cd07836   2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEI--HLDAEEGTPSTaIREISLMKELKHENIVRLHDVI-----HTENKLM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 yVVLDLMESDLHQI--IHSSQ-PLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR--GLC 208
Cdd:cd07836  75 -LVFEYMDKDLKKYmdTHGVRgALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARafGIP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPaehqyFMTEyVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQA 288
Cdd:cd07836 154 VNT-----FSNE-VVTLWYRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGTPTESTWPG 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 289 VgaERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd07836 228 I--SQLPEYKPTFPRYPPQDLQQLFPHADPLGIDLLHRLLQLNPELRISAHDALQHPW 283
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
61-365 2.42e-69

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 232.34  E-value: 2.42e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   61 IGNGAYGVVSSARRRLTGQQVAIKKIPN---AFDVVTNAKR---------TLRELKILKHFKHDNIIAIKDIlrptvpYG 128
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAIKKVKIieiSNDVTKDRQLvgmcgihftTLRELKIMNEIKHENIMGLVDV------YV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  129 EFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLC 208
Cdd:PTZ00024  91 EGDFINLVMDIMASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRYG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  209 TSPAEHQYF----------MTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVL 278
Cdd:PTZ00024 171 YPPYSDTLSkdetmqrreeMTSKVVTLWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIFELL 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  279 GTPSPAVIQAvgAERVRAYIQsLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHpflaKYHDPDDEPd 358
Cdd:PTZ00024 251 GTPNEDNWPQ--AKKLPLYTE-FTPRKPKDLKTIFPNASDDAIDLLQSLLKLNPLERISAKEALKH----EYFKSDPLP- 322
                        330
                 ....*....|
gi 20986497  359 CAP---PFDF 365
Cdd:PTZ00024 323 CDPsqlPFNF 332
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
54-363 5.62e-69

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: 230.33  E-value: 5.62e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKipnafdVVTNAKR------TLRELKILKHFKHDNIIAIKDIlrptVPY 127
Cdd:cd07845   8 EFEKLNRIGEGTYGIVYRARDTTSGEIVALKK------VRMDNERdgipisSLREITLLLNLRHPNIVELKEV----VVG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 128 GEFKSVYVVLDLMESDLHQIIHS-SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARg 206
Cdd:cd07845  78 KHLDSIFLVMEYCEQDLASLLDNmPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLAR- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 207 LCTSPAEHqyfMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSpavi 286
Cdd:cd07845 157 TYGLPAKP---MTPKVVTLWYRAPELLLGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLLGTPN---- 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 287 qavgaERVRAYIQSLP-------PRQPVP-WETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLaKYHDPDDEPD 358
Cdd:cd07845 230 -----ESIWPGFSDLPlvgkftlPKQPYNnLKHKFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYF-KEKPLPCEPE 303

                ....*
gi 20986497 359 CAPPF 363
Cdd:cd07845 304 MMPTF 308
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
55-347 3.64e-68

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: 227.26  E-value: 3.64e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnAFDVVTNAKRT-LRELKILKHFKHDNIIAIKDILRPTvpygefKSV 133
Cdd:cd07844   2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEI--RLEHEEGAPFTaIREASLLKDLKHANIVTLHDIIHTK------KTL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMESDLHQII-HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGlcTSPA 212
Cdd:cd07844  74 TLVFEYLDTDLKQYMdDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARA--KSVP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 213 EHQYfmTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPG-KNYVHQLQLIMMVLGTPSPAVIQAVGA 291
Cdd:cd07844 152 SKTY--SNEVVTLWYRPPDVLLGSTEYSTSLDMWGVGCIFYEMATGRPLFPGsTDVEDQLHKIFRVLGTPTEETWPGVSS 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 292 -ERVRAYiqSLPPRQPVPWETVYPGADR--QALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd07844 230 nPEFKPY--SFPFYPPRPLINHAPRLDRipHGEELALKFLQYEPKKRISAAEAMKHPYF 286
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
53-346 2.09e-66

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 222.77  E-value: 2.09e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILrptvpYGEfKS 132
Cdd:PLN00009   2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVV-----HSE-KR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  133 VYVVLDLMESDLHQIIHSSQPLTLEH--VRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNE-NCELKIGDFGMAR--GL 207
Cdd:PLN00009  76 LYLVFEYLDLDLKKHMDSSPDFAKNPrlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRrTNALKLADFGLARafGI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  208 CTSPAEHQyfmteyVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQ 287
Cdd:PLN00009 156 PVRTFTHE------VVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETWP 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497  288 AVGAerVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:PLN00009 230 GVTS--LPDYKSAFPKWPPKDLATVVPTLEPAGVDLLSKMLRLDPSKRITARAALEHEY 286
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
55-346 4.14e-66

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: 222.93  E-value: 4.14e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARR--RLTGQQVAIKKIPNAFDVVTN-AKRTLRELKILKHFKHDNIIAIKDILrptVPYGEfK 131
Cdd:cd07842   2 YEIEGCIGRGTYGRVYKAKRknGKDGKEYAIKKFKGDKEQYTGiSQSACREIALLRELKHENVVSLVEVF---LEHAD-K 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQIIH--------SSQPLTlehVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV----NENCELKIG 199
Cdd:cd07842  78 SVYLLFDYAEHDLWQIIKfhrqakrvSIPPSM---VKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 200 DFGMARgLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKN---------YVHQ 270
Cdd:cd07842 155 DLGLAR-LFNAPLKPLADLDPVVVTIWYRAPELLLGARHYTKAIDIWAIGCIFAELLTLEPIFKGREakikksnpfQRDQ 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 271 LQLIMMVLGTPS----PAVI------QAVGAERVRAYIQSLPPrqpvPWETVYPGADRQALSLLGRMLRFEPSARISAAA 340
Cdd:cd07842 234 LERIFEVLGTPTekdwPDIKkmpeydTLKSDTKASTYPNSLLA----KWMHKHKKPDSQGFDLLRKLLEYDPTKRITAEE 309

                ....*.
gi 20986497 341 ALRHPF 346
Cdd:cd07842 310 ALEHPY 315
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
53-346 3.81e-63

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: 214.54  E-value: 3.81e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnafdVVTNAKR-----TLRELKILKHFKHDNIIAIKDILR-PTVP 126
Cdd:cd07865  12 SKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKV-----LMENEKEgfpitALREIKILQLLKHENVVNLIEICRtKATP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 YGEFK-SVYVVLDLMESDLHQIIhsSQPL---TLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFG 202
Cdd:cd07865  87 YNRYKgSIYLVFEFCEHDLAGLL--SNKNvkfTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 203 MARGLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPS 282
Cdd:cd07865 165 LARAFSLAKNSQPNRYTNRVVTLWYRPPELLLGERDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQHQLTLISQLCGSIT 244
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 283 PAVIQAVgaERVRAYIQSLPPRQPVPWETV---YPGADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd07865 245 PEVWPGV--DKLELFKKMELPQGQKRKVKErlkPYVKDPYALDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
53-347 7.70e-63

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: 212.95  E-value: 7.70e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDvvTNAKRT-LRELKILKHFKHDNIIAIKDILRPTvpygefK 131
Cdd:cd07871   5 ETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHE--EGAPCTaIREVSLLKNLKHANIVTLHDIIHTE------R 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQII-HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGlcTS 210
Cdd:cd07871  77 CLTLVFEYLDSDLKQYLdNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARA--KS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 211 PAEHQYfmTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVG 290
Cdd:cd07871 155 VPTKTY--SNEVVTLWYRPPDVLLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLLGTPTEETWPGVT 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 291 A-ERVRAYiqSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd07871 233 SnEEFRSY--LFPQYRAQPLINHAPRLDTDGIDLLSSLLLYETKSRISAEAALRHSYF 288
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
53-346 8.66e-63

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: 212.62  E-value: 8.66e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTvpygefKS 132
Cdd:cd07847   1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVIKKIALREIRMLKQLKHPNLVNLIEVFRRK------RK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLctSP 211
Cdd:cd07847  75 LHLVFEYCDhTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARIL--TG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 212 AEHQYfmTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGA 291
Cdd:cd07847 153 PGDDY--TDYVATRWYRAPELLVGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLGDLIPRHQQIFST 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 292 ERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd07847 231 NQFFKGLSIPEPETREPLESKFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
53-347 2.57e-62

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: 211.97  E-value: 2.57e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPnafdvVTNAKR-----TLRELKILKHFKHDNIIAIKDILRPTVPY 127
Cdd:cd07864   7 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVR-----LDNEKEgfpitAIREIKILRQLNHRSVVNLKEIVTDKQDA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 128 GEFK----SVYVVLDLMESDLHQIIHSSQ-PLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFG 202
Cdd:cd07864  82 LDFKkdkgAFYLVFEYMDHDLMGLLESGLvHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 203 MARglcTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPS 282
Cdd:cd07864 162 LAR---LYNSEESRPYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPC 238
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 283 PA----VIQAVG----------AERVRAYIQSLPprqpvpwetvypgadRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd07864 239 PAvwpdVIKLPYfntmkpkkqyRRRLREEFSFIP---------------TPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
55-346 1.09e-61

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: 209.60  E-value: 1.09e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFD---VVTNAkrtLRELKILKHFKHDNIIAIKDILrptvpYGEfK 131
Cdd:cd07839   2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDdegVPSSA---LREICLLKELKHKNIVRLYDVL-----HSD-K 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQIIHSSQPlTLEH--VRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL-- 207
Cdd:cd07839  73 KLTLVFEYCDQDLKKYFDSCNG-DIDPeiVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFgi 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 ---CTSpAEhqyfmteyVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEML-ARRQLFPGKNYVHQLQLIMMVLGTPSp 283
Cdd:cd07839 152 pvrCYS-AE--------VVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELAnAGRPLFPGNDVDDQLKRIFRLLGTPT- 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 284 aviqavgaERVRAYIQSLPPRQPVP-------WETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd07839 222 --------EESWPGVSKLPDYKPYPmypattsLVNVVPKLNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
53-347 2.00e-61

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: 209.47  E-value: 2.00e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnAFDVVTNAKRT-LRELKILKHFKHDNIIAIKDILRPTvpygefK 131
Cdd:cd07873   2 ETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEI--RLEHEEGAPCTaIREVSLLKDLKHANIVTLHDIIHTE------K 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQIIHS-SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGlcTS 210
Cdd:cd07873  74 SLTLVFEYLDKDLKQYLDDcGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARA--KS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 211 PAEHQYfmTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPS----PAVI 286
Cdd:cd07873 152 IPTKTY--SNEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRILGTPTeetwPGIL 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 287 QavgAERVRAYiqSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd07873 230 S---NEEFKSY--NYPKYRADALHNHAPRLDSDGADLLSKLLQFEGRKRISAEEAMKHPYF 285
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
53-346 2.34e-61

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: 208.82  E-value: 2.34e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTvpygefKS 132
Cdd:cd07846   1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRK------KR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLcTSP 211
Cdd:cd07846  75 WYLVFEFVDhTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTL-AAP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 212 AEhqyFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGA 291
Cdd:cd07846 154 GE---VYTDYVATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKCLGNLIPRHQELFQK 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 292 ERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd07846 231 NPLFAGVRLPEVKEVEPLERRYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
54-347 4.63e-61

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: 208.04  E-value: 4.63e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRptvpygEFKSV 133
Cdd:cd07861   1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLM------QENRL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMESDLHQ---IIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR--GLC 208
Cdd:cd07861  75 YLVFEFLSMDLKKyldSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARafGIP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAEHQyfmteyVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQa 288
Cdd:cd07861 155 VRVYTHE------VVTLWYRAPEVLLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILGTPTEDIWP- 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 289 vGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd07861 228 -GVTSLPDYKNTFPKWKKGSLRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
53-346 3.80e-58

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: 200.45  E-value: 3.80e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIaIKDILRPTVPYGEFKS 132
Cdd:cd07837   1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEEGVPSTALREVSLLQMLSQSIYI-VRLLDVEHVEENGKPL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMESDLHQIIHS-----SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNE--NCeLKIGDFGMAR 205
Cdd:cd07837  80 LYLVFEYLDTDLKKFIDSygrgpHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKqkGL-LKIADLGLGR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 206 GLcTSPAEHqyfMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAV 285
Cdd:cd07837 159 AF-TIPIKS---YTHEIVTLWYRAPEVLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLLGTPNEEV 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 286 IQavGAERVRAYiQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd07837 235 WP--GVSKLRDW-HEYPQWKPQDLSRAVPDLEPEGVDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
53-347 1.23e-57

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: 199.45  E-value: 1.23e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnAFDVVTNAKRT-LRELKILKHFKHDNIIAIKDILRPTvpygefK 131
Cdd:cd07872   6 ETYIKLEKLGEGTYATVFKGRSKLTENLVALKEI--RLEHEEGAPCTaIREVSLLKDLKHANIVTLHDIVHTD------K 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQIIHS-SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGlcTS 210
Cdd:cd07872  78 SLTLVFEYLDKDLKQYMDDcGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARA--KS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 211 PAEHQYfmTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVG 290
Cdd:cd07872 156 VPTKTY--SNEVVTLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPTEETWPGIS 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 291 A-ERVRAYiqSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd07872 234 SnDEFKNY--NFPKYKPQPLINHAPRLDTEGIELLTKFLQYESKKRISAEEAMKHAYF 289
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
55-347 2.13e-57

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: 198.92  E-value: 2.13e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdVVTNAKRTLR----ELKILKHFKH------DNIIAIKDilrpt 124
Cdd:cd14210  15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIK-------IIRNKKRFHQqalvEVKILKHLNDndpddkHNIVRYKD----- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 125 vpYGEFKS-VYVVLDLMESDLHQIIHSS--QPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSN-LLVNEN-CELKIG 199
Cdd:cd14210  83 --SFIFRGhLCIVFELLSINLYELLKSNnfQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENiLLKQPSkSSIKVI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 200 DFGMArglCTspaEHQYfMTEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLG 279
Cdd:cd14210 161 DFGSS---CF---EGEK-VYTYIQSRFYRAPEVILGL-PYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIMEVLG 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 280 TPSPAVIQAvgAERVRAYIQS---LPPRQPVPWETVYPG----------ADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd14210 233 VPPKSLIDK--ASRRKKFFDSngkPRPTTNSKGKKRRPGskslaqvlkcDDPSFLDFLKKCLRWDPSERMTPEEALQHPW 310

                .
gi 20986497 347 L 347
Cdd:cd14210 311 I 311
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
54-347 1.16e-56

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: 195.95  E-value: 1.16e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnafDVVTNAK----RTLRE---LKILKHFKHDNIIAIKDILRPTVP 126
Cdd:cd07863   1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALKSV----RVQTNEDglplSTVREvalLKRLEAFDHPNIVRLMDVCATSRT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 YGEFKsVYVVLDLMESDLHQIIHSSQP--LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA 204
Cdd:cd07863  77 DRETK-VTLVFEHVDQDLRTYLDKVPPpgLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RglctsPAEHQYFMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSpa 284
Cdd:cd07863 156 R-----IYSCQMALTPVVVTLWYRAPEVLLQ-STYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPP-- 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 285 viQAVGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd07863 228 --EDDWPRDVTLPRGAFSPRGPRPVQSVVPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
43-346 4.88e-55

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: 191.99  E-value: 4.88e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  43 RSFDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNafdvvTNAKRTLRELKILKHFK-HDNIIAIKDIL 121
Cdd:cd14132   8 ENLNVEWGSQDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKP-----VKKKKIKREIKILQNLRgGPNIVKLLDVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 122 RptvpYGEFKSVYVVLDLMES-DLHQIIHSsqpLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENC-ELKIG 199
Cdd:cd14132  83 K----DPQSKTPSLIFEYVNNtDFKTLYPT---LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKrKLRLI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 200 DFGMArglctspaEHQYFMTEY---VATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQ-LFPGKNYVHQLQLIM 275
Cdd:cd14132 156 DWGLA--------EFYHPGQEYnvrVASRYYKGPELLVDYQYYDYSLDMWSLGCMLASMIFRKEpFFHGHDNYDQLVKIA 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 276 MVLGTpspaviqavgaERVRAYIQ----SLPPR--------QPVPWETVYPG-----ADRQALSLLGRMLRFEPSARISA 338
Cdd:cd14132 228 KVLGT-----------DDLYAYLDkygiELPPRlndilgrhSKKPWERFVNSenqhlVTPEALDLLDKLLRYDHQERITA 296

                ....*...
gi 20986497 339 AAALRHPF 346
Cdd:cd14132 297 KEAMQHPY 304
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
55-379 4.59e-54

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 193.71  E-value: 4.59e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKipnafdVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFKSVY 134
Cdd:PTZ00036  68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIKK------VLQDPQYKNRELLIMKNLNHINIIFLKDYYYTECFKKNEKNIF 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  135 --VVLDLMESDLHQII----HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE-LKIGDFGMARGL 207
Cdd:PTZ00036 142 lnVVMEFIPQTVHKYMkhyaRNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGSAKNL 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  208 CTSPAEhqyfmTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQ 287
Cdd:PTZ00036 222 LAGQRS-----VSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQVLGTPTEDQLK 296
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  288 AVGAERVRAyiqSLPPRQPVPWETVYP-GADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDP--------DDEPD 358
Cdd:PTZ00036 297 EMNPNYADI---KFPDVKPKDLKKVFPkGTPDDAINFISQFLKYEPLKRLNPIEALADPFFDDLRDPciklpkyiDKLPD 373
                        330       340
                 ....*....|....*....|.
gi 20986497  359 CappFDFafdrealTRERIKE 379
Cdd:PTZ00036 374 L---FNF-------CDAEIKE 384
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
55-346 2.42e-53

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: 185.76  E-value: 2.42e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDIlrptvpYGEFKSVY 134
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEV------FEDDKNLY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV---NENCELKIGDFGMARGLcts 210
Cdd:cd05117  76 LVMELCTGgELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKIF--- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 211 paEHQYFMTEYVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMvlgtpspaviqavg 290
Cdd:cd05117 153 --EEGEKLKTVCGTPYYVAPE-VLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILK-------------- 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 291 aervRAYiqSLPPRqpvPWETVYPgadrQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd05117 216 ----GKY--SFDSP---EWKNVSE----EAKDLIKRLLVVDPKKRLTAAEALNHPW 258
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
61-255 6.57e-53

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: 182.86  E-value: 6.57e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAfDVVTNAKRTLRELKILKHFKHDNIIAIKDIlrptvpYGEFKSVYVVLDLM 140
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKE-KLKKLLEELLREIEILKKLNHPNIVKLYDV------FETENFLYLVMEYC 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 ES-DLHQIIHS-SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARgLCTSPAEHQYFM 218
Cdd:cd00180  74 EGgSLKDLLKEnKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAK-DLDSDDSLLKTT 152
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20986497 219 TEYvaTRWYRAPELMLSLHEYTQAIDLWSVGCIFGEM 255
Cdd:cd00180 153 GGT--TPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
53-345 1.13e-52

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: 185.20  E-value: 1.13e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRptvpygEFKS 132
Cdd:cd07848   1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFR------RRGK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMESDLHQIIHSSQPLTL-EHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLcTSP 211
Cdd:cd07848  75 LYLVFEYVEKNMLELLEEMPNGVPpEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNL-SEG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 212 AEHQYfmTEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGtPSPAVIQAVGA 291
Cdd:cd07848 154 SNANY--TEYVATRWYRSPELLLGA-PYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLG-PLPAEQMKLFY 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 292 ERVRAYIQSLPP-RQPVPWETVYPGA-DRQALSLLGRMLRFEPSARISAAAALRHP 345
Cdd:cd07848 230 SNPRFHGLRFPAvNHPQSLERRYLGIlSGVLLDLMKNLLKLNPTDRYLTEQCLNHP 285
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
55-347 1.25e-51

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: 182.08  E-value: 1.25e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIP-NAFDVVTNAkrTLRELKILKHFKHDNIIAIKDILRPTvpygefKSV 133
Cdd:cd07870   2 YLNLEKLGEGSYATVYKGISRINGQLVALKVISmKTEEGVPFT--AIREASLLKGLKHANIVLLHDIIHTK------ETL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMESDLHQIIhSSQPLTLE--HVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglcTSP 211
Cdd:cd07870  74 TFVFEYMHTDLAQYM-IQHPGGLHpyNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLAR---AKS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 212 AEHQYFMTEyVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPG-KNYVHQLQLIMMVLGTPSPAVIQAVG 290
Cdd:cd07870 150 IPSQTYSSE-VVTLWYRPPDVLLGATDYSSALDIWGAGCIFIEMLQGQPAFPGvSDVFEQLEKIWTVLGVPTEDTWPGVS 228
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 291 A-ERVRAYIQSLPPRQP--VPWETVypGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd07870 229 KlPNYKPEWFLPCKPQQlrVVWKRL--SRPPKAEDLASQMLMMFPKDRISAQDALLHPYF 286
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
55-346 6.81e-49

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: 173.09  E-value: 6.81e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTvpygefKSVY 134
Cdd:cd14003   2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETE------NKIY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFgmarGLCTSPAE 213
Cdd:cd14003  76 LVMEYASGgELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDF----GLSNEFRG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 214 HQYFMTeYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMmvlgtpspaviqavgaer 293
Cdd:cd14003 152 GSLLKT-FCGTPAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKIL------------------ 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 20986497 294 vrAYIQSLPPRQPVpwetvypgadrQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd14003 213 --KGKYPIPSHLSP-----------DARDLIRRMLVVDPSKRITIEEILNHPW 252
Pkinase pfam00069
Protein kinase domain;
55-347 1.18e-48

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 171.27  E-value: 1.18e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497    55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDIlrptvpYGEFKSVY 134
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDA------FEDKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   135 VVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLkymhsaqvihrdlkpsnllvnencelkigdfgmarglctspaE 213
Cdd:pfam00069  75 LVLEYVEgGSLFDLLSEKGAFSEREAKFIMKQILEGL------------------------------------------E 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   214 HQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMmvlgtpspaviqavgaer 293
Cdd:pfam00069 113 SGSSLTTFVGTPWYMAPEV-LGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELII------------------ 173
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 20986497   294 vrayiqslppRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:pfam00069 174 ----------DQPYAFPELPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
55-347 1.27e-48

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: 172.84  E-value: 1.27e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAkrtLRELKILKHF-KHD-----NIIAIKDilrptvpYG 128
Cdd:cd14133   1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQS---LDEIRLLELLnKKDkadkyHIVRLKD-------VF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKS-VYVVLDLMESDLHQIIH--SSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV--NENCELKIGDFGM 203
Cdd:cd14133  71 YFKNhLCIVFELLSQNLYEFLKqnKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLasYSRCQIKIIDFGS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 204 ArglCTSPaEHQYFmteYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSP 283
Cdd:cd14133 151 S---CFLT-QRLYS---YIQSRYYRAPEVILGL-PYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPA 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 284 AVIQAVGAErvrayiqslpprqpvpwetvypgaDRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14133 223 HMLDQGKAD------------------------DELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
54-346 3.75e-48

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: 172.52  E-value: 3.75e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARR-RLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKH---FKHDNIIAIKDILRPTVPYGE 129
Cdd:cd07862   2 QYECVAEIGEGAYGKVFKARDlKNGGRFVALKRVRVQTGEEGMPLSTIREVAVLRHletFEHPNVVRLFDVCTVSRTDRE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKsVYVVLDLMESDLHQIIHSS-QP-LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARgl 207
Cdd:cd07862  82 TK-LTLVFEHVDQDLTTYLDKVpEPgVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLAR-- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 ctsPAEHQYFMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPA-VI 286
Cdd:cd07862 159 ---IYSFQMALTSVVVTLWYRAPEVLLQ-SSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIGLPGEEdWP 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 287 QAVGAERvrayiQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd07862 235 RDVALPR-----QAFHSKSAQPIEKFVTDIDELGKDLLLKCLTFNPAKRISAYSALSHPY 289
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
49-348 1.81e-47

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: 171.03  E-value: 1.81e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  49 FDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKrTLRELKILKHFKHDNIIAIKDILRPTvpyg 128
Cdd:cd07869   1 FGKADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFT-AIREASLLKGLKHANIVLLHDIIHTK---- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 efKSVYVVLDLMESDLHQIIhSSQP--LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARG 206
Cdd:cd07869  76 --ETLTLVFEYVHTDLCQYM-DKHPggLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 207 lcTSPAEHQYfmTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPG-KNYVHQLQLIMMVLGTPSpav 285
Cdd:cd07869 153 --KSVPSHTY--SNEVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGmKDIQDQLERIFLVLGTPN--- 225
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 286 iqavgaERVRAYIQSLPPRQPVPWeTVYPGAD-RQALS----------LLGRMLRFEPSARISAAAALRHPFLA 348
Cdd:cd07869 226 ------EDTWPGVHSLPHFKPERF-TLYSPKNlRQAWNklsyvnhaedLASKLLQCFPKNRLSAQAALSHEYFS 292
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
55-343 9.52e-47

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: 167.38  E-value: 9.52e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKI-PNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDilrptvpYGEF-KS 132
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLrPELAEDEEFRERFLREARALARLSHPNIVRVYD-------VGEDdGR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLctsP 211
Cdd:cd14014  75 PYIVMEYVEGgSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARAL---G 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 212 AEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMmvlgtpspaviqavga 291
Cdd:cd14014 152 DSGLTQTGSVLGTPAYMAPEQ-ARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHL---------------- 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 20986497 292 ervrayiqslpPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALR 343
Cdd:cd14014 215 -----------QEAPPPPSPLNPDVPPALDAIILRALAKDPEERPQSAAELL 255
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
61-346 1.45e-45

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: 163.93  E-value: 1.45e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKkipnAFDVVTNAKRTL----RELKILKHFKHDNIIAIKDILRPTvpygefKSVYVV 136
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIK----EISRKKLNKKLQenleSEIAILKSIKHPNIVRLYDVQKTE------DFIYLV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 137 LDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV---NENCELKIGDFGMARGL----- 207
Cdd:cd14009  71 LEYCAGgDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGFARSLqpasm 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 ----CTSPaehqyfmteyvatrWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLImmvlgtpsp 283
Cdd:cd14009 151 aetlCGSP--------------LYMAPE-ILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNI--------- 206
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 284 aviqavgaERVRAYIQSLPPRQPVPwetvypgadrQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd14009 207 --------ERSDAVIPFPIAAQLSP----------DCKDLLRRLLRRDPAERISFEEFFAHPF 251
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
59-347 1.70e-45

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: 163.85  E-value: 1.70e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRptvpygEFKSVYVVLD 138
Cdd:cd06606   6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTER------TENTLNIFLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 139 LM-ESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR---GLCTSPAEH 214
Cdd:cd06606  80 YVpGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKrlaEIATGEGTK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 215 Q-----YFMteyvatrwyrAPELMlSLHEYTQAIDLWSVGCIFGEMLARRQLFPgkNYVHQLQLIMMVLGTPSPAVIQAv 289
Cdd:cd06606 160 SlrgtpYWM----------APEVI-RGEGYGRAADIWSLGCTVIEMATGKPPWS--ELGNPVAALFKIGSSGEPPPIPE- 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 290 gaervrayiqSLPPrqpvpwetvypgadrQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd06606 226 ----------HLSE---------------EAKDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
55-347 2.68e-45

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: 163.40  E-value: 2.68e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpNAFDVVTNAKR-TLRELKILKHFKHDNIIAIKDilrptvPYGEFKSV 133
Cdd:cd08215   2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEI-DLSNMSEKEREeALNEVKLLSKLKHPNIVKYYE------SFEENGKL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMES-DLHQII----HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLc 208
Cdd:cd08215  75 CIVMEYADGgDLAQKIkkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVL- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 tspAEHQYFMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhQLQLIMMVlgtpspaviqa 288
Cdd:cd08215 154 ---ESTTDLAKTVVGTPYYLSPELCEN-KPYNYKSDIWALGCVLYELCTLKHPFEANN---LPALVYKI----------- 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 289 vgaerVRAYIQSLPPRqpvpwetvYPgadrQAL-SLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd08215 216 -----VKGQYPPIPSQ--------YS----SELrDLVNSMLQKDPEKRPSANEILSSPFI 258
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
55-347 3.86e-45

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 165.65  E-value: 3.86e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdVVTNAKR----TLRELKILKHF-KHD-----NIIAIKDilrpt 124
Cdd:cd14225  45 YEILEVIGKGSFGQVVKALDHKTNEHVAIK-------IIRNKKRfhhqALVEVKILDALrRKDrdnshNVIHMKE----- 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 125 vpYGEFKS-VYVVLDLMESDLHQII--HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNE--NCELKIG 199
Cdd:cd14225 113 --YFYFRNhLCITFELLGMNLYELIkkNNFQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQrgQSSIKVI 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 200 DFGmarglcTSPAEHQYFMTeYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLG 279
Cdd:cd14225 191 DFG------SSCYEHQRVYT-YIQSRFYRSPEVILG-LPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEVLG 262
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 280 TPSPAVIQAvgAERVRAYIQSL-PPRQPV--PWETVYPGA----------DRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd14225 263 LPPPELIEN--AQRRRLFFDSKgNPRCITnsKGKKRRPNSkdlasalktsDPLFLDFIRRCLEWDPSKRMTPDEALQHEW 340

                .
gi 20986497 347 L 347
Cdd:cd14225 341 I 341
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
53-347 7.87e-44

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 158.95  E-value: 7.87e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNafdVVTNAK--RTLR-ELKILKHFKHDNIIAIKDilrptvPYGE 129
Cdd:cd14002   1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPK---RGKSEKelRNLRqEIEILRKLNHPNIIEMLD------SFET 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLct 209
Cdd:cd14002  72 KKEFVVVTEYAQGELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAM-- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 210 spAEHQYFMTEYVATRWYRAPELmlsLHE--YTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMmvlgtpspaviq 287
Cdd:cd14002 150 --SCNTLVLTSIKGTPLYMAPEL---VQEqpYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIV------------ 212
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 288 avgaervrayiqslppRQPVPW-ETVYPgadrQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14002 213 ----------------KDPVKWpSNMSP----EFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
53-347 3.65e-42

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 157.10  E-value: 3.65e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDN---IIAIKDilrptvpYGE 129
Cdd:cd14226  13 DRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTENkyyIVRLKR-------HFM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKS-VYVVLDLMESDLHQIIHSS--QPLTLEHVRYFLYQLLRGLKYMHSA--QVIHRDLKPSN-LLVNEN-CELKIGDFG 202
Cdd:cd14226  86 FRNhLCLVFELLSYNLYDLLRNTnfRGVSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPENiLLCNPKrSAIKIIDFG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 203 MArglCTsPAEHQYfmtEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPS 282
Cdd:cd14226 166 SS---CQ-LGQRIY---QYIQSRFYRSPEVLLGL-PYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGMPP 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 283 PAVIQAvgAERVRAYIQSLPPRQPVP------WETVYPGADR----------------------------QALSLLGRML 328
Cdd:cd14226 238 VHMLDQ--APKARKFFEKLPDGTYYLkktkdgKKYKPPGSRKlheilgvetggpggrragepghtvedylKFKDLILRML 315
                       330
                ....*....|....*....
gi 20986497 329 RFEPSARISAAAALRHPFL 347
Cdd:cd14226 316 DYDPKTRITPAEALQHSFF 334
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
53-347 3.91e-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: 154.86  E-value: 3.91e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAF------DVVTNAKRTLRELKILKHFKHDNIIAIKDILrpTVP 126
Cdd:cd14084   6 KKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKftigsrREINKPRNIETEIEILKKLSHPCIIKIEDFF--DAE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 ygefKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV---NENCELKIGDFG 202
Cdd:cd14084  84 ----DDYYIVLELMEGgELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 203 MARGLctspaEHQYFMTEYVATRWYRAPELMLS--LHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhqlqlimmvlgT 280
Cdd:cd14084 160 LSKIL-----GETSLMKTLCGTPTYLAPEVLRSfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEY-------------T 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 281 PSPAVIQAVGAErvRAYIQSlpprqpvPWETVypgaDRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14084 222 QMSLKEQILSGK--YTFIPK-------AWKNV----SEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
51-344 1.50e-41

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 159.02  E-value: 1.50e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  51 VGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKI-PNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDilrptvpYGE 129
Cdd:COG0515   5 LLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLrPELAADPEARERFRREARALARLNHPNIVRVYD-------VGE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSV-YVVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL 207
Cdd:COG0515  78 EDGRpYLVMEYVEgESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 CTSPAEHQYFMteyVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhQLQLIMMVLgtpspaviq 287
Cdd:COG0515 158 GGATLTQTGTV---VGTPGYMAPEQARG-EPVDPRSDVYSLGVTLYELLTGRPPFDGDS---PAELLRAHL--------- 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 288 avgaervrayiqslpPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRH 344
Cdd:COG0515 222 ---------------REPPPPPSELRPDLPPALDAIVLRALAKDPEERYQSAAELAA 263
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
54-347 1.81e-41

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: 152.36  E-value: 1.81e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPnafdVVTNAKRT--LRELKILKHFKHDNIIAIkdilrptvpYGEF- 130
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKIN----LESKEKKEsiLNEIAILKKCKHPNIVKY---------YGSYl 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 --KSVYVVLDLMES-DLHQIIHS-SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARG 206
Cdd:cd05122  68 kkDELWIVMEFCSGgSLKDLLKNtNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQ 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 207 LCTSPAEHqyfmtEYVATRWYRAPELMLSLHeYTQAIDLWSVGCIFGEMLARRQLFPgknyvhqlQLIMMvlgtpspavi 286
Cdd:cd05122 148 LSDGKTRN-----TFVGTPYWMAPEVIQGKP-YGFKADIWSLGITAIEMAEGKPPYS--------ELPPM---------- 203
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 287 qavgaeRVRAYIQSLPP---RQPVPWETVYpgadrqaLSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd05122 204 ------KALFLIATNGPpglRNPKKWSKEF-------KDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
53-347 3.16e-40

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 148.91  E-value: 3.16e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLT-------GQQVAIKKIpnafdVVTN-AKRTLRELKILKHFK-HDNIIAIKDILRp 123
Cdd:cd14019   1 NKYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHI-----YPTSsPSRILNELECLERLGgSNNVSGLITAFR- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 124 tvpYGEfkSVYVVLDLME-SDLHQIIHSsqpLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNEncELKIG--- 199
Cdd:cd14019  75 ---NED--QVVAVLPYIEhDDFRDFYRK---MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNR--ETGKGvlv 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 200 DFGMARGLCTSPAEHqyfmTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEML-ARRQLFPGKNYVHQLQLIMMVL 278
Cdd:cd14019 145 DFGLAQREEDRPEQR----APRAGTRGFRAPEVLFKCPHQTTAIDIWSAGVILLSILsGRFPFFFSSDDIDALAEIATIF 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 279 GTPSpaviqavgaervrayiqslpprqpvpwetvypgadrqALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14019 221 GSDE-------------------------------------AYDLLDKLLELDPSKRITAEEALKHPFF 252
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
54-347 1.86e-39

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: 146.47  E-value: 1.86e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNA----FDVVTNAKRtlrELKILKHFKHDNIIAIkdilrptvpYGE 129
Cdd:cd14007   1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSqlqkSGLEHQLRR---EIEIQSHLRHPNILRL---------YGY 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 F---KSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd14007  69 FedkKRIYLILEYAPNgELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSV 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 206 GLCTSPAehqyfMTeYVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYvhqlqlimmvlgtpspav 285
Cdd:cd14007 149 HAPSNRR-----KT-FCGTLDYLPPE-MVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSH------------------ 203
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497 286 iqavgaERVRAYIQSLPPRQPvpwETVYPGADrqalSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14007 204 ------QETYKRIQNVDIKFP---SSVSPEAK----DLISKLLQKDPSKRLSLEQVLNHPWI 252
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
53-351 7.28e-39

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: 145.43  E-value: 7.28e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpNAFDVVTNAKRTLRELKILKHFKHDNIIAIkdilrptvpYGEF-- 130
Cdd:cd06623   1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKKI-HVDGDEEFRKQLLRELKTLRSCESPYVVKC---------YGAFyk 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 -KSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHS-AQVIHRDLKPSNLLVNENCELKIGDFGMARGL 207
Cdd:cd06623  71 eGEISIVLEYMDGgSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGEVKIADFGISKVL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 CTSPAEHQyfmtEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPaviq 287
Cdd:cd06623 151 ENTLDQCN----TFVGTVTYMSPERIQG-ESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAICDGPPP---- 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 288 avgaervrayiqSLPPRQpvpwetvypgADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYH 351
Cdd:cd06623 222 ------------SLPAEE----------FSPEFRDFISACLQKDPKKRPSAAELLQHPFIKKAD 263
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
55-347 2.90e-38

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


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 146.82  E-value: 2.90e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdVVTNAKRTLR----ELKILKHFK-HD-----NIIAIKDilrpt 124
Cdd:cd14224  67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALK-------MVRNEKRFHRqaaeEIRILEHLKkQDkdntmNVIHMLE----- 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 125 vpYGEFKS-VYVVLDLMESDLHQIIHSS--QPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE--LKIG 199
Cdd:cd14224 135 --SFTFRNhICMTFELLSMNLYELIKKNkfQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVI 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 200 DFGmarglcTSPAEHQYFMTeYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLG 279
Cdd:cd14224 213 DFG------SSCYEHQRIYT-YIQSRFYRAPEVILG-ARYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIELLG 284
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 280 TPSPAVIQAvgAERVRAYIQS-----------LP------------------PRQPVPWETVYPGADRQA-LSLLGRMLR 329
Cdd:cd14224 285 MPPQKLLET--SKRAKNFISSkgypryctvttLPdgsvvlnggrsrrgkmrgPPGSKDWVTALKGCDDPLfLDFLKRCLE 362
                       330
                ....*....|....*...
gi 20986497 330 FEPSARISAAAALRHPFL 347
Cdd:cd14224 363 WDPAARMTPSQALRHPWL 380
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
53-347 6.00e-38

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: 144.63  E-value: 6.00e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdVVTNAKR----TLRELKILKHFKHD------NIIAIKDilr 122
Cdd:cd14134  12 NRYKILRLLGEGTFGKVLECWDRKRKRYVAVK-------IIRNVEKyreaAKIEIDVLETLAEKdpngksHCVQLRD--- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 123 ptvpYGEFKS-VYVVLDLMESDLHQII--HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSN-LLVN------- 191
Cdd:cd14134  82 ----WFDYRGhMCIVFELLGPSLYDFLkkNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENiLLVDsdyvkvy 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 192 -----------ENCELKIGDFGMArglctsPAEHQYFMTeYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQ 260
Cdd:cd14134 158 npkkkrqirvpKSTDIKLIDFGSA------TFDDEYHSS-IVSTRHYRAPEVILGL-GWSYPCDVWSIGCILVELYTGEL 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 261 LFPGKNYVHQLQLIMMVLGTPSPAVIQAVGAER-----------------VRAYIQSLpPRQPVPWETVYPGADRQALSL 323
Cdd:cd14134 230 LFQTHDNLEHLAMMERILGPLPKRMIRRAKKGAkyfyfyhgrldwpegssSGRSIKRV-CKPLKRLMLLVDPEHRLLFDL 308
                       330       340
                ....*....|....*....|....
gi 20986497 324 LGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14134 309 IRKMLEYDPSKRITAKEALKHPFF 332
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
54-347 8.37e-38

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: 142.29  E-value: 8.37e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnAFDVVTNAKRTL--RELKILKHFKHDNIIAIKD--ILRPTvpyge 129
Cdd:cd08217   1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEI--DYGKMSEKEKQQlvSEVNILRELKHPNIVRYYDriVDRAN----- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 fKSVYVVldlME----SDLHQIIHSS----QPLTLEHVRYFLYQLLRGLKYMH-----SAQVIHRDLKPSNLLVNENCEL 196
Cdd:cd08217  74 -TTLYIV---MEycegGDLAQLIKKCkkenQYIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDNNV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 197 KIGDFGMARGLctspAEHQYFMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhQLQLIMM 276
Cdd:cd08217 150 KLGDFGLARVL----SHDSSFAKTYVGTPYYMSPELLNE-QSYDEKSDIWSLGCLIYELCALHPPFQAAN---QLELAKK 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 277 VlgtpspaviqAVGAERvrayiqSLPPRqpvpwetvYpgaDRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd08217 222 I----------KEGKFP------RIPSR--------Y---SSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
61-270 3.65e-37

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: 139.60  E-value: 3.65e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRltGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYgefksvYVVLDLM 140
Cdd:cd13999   1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPL------CIVTEYM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 E-SDLHQIIHS-SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglctSPAEHQYFM 218
Cdd:cd13999  73 PgGSLYDLLHKkKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSR----IKNSTTEKM 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 20986497 219 TEYVAT-RWyRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQ 270
Cdd:cd13999 149 TGVVGTpRW-MAPEVLRGE-PYTEKADVYSFGIVLWELLTGEVPFKELSPIQI 199
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
55-347 6.00e-37

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: 141.59  E-value: 6.00e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQ-VAIKKIPNAfDVVTnaKRTLRELKILK------------------HFKHDNII 115
Cdd:cd14135   2 YRVYGYLGKGVFSNVVRARDLARGNQeVAIKIIRNN-ELMH--KAGLKELEILKklndadpddkkhcirllrHFEHKNHL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 116 AIkdilrptvpygefksvyvVLDLMESDLHQIIH---SSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNE 192
Cdd:cd14135  79 CL------------------VFESLSMNLREVLKkygKNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNE 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 193 NCE-LKIGDFGMArglctSPAEHQYfMTEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQL 271
Cdd:cd14135 141 KKNtLKLCDFGSA-----SDIGENE-ITPYLVSRFYRAPEIILGL-PYDYPIDMWSVGCTLYELYTGKILFPGKTNNHML 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 272 QLIMMVLGTPSPAVIQ---------------------AVGAERVRAYIQSLPPRQPVPWETV----YPGADR----QALS 322
Cdd:cd14135 214 KLMMDLKGKFPKKMLRkgqfkdqhfdenlnfiyrevdKVTKKEVRRVMSDIKPTKDLKTLLIgkqrLPDEDRkkllQLKD 293
                       330       340
                ....*....|....*....|....*
gi 20986497 323 LLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14135 294 LLDKCLMLDPEKRITPNEALQHPFI 318
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
55-348 1.97e-36

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: 138.11  E-value: 1.97e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDvvtNAKRTLRELKILKHFKHDNIIAIkdilrptvpYGEF---K 131
Cdd:cd06614   2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQ---NKELIINEILIMKECKHPNIVDY---------YDSYlvgD 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMES----DLhqIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL 207
Cdd:cd06614  70 ELWVVMEYMDGgsltDI--ITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 cTSPAEHQYFMteyVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLArrqlfpgknyvhqlqlimmvlGTP-----S 282
Cdd:cd06614 148 -TKEKSKRNSV---VGTPYWMAPEVIKR-KDYGPKVDIWSLGIMCIEMAE---------------------GEPpyleeP 201
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 283 PAviqavgaeRVRAYI-QSLPPRQPVPWetvypGADRQALSLLGRMLRFEPSARISAAAALRHPFLA 348
Cdd:cd06614 202 PL--------RALFLItTKGIPPLKNPE-----KWSPEFKDFLNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
54-347 2.87e-36

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: 137.36  E-value: 2.87e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRptvpygEFKSV 133
Cdd:cd06627   1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVK------TKDSL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLctsPA 212
Cdd:cd06627  75 YIILEYVENgSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKL---NE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 213 EHQYfMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLArrqlfpGKNYVHQLQlimmvlgtPSPAVIQAVGAe 292
Cdd:cd06627 152 VEKD-ENSVVGTPYWMAPEV-IEMSGVTTASDIWSVGCTVIELLT------GNPPYYDLQ--------PMAALFRIVQD- 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 293 rvrayiqslpPRQPVPwetvyPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd06627 215 ----------DHPPLP-----ENISPELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
53-347 4.06e-36

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: 137.30  E-value: 4.06e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLR-ELKILKHFKHDNIIAIKDilrptvpYGEFK 131
Cdd:cd14099   1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKsEIKIHRSLKHPNIVKFHD-------CFEDE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 S-VYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMArGLCT 209
Cdd:cd14099  74 EnVYILLELCSNgSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLA-ARLE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 210 SPAEHQYFMteyVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhqLQLIMmvlgtpspaviqav 289
Cdd:cd14099 153 YDGERKKTL---CGTPNYIAPEVLEKKKGHSFEVDIWSLGVILYTLLVGKPPFETSD----VKETY-------------- 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 290 gaERVRAYIQSLPPRQPVPWEtvypgadrqALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14099 212 --KRIKKNEYSFPSHLSISDE---------AKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
56-266 1.33e-35

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: 135.75  E-value: 1.33e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497     56 EIIETIGNGAYGVVSSAR----RRLTGQQVAIKKIPNafDVVTNAKRT-LRELKILKHFKHDNIIAIKDILRPTVPYgef 130
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTlkgkGDGKEVEVAVKTLKE--DASEQQIEEfLREARIMRKLDHPNIVKLLGVCTEEEPL--- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497    131 ksvYVVLDLMES-DLHQIIHSSQP--LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL 207
Cdd:smart00221  77 ---MIVMEYMPGgDLLDYLRKNRPkeLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDL 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497    208 ctspAEHQYFMT--EYVATRWYrAPElMLSLHEYTQAIDLWSVGCIFGEMLAR-RQLFPGKN 266
Cdd:smart00221 154 ----YDDDYYKVkgGKLPIRWM-APE-SLKEGKFTSKSDVWSFGVLLWEIFTLgEEPYPGMS 209
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
56-266 1.41e-35

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 135.74  E-value: 1.41e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497     56 EIIETIGNGAYGVVSSARRRL----TGQQVAIKKIPNafDVVTNAKRT-LRELKILKHFKHDNIIAIKDILRPTVPYgef 130
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKLKGkggkKKVEVAVKTLKE--DASEQQIEEfLREARIMRKLDHPNVVKLLGVCTEEEPL--- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497    131 ksvYVVLDLMES-DLHQIIHSSQP-LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLc 208
Cdd:smart00219  77 ---YIVMEYMEGgDLLSYLRKNRPkLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDL- 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497    209 tspAEHQYFMTEY--VATRWYrAPElMLSLHEYTQAIDLWSVGCIFGEMLAR-RQLFPGKN 266
Cdd:smart00219 153 ---YDDDYYRKRGgkLPIRWM-APE-SLKEGKFTSKSDVWSFGVLLWEIFTLgEQPYPGMS 208
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
54-347 2.16e-35

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: 137.12  E-value: 2.16e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIEtIGNGAYGVVSSARRR--LTGQQVAIKKIPNAfdvvTNAKRTLRELKILKHFKHDNIIAIKDILrptVPYGEfK 131
Cdd:cd07867   4 EYEGCK-VGRGTYGHVYKAKRKdgKDEKEYALKQIEGT----GISMSACREIALLRELKHPNVIALQKVF---LSHSD-R 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQIIH-------SSQPLTLEH--VRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV----NENCELKI 198
Cdd:cd07867  75 KVWLLFDYAEHDLWHIIKfhraskaNKKPMQLPRsmVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKI 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 199 GDFGMARgLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGK-------NYVH-- 269
Cdd:cd07867 155 ADMGFAR-LFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRqediktsNPFHhd 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 270 QLQLIMMVLGTPSPAviqavGAERVRAyIQSLPPRQPVPWETVYPGA-------------DRQALSLLGRMLRFEPSARI 336
Cdd:cd07867 234 QLDRIFSVMGFPADK-----DWEDIRK-MPEYPTLQKDFRRTTYANSslikymekhkvkpDSKVFLLLQKLLTMDPTKRI 307
                       330
                ....*....|.
gi 20986497 337 SAAAALRHPFL 347
Cdd:cd07867 308 TSEQALQDPYF 318
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
61-347 3.22e-35

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: 134.99  E-value: 3.22e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKI-----------PNAFDVVTNAKRTL-RELKILKHFKHDNIIAIKDILRPtvPYG 128
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAIKIFnksrlrkrregKNDRGKIKNALDDVrREIAIMKKLDHPNIVRLYEVIDD--PES 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EfkSVYVVLDLMESDlhQII-----HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGM 203
Cdd:cd14008  79 D--KLYLVLEYCEGG--PVMeldsgDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGV 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 204 ARGLCTSPAEHQ------YFMteyvatrwyrAPELMLSLHEY--TQAIDLWSVG-CIFgemlarrqlfpgknyvhqlqli 274
Cdd:cd14008 155 SEMFEDGNDTLQktagtpAFL----------APELCDGDSKTysGKAADIWALGvTLY---------------------- 202
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 275 MMVLGTP---SPAVIQavgaerVRAYIQSLPprQPVPWEtvyPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14008 203 CLVFGRLpfnGDNILE------LYEAIQNQN--DEFPIP---PELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
54-346 4.32e-35

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: 134.53  E-value: 4.32e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpNAFDVVTNAKRT---LRELKILKHFKHDNIIAIKDIlrptvpYGEF 130
Cdd:cd14098   1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQI-VKRKVAGNDKNLqlfQREINILKSLEHPGIVRLIDW------YEDD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE--LKIGDFGMARGL 207
Cdd:cd14098  74 QHIYLVMEYVEGgDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPviVKISDFGLAKVI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 CTSPaehqyFMTEYVATRWYRAPELMLSLH-----EYTQAIDLWSVGCIFGEMLARRQLFPgknyvhqlqlimmvlGTPS 282
Cdd:cd14098 154 HTGT-----FLVTFCGTMAYLAPEILMSKEqnlqgGYSNLVDMWSVGCLVYVMLTGALPFD---------------GSSQ 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 283 PAVIQAVGAERVrayiqslpPRQPVPWETVYPgadrQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd14098 214 LPVEKRIRKGRY--------TQPPLVDFNISE----EAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
54-351 1.63e-34

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: 133.53  E-value: 1.63e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdVVTNAKRTLR-ELKIL-KHFKHDNIIAIKDIlrptvpYGEFK 131
Cdd:cd14091   1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVK-------IIDKSKRDPSeEIEILlRYGQHPNIITLRDV------YDDGN 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL-VNENCE---LKIGDFGMARG 206
Cdd:cd14091  68 SVYLVTELLRGgELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILyADESGDpesLRICDFGFAKQ 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 207 LctsPAEHQYFMTE-YVATrwYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhqlqlimmvlgTPSPAV 285
Cdd:cd14091 148 L---RAENGLLMTPcYTAN--FVAPEV-LKKQGYDAACDIWSLGVLLYTMLAGYTPFASGP-------------NDTPEV 208
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 286 IQAvgaeRVRAYIQSLpprQPVPWETVYPGADrqalSLLGRMLRFEPSARISAAAALRHPFLAKYH 351
Cdd:cd14091 209 ILA----RIGSGKIDL---SGGNWDHVSDSAK----DLVRKMLHVDPSQRPTAAQVLQHPWIRNRD 263
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
54-347 1.00e-33

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: 132.49  E-value: 1.00e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIEtIGNGAYGVVSSARRR--LTGQQVAIKKIPNAFDVVTnakrTLRELKILKHFKHDNIIAIKDILRPTVPygefK 131
Cdd:cd07868  19 EYEGCK-VGRGTYGHVYKAKRKdgKDDKDYALKQIEGTGISMS----ACREIALLRELKHPNVISLQKVFLSHAD----R 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQIIH-------SSQPLTLEH--VRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV----NENCELKI 198
Cdd:cd07868  90 KVWLLFDYAEHDLWHIIKfhraskaNKKPVQLPRgmVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKI 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 199 GDFGMARgLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKN--------YVH- 269
Cdd:cd07868 170 ADMGFAR-LFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQediktsnpYHHd 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 270 QLQLIMMVLGTPS----------PAVIQAVGAERVRAY-----IQSLPPRQPVPwetvypgaDRQALSLLGRMLRFEPSA 334
Cdd:cd07868 249 QLDRIFNVMGFPAdkdwedikkmPEHSTLMKDFRRNTYtncslIKYMEKHKVKP--------DSKAFHLLQKLLTMDPIK 320
                       330
                ....*....|...
gi 20986497 335 RISAAAALRHPFL 347
Cdd:cd07868 321 RITSEQAMQDPYF 333
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
61-346 7.48e-33

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: 127.63  E-value: 7.48e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNA-KRTLRELKILKHFKHDNII----AIKDIlrptvpygefKSVYV 135
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEvEHTLNERNILERVNHPFIVklhyAFQTE----------EKLYL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 136 VLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLctspAEH 214
Cdd:cd05123  71 VLDYVPGgELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKEL----SSD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 215 QYFMTEYVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyVHQLQlimmvlgtpspaviqavgaerv 294
Cdd:cd05123 147 GDRTYTFCGTPEYLAPE-VLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAEN-RKEIY---------------------- 202
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 295 rAYIQSLPPRQPvpwetvyPGADRQALSLLGRMLRFEPSARISAAAA---LRHPF 346
Cdd:cd05123 203 -EKILKSPLKFP-------EYVSPEAKSLISGLLQKDPTKRLGSGGAeeiKAHPF 249
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
55-346 9.04e-33

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: 127.80  E-value: 9.04e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNA-FDVVTNAKRTLRELKilkhfkHDNIIAIKDIlrptvpYGEFKSV 133
Cdd:cd14010   2 YVLYDEIGRGKHSVVYKGRRKGTIEFVAIKCVDKSkRPEVLNEVRLTHELK------HPNVLKFYEW------YETSNHL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDL-MESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL----- 207
Cdd:cd14010  70 WLVVEYcTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARREgeilk 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 ----CTSPAEHQYFMTEYVATR---WYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhQLQLIMMVLGT 280
Cdd:cd14010 150 elfgQFSDEGNVNKVSKKQAKRgtpYYMAPELFQG-GVHSFASDLWALGCVLYEMFTGKPPFVAES---FTELVEKILNE 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 281 PSPaviqavgaervrayiqslPPRQPVPwetvyPGADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd14010 226 DPP------------------PPPPKVS-----SKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
53-275 5.09e-32

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: 125.79  E-value: 5.09e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdvVTNAKRTLRELK---------ILKHFKHDNIIAIkdilrp 123
Cdd:cd05581   1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIK--------VLDKRHIIKEKKvkyvtiekeVLSRLAHPGIVKL------ 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 124 tvpYGEFK---SVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIG 199
Cdd:cd05581  67 ---YYTFQdesKLYFVLEYAPNgDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKIT 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 200 DFGMARGLC-------------TSPAEHQYFMTEYVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKN 266
Cdd:cd05581 144 DFGTAKVLGpdsspestkgdadSQIAYNQARAASFVGTAEYVSPE-LLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSN 222

                ....*....
gi 20986497 267 YVHQLQLIM 275
Cdd:cd05581 223 EYLTFQKIV 231
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
59-346 9.17e-32

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: 124.32  E-value: 9.17e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSA-RRRLTGQQVAIKKIpnafdvvtnAKRTLR---------ELKILKHFKHDNIIAIKDilrptvpyg 128
Cdd:cd14121   1 EKLGSGTYATVYKAyRKSGAREVVAVKCV---------SKSSLNkastenlltEIELLKKLKHPHIVELKD--------- 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 eF----KSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV--NENCELKIGDF 201
Cdd:cd14121  63 -FqwdeEHIYLIMEYCSGgDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLssRYNPVLKLADF 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 202 GMARGLctSPAEHqyfMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYvHQLqlimmvlgtp 281
Cdd:cd14121 142 GFAQHL--KPNDE---AHSLRGSPLYMAPEMILK-KKYDARVDLWSVGVILYECLFGRAPFASRSF-EEL---------- 204
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 282 spaviqavgAERVR--AYIQsLPPRqpvpwetvyPGADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd14121 205 ---------EEKIRssKPIE-IPTR---------PELSADCRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
55-347 1.31e-31

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


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 126.41  E-value: 1.31e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfdvVTNAKRTLRELKILKHFKHDNIIAIkDILRPTVPYGEFKSVY 134
Cdd:cd14211   1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNH---PSYARQGQIEVSILSRLSQENADEF-NFVRAYECFQHKNHTC 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMESDLHQIIHSS--QPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL----VNENCELKIGDFGMA---- 204
Cdd:cd14211  77 LVFEMLEQNLYDFLKQNkfSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMlvdpVRQPYRVKVIDFGSAshvs 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RGLCTSpaehqyfmteYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPA 284
Cdd:cd14211 157 KAVCST----------YLQSRYYRAPEIILGL-PFCEAIDMWSLGCVIAELFLGWPLYPGSSEYDQIRYISQTQGLPAEH 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 285 VIQA--------------------------------VGAERVRAYI-QSLPPRQPVPWETVYPGAD--------RQALSL 323
Cdd:cd14211 226 LLNAatktsrffnrdpdspyplwrlktpeeheaetgIKSKEARKYIfNCLDDMAQVNGPSDLEGSEllaekadrREFIDL 305
                       330       340
                ....*....|....*....|....
gi 20986497 324 LGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14211 306 LKRMLTIDQERRITPGEALNHPFV 329
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
53-346 2.54e-31

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: 123.62  E-value: 2.54e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpNAFDVVTNAKRTLRELKILKHFKHDNIIAIkdilrptvpYGEF-- 130
Cdd:cd06610   1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRI-DLEKCQTSMDELRKEIQAMSQCNHPNVVSY---------YTSFvv 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 -KSVYVVLDLMES-DLHQIIHSSQP---LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd06610  71 gDELWLVMPLLSGgSLLDIMKSSYPrggLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 206 GLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGcIFGEMLARRQLfPGKNYvHQLQLIMMVLgtpspav 285
Cdd:cd06610 151 SLATGGDRTRKVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFG-ITAIELATGAA-PYSKY-PPMKVLMLTL------- 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 286 iqavgaervrayiQSLPPRQPVpwetvypGADRQALS-----LLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd06610 221 -------------QNDPPSLET-------GADYKKYSksfrkMISLCLQKDPSKRPTAEELLKHKF 266
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
51-347 3.41e-31

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: 124.61  E-value: 3.41e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  51 VGDE----YEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdVVTNAKR----TLRELKILK--------HFKHDNI 114
Cdd:cd14136   4 IGEVyngrYHVVRKLGWGHFSTVWLCWDLQNKRFVALK-------VVKSAQHyteaALDEIKLLKcvreadpkDPGREHV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 115 IAIKDILRPTVPYGefKSVYVVLDLM-ESDLHQIIHSS-QPLTLEHVRYFLYQLLRGLKYMHS-AQVIHRDLKPSNLLVN 191
Cdd:cd14136  77 VQLLDDFKHTGPNG--THVCMVFEVLgPNLLKLIKRYNyRGIPLPLVKKIARQVLQGLDYLHTkCGIIHTDIKPENVLLC 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 192 E-NCELKIGDFGMArglCTSpaEHQYfmTEYVATRWYRAPELMLSLHeYTQAIDLWSVGCIFGEMLARRQLF---PGKNY 267
Cdd:cd14136 155 IsKIEVKIADLGNA---CWT--DKHF--TEDIQTRQYRSPEVILGAG-YGTPADIWSTACMAFELATGDYLFdphSGEDY 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 268 ----VHqLQLIMMVLGTPSPAVIQavGAERVRAYIQS----LPPRQPVPW--ETV----YPGADRQAL---SLLGRMLRF 330
Cdd:cd14136 227 srdeDH-LALIIELLGRIPRSIIL--SGKYSREFFNRkgelRHISKLKPWplEDVlvekYKWSKEEAKefaSFLLPMLEY 303
                       330
                ....*....|....*..
gi 20986497 331 EPSARISAAAALRHPFL 347
Cdd:cd14136 304 DPEKRATAAQCLQHPWL 320
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
53-347 5.89e-31

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: 122.37  E-value: 5.89e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKrtlrELKILKHFKHDNIIAIkdilrptvpYGEFKS 132
Cdd:cd06612   3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIK----EISILKQCDSPYIVKY---------YGSYFK 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLME-------SDLHQIIHSSqpLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd06612  70 NTDLWIVMEycgagsvSDIMKITNKT--LTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 206 GLCTSPAEhqyfMTEYVATRWYRAPELMLSLhEYTQAIDLWSVGcifgemlarrqlfpgknyvhqLQLIMMVLGTPSPAV 285
Cdd:cd06612 148 QLTDTMAK----RNTVIGTPFWMAPEVIQEI-GYNNKADIWSLG---------------------ITAIEMAEGKPPYSD 201
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 286 IQAVgaeRVRAYIQSLPP---RQPVPWETVYPgadrqalSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd06612 202 IHPM---RAIFMIPNKPPptlSDPEKWSPEFN-------DFVKKCLVKDPEERPSAIQLLQHPFI 256
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
55-347 6.01e-31

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 124.28  E-value: 6.01e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAK------RTLRE----------LKILKHFKHDNIIAIk 118
Cdd:cd14212   1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQAMleiailTLLNTkydpedkhhiVRLLDHFMHHGHLCI- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 119 dilrptvpygefksvyvVLDLMESDLHQIIHSSQ--PLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENC-- 194
Cdd:cd14212  80 -----------------VFELLGVNLYELLKQNQfrGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDsp 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 195 ELKIGDFGMArglCTSpaehQYFMTEYVATRWYRAPELMLSLHeYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLI 274
Cdd:cd14212 143 EIKLIDFGSA---CFE----NYTLYTYIQSRFYRSPEVLLGLP-YSTAIDMWSLGCIAAELFLGLPLFPGNSEYNQLSRI 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 275 MMVLGTPSPAVIQ---------------------------------AVGAERVRAY---------IQSLPPRQPVPWETV 312
Cdd:cd14212 215 IEMLGMPPDWMLEkgkntnkffkkvaksggrstyrlktpeefeaenNCKLEPGKRYfkyktlediIMNYPMKKSKKEQID 294
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 20986497 313 YPGADRQAL-SLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14212 295 KEMETRLAFiDFLKGLLEYDPKKRWTPDQALNHPFI 330
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
55-272 8.67e-31

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: 122.02  E-value: 8.67e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIK-----KIPNafDVVTnaKRTLRELKILKHFKHDNII----AIKDILRptv 125
Cdd:cd14162   2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKivskkKAPE--DYLQ--KFLPREIEVIKGLKHPNLIcfyeAIETTSR--- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 pygefksVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA 204
Cdd:cd14162  75 -------VYIIMELAENgDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFA 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 205 RGlCTSPAEHQYFMTE-YVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQ 272
Cdd:cd14162 148 RG-VMKTKDGKPKLSEtYCGSYAYASPEILRGIPYDPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLK 215
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
54-249 9.40e-31

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 121.64  E-value: 9.40e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIP----NAFDVVTNakrtlrELKILKHFKHDNIIAIkdilrptvpYGE 129
Cdd:cd06613   1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKlepgDDFEIIQQ------EISMLKECRHPNIVAY---------FGS 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDLME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd06613  66 YLRRDKLWIVMEycggGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSA 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 20986497 206 GLCTSPAEHQYFmteyVATRWYRAPELMLSLHE--YTQAIDLWSVG 249
Cdd:cd06613 146 QLTATIAKRKSF----IGTPYWMAPEVAAVERKggYDGKCDIWALG 187
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
61-346 1.43e-30

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 120.94  E-value: 1.43e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSAR-RRLTGQQVAIKKIpnafdvvtnAKRTL--------RELKILKHFKHDNIIAIKDILRPTvpygefK 131
Cdd:cd14120   1 IGHGAFAVVFKGRhRKKPDLPVAIKCI---------TKKNLsksqnllgKEIKILKELSHENVVALLDCQETS------S 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVldlME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE---------LKI 198
Cdd:cd14120  66 SVYLV---MEycngGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGrkpspndirLKI 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 199 GDFG---------MARGLCTSPaehqyfMteyvatrwYRAPELMLSLHeYTQAIDLWSVGCIFgemlarRQLFPGKnyvh 269
Cdd:cd14120 143 ADFGfarflqdgmMAATLCGSP------M--------YMAPEVIMSLQ-YDAKADLWSIGTIV------YQCLTGK---- 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 270 qlqlimmvlgtpspAVIQAVGAERVRAYIQ---SLPPRQPvpwetvyPGADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd14120 198 --------------APFQAQTPQELKAFYEknaNLRPNIP-------SGTSPALKDLLLGLLKRNPKDRIDFEDFFSHPF 256
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
54-266 1.47e-30

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: 121.22  E-value: 1.47e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpNAFDVVTNAKRT--LRELKILKHFKHDNIIAIKDilrptvPYGEFK 131
Cdd:cd08224   1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKV-QIFEMMDAKARQdcLKEIDLLQQLNHPNIIKYLA------SFIENN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMES-DLHQIIH--SSQPLTLEHV---RYFlYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd08224  74 ELNIVLELADAgDLSRLIKhfKKQKRLIPERtiwKYF-VQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGR 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 206 glctspaehqYFMTE------YVATRWYRAPELmlsLHE--YTQAIDLWSVGCIFGEMLARRQLFPGKN 266
Cdd:cd08224 153 ----------FFSSKttaahsLVGTPYYMSPER---IREqgYDFKSDIWSLGCLLYEMAALQSPFYGEK 208
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
55-252 1.90e-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: 120.92  E-value: 1.90e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKI----PNAFDVVTNAKRT-LRELKI-LKHFKHDNIIAIKDILRPTVPYg 128
Cdd:cd13993   2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLyksgPNSKDGNDFQKLPqLREIDLhRRVSRHPNIITLHDVFETEVAI- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 efksvYVVLDLMES-DLHQIIHSSQ--PLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE-LKIGDFGMA 204
Cdd:cd13993  81 -----YIVLEYCPNgDLFEAITENRiyVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGtVKLCDFGLA 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 20986497 205 rglCTSPaehqYFMTEYVATRWYRAPELMLSLHE-----YTQAIDLWSVGCIF 252
Cdd:cd13993 156 ---TTEK----ISMDFGVGSEFYMAPECFDEVGRslkgyPCAAGDIWSLGIIL 201
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
55-347 2.03e-30

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: 120.75  E-value: 2.03e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSA--RRRLTGQQVAIKKI-----PNAFdvvtnAKRTL-RELKILKHFKHDNIIAIKDILrptvp 126
Cdd:cd14080   2 YRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKIIdkkkaPKDF-----LEKFLpRELEILRKLRHPNIIQVYSIF----- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 ygEFKS-VYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA 204
Cdd:cd14080  72 --ERGSkVFIFMEYAEHgDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RgLCTSPaEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyVHQL--QLIMMVLGTPS 282
Cdd:cd14080 150 R-LCPDD-DGDVLSKTFCGSAAYAAPEILQGIPYDPKKYDIWSLGVILYIMLCGSMPFDDSN-IKKMlkDQQNRKVRFPS 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 283 PavIQAVGAERVRayiqslpprqpvpwetvypgadrqalsLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14080 227 S--VKKLSPECKD---------------------------LIDQLLEPDPTKRATIEEILNHPWL 262
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
55-347 2.09e-30

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: 120.44  E-value: 2.09e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTL-RELKILKHFKHDNIIAIKDIlrptvpYGEFKSV 133
Cdd:cd14081   3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVeREIAIMKLIEHPNVLKLYDV------YENKKYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR------- 205
Cdd:cd14081  77 YLVLEYVSGgELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASlqpegsl 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 206 --GLCTSPaeHqyfmteyvatrwYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyVHQLqlimmvlgtpsp 283
Cdd:cd14081 157 leTSCGSP--H------------YACPEVIKGEKYDGRKADIWSCGVILYALLVGALPFDDDN-LRQL------------ 209
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 284 aviqavgAERVRAYIQSLPPRQPVpwetvypgadrQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14081 210 -------LEKVKRGVFHIPHFISP-----------DAQDLLRRMLEVNPEKRITIEEIKKHPWF 255
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
56-249 2.60e-30

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: 120.29  E-value: 2.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497    56 EIIETIGNGAYGVVSSARRRL----TGQQVAIKKIPNAFDVVTNAKrTLRELKILKHFKHDNIIAIkdilrptvpYG--- 128
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGTLKGegenTKIKVAVKTLKEGADEEERED-FLEEASIMKKLDHPNIVKL---------LGvct 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   129 EFKSVYVVLDLMES-DLHQIIHSS-QPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARG 206
Cdd:pfam07714  72 QGEPLYIVTEYMPGgDLLDFLRKHkRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRD 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 20986497   207 LctsPAEHQYFMTE--YVATRWYrAPELmLSLHEYTQAIDLWSVG 249
Cdd:pfam07714 152 I---YDDDYYRKRGggKLPIKWM-APES-LKDGKFTSKSDVWSFG 191
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
53-347 2.66e-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: 120.92  E-value: 2.66e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKI--------PNAFDVVTNAkrTLRELKILKHF-KHDNIIAIKDIlrp 123
Cdd:cd14093   3 AKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIditgekssENEAEELREA--TRREIEILRQVsGHPNIIELHDV--- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 124 tvpygeFKS---VYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIG 199
Cdd:cd14093  78 ------FESptfIFLVFELCRKgELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKIS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 200 DFGMARGLctspAEHQYfMTEYVATRWYRAPEL----MLSLHE-YTQAIDLWSVGCIFGEMLARRQLFpgknyVHQLQLI 274
Cdd:cd14093 152 DFGFATRL----DEGEK-LRELCGTPGYLAPEVlkcsMYDNAPgYGKEVDMWACGVIMYTLLAGCPPF-----WHRKQMV 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 275 MMvlgtpspaviqavgaervRAyIQSLPPRQPVP-WETVypgaDRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14093 222 ML------------------RN-IMEGKYEFGSPeWDDI----SDTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
54-347 1.10e-29

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: 118.79  E-value: 1.10e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnafdvvtNAKRTLR-----ELKILKHFKHDNIIAIKDIlrptvpyg 128
Cdd:cd14087   2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMI--------ETKCRGRevcesELNVLRRVRHTNIIQLIEV-------- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 eFKS---VYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV---NENCELKIGDF 201
Cdd:cd14087  66 -FETkerVYMVMELATGgELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYyhpGPDSKIMITDF 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 202 GMARGLCTSPAEhqyFMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhqlqlimmvlgtp 281
Cdd:cd14087 145 GLASTRKKGPNC---LMKTTCGTPEYIAPEILLR-KPYTQSVDMWAVGVIAYILLSGTMPFDDDN--------------- 205
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 282 spaviqavgaeRVRAYIQSLPPR---QPVPWetvyPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14087 206 -----------RTRLYRQILRAKysySGEPW----PSVSNLAKDFIDRLLTVNPGERLSATQALKHPWI 259
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
59-250 1.87e-29

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: 118.03  E-value: 1.87e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSAR-RRLTGQ--QVAIKKIPNAFDvvtNAKRT--LRELKILKHFKHDNIIAIkdilrptvpYG---EF 130
Cdd:cd00192   1 KKLGEGAFGEVYKGKlKGGDGKtvDVAVKTLKEDAS---ESERKdfLKEARVMKKLGHPNVVRL---------LGvctEE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVLDLMES-DLHQ---------IIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGD 200
Cdd:cd00192  69 EPLYLVMEYMEGgDLLDflrksrpvfPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISD 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 201 FGMARglctspaeHQYFMTEYVAT-------RWYrAPElMLSLHEYTQAIDLWSVGC 250
Cdd:cd00192 149 FGLSR--------DIYDDDYYRKKtggklpiRWM-APE-SLKDGIFTSKSDVWSFGV 195
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
55-347 2.92e-29

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: 117.43  E-value: 2.92e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDilrpTVPYGEFKsvY 134
Cdd:cd14069   3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYG----HRREGEFQ--Y 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAE 213
Cdd:cd14069  77 LFLEYASGgELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKGKE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 214 HqyFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIfgemlarrqlfpgknyvhqlqLIMMVLG-TP--SPaviqavg 290
Cdd:cd14069 157 R--LLNKMCGTLPYVAPELLAKKKYRAEPVDVWSCGIV---------------------LFAMLAGeLPwdQP------- 206
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 291 AERVRAYIQSLPPRQP--VPWetvyPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14069 207 SDSCQEYSDWKENKKTylTPW----KKIDTAALSLLRKILTENPNKRITIEDIKKHPWY 261
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
53-350 3.56e-29

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 117.45  E-value: 3.56e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNaKRTLRELKILKHFKHDNIIAIkdilrptvpYGEFKS 132
Cdd:cd06605   1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQ-KQILRELDVLHKCNSPYIVGF---------YGAFYS 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 ---VYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSA-QVIHRDLKPSNLLVNENCELKIGDFGMARGL 207
Cdd:cd06605  71 egdISICMEYMDGgSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVSGQL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 CTSPAEhqyfmtEYVATRWYRAPELMLSLHeYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhqlqlimmvlGTPSPAVIq 287
Cdd:cd06605 151 VDSLAK------TFVGTRSYMAPERISGGK-YTVKSDIWSLGLSLVELATGRFPYPPPN------------AKPSMMIF- 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 288 avgaERVRAYIQSLPPRQPVpweTVYPGadrQALSLLGRMLRFEPSARISAAAALRHPFLAKY 350
Cdd:cd06605 211 ----ELLSYIVDEPPPLLPS---GKFSP---DFQDFVSQCLQKDPTERPSYKELMEHPFIKRY 263
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
50-262 3.68e-29

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: 117.40  E-value: 3.68e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  50 DVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDvvtNAKRTLRELKILKHF-KHDNIIAIKDILRPTVPYG 128
Cdd:cd06608   3 DPAGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIED---EEEEIKLEINILRKFsNHPNIATFYGAFIKKDPPG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLME----SDLHQ-IIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGM 203
Cdd:cd06608  80 GDDQLWLVMEYCGggsvTDLVKgLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGV 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 204 ARGLCTSPAEHQYFmteyVATRWYRAPEL---MLSLHE-YTQAIDLWSVGCI----------FGEMLARRQLF 262
Cdd:cd06608 160 SAQLDSTLGRRNTF----IGTPYWMAPEViacDQQPDAsYDARCDVWSLGITaieladgkppLCDMHPMRALF 228
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
54-361 3.71e-29

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: 118.56  E-value: 3.71e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEI---IETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDvvtnakrTLRELKILKHFK-HDNIIAIKDILrptvpYGE 129
Cdd:cd14092   4 NYELdlrEEALGDGSFSVCRKCVHKKTGQEFAVKIVSRRLD-------TSREVQLLRLCQgHPNIVKLHEVF-----QDE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKsVYVVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV---NENCELKIGDFGMAR 205
Cdd:cd14092  72 LH-TYLVMELLRgGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGFAR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 206 GLctspAEHQYFMTEyVATRWYRAPELM---LSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYvhqlqlimmvlGTPS 282
Cdd:cd14092 151 LK----PENQPLKTP-CFTLPYAAPEVLkqaLSTQGYDESCDLWSLGVILYTMLSGQVPFQSPSR-----------NESA 214
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 283 PAVIQavgaeRVRAYIQSLPPRQpvpWETVYPgadrQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCAP 361
Cdd:cd14092 215 AEIMK-----RIKSGDFSFDGEE---WKNVSS----EAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSSPSSTPLMTP 281
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
55-346 4.77e-29

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: 116.74  E-value: 4.77e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpNAFDVVTN--AKRTLRELKILKHFKHDNIIAIKDILRPTvpygefKS 132
Cdd:cd14663   2 YELGRTLGEGTFAKVKFARNTKTGESVAIKII-DKEQVAREgmVEQIKREIAIMKLLRHPNIVELHEVMATK------TK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMArglctsp 211
Cdd:cd14663  75 IFFVMELVTgGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLS------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 212 AEHQYFMTEYV-----ATRWYRAPELmLSLHEYTQAI-DLWSVGCIFGEMLARRQLFPGKNyvhqlqliMMVLGTPspav 285
Cdd:cd14663 148 ALSEQFRQDGLlhttcGTPNYVAPEV-LARRGYDGAKaDIWSCGVILFVLLAGYLPFDDEN--------LMALYRK---- 214
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 286 iqavgaervrayIQSLPPRQPvPWetVYPGADRqalsLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd14663 215 ------------IMKGEFEYP-RW--FSPGAKS----LIKRILDPNPSTRITVEQIMASPW 256
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
55-347 6.65e-29

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


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 118.41  E-value: 6.65e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYG-VVSSARRRLTGQQVAIKKIPNAfDVVTNAKRTlrELKILKHFKHDNIIAIKDILRPTVPYGEFKSV 133
Cdd:cd14213  14 YEIVDTLGEGAFGkVVECIDHKMGGMHVAVKIVKNV-DRYREAARS--EIQVLEHLNTTDPNSTFRCVQMLEWFDHHGHV 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMESDLHQII--HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNE------------------- 192
Cdd:cd14213  91 CIVFELLGLSTYDFIkeNSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQsdyvvkynpkmkrdertlk 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 193 NCELKIGDFGMArglcTSPAEHQyfmTEYVATRWYRAPELMLSLHeYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQ 272
Cdd:cd14213 171 NPDIKVVDFGSA----TYDDEHH---STLVSTRHYRAPEVILALG-WSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHLA 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 273 LIMMVLGtPSPA-VIQAVgaeRVRAYIQ---------SLPPR------QPVPWETVYPGADRQAL-SLLGRMLRFEPSAR 335
Cdd:cd14213 243 MMERILG-PLPKhMIQKT---RKRKYFHhdqldwdehSSAGRyvrrrcKPLKEFMLSQDVDHEQLfDLIQKMLEYDPAKR 318
                       330
                ....*....|..
gi 20986497 336 ISAAAALRHPFL 347
Cdd:cd14213 319 ITLDEALKHPFF 330
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
55-274 8.80e-29

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: 115.95  E-value: 8.80e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIP-NAFDVVTNAKRTLRELKILKHFKHDNIIAIkdilrptvpYGEFKSV 133
Cdd:cd14073   3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKkDKIEDEQDMVRIRREIEIMSSLNHPHIIRI---------YEVFENK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMArglct 209
Cdd:cd14073  74 DKIVIVMEyasgGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLS----- 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 210 SPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLI 274
Cdd:cd14073 149 NLYSKDKLLQTFCGSPLYASPEIVNGTPYQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQI 213
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
54-266 9.26e-29

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: 115.97  E-value: 9.26e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPnafdvVTNAKRTLR-----ELKILKHFKHDNIIAIKDilrptvPYG 128
Cdd:cd08529   1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQID-----ISRMSRKMReeaidEARVLSKLNSPYVIKYYD------SFV 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMES-DLHQIIHS--SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd08529  70 DKGKLNIVMEYAENgDLHSLIKSqrGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAK 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 206 GLCTSpaehQYFMTEYVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKN 266
Cdd:cd08529 150 ILSDT----TNFAQTIVGTPYYLSPE-LCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQN 205
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
53-256 1.11e-28

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: 116.24  E-value: 1.11e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKrTLRELKILKHFKHDNIIaikdilRPTVPYGEFKS 132
Cdd:cd13996   6 NDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEK-VLREVKALAKLNHPNIV------RYYTAWVEEPP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLME-SDLHQII----HSSQPLTLEHVRYFlYQLLRGLKYMHSAQVIHRDLKPSNLLVNENC-ELKIGDFGMAR- 205
Cdd:cd13996  79 LYIQMELCEgGTLRDWIdrrnSSSKNDRKLALELF-KQILKGVSYIHSKGIVHRDLKPSNIFLDNDDlQVKIGDFGLATs 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 206 ---------GLCTSPAEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd13996 158 ignqkrelnNLNNNNNGNTSNNSVGIGTPLYASPEQ-LDGENYNEKADIYSLGIILFEML 216
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
54-347 1.94e-28

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: 115.84  E-value: 1.94e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKI--------PNAFDVVTNAkrTLRELKILKHFK-HDNIIAIKDilrpt 124
Cdd:cd14181  11 KYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIevtaerlsPEQLEEVRSS--TLKEIHILRQVSgHPSIITLID----- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 125 vPYGEFKSVYVVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGM 203
Cdd:cd14181  84 -SYESSTFIFLVFDLMRrGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGF 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 204 ARGLctSPAEHqyfMTEYVATRWYRAPEL----MLSLHE-YTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIM--- 275
Cdd:cd14181 163 SCHL--EPGEK---LRELCGTPGYLAPEIlkcsMDETHPgYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMegr 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 276 MVLGTPSpaviqavgaervrayiqslpprqpvpWEtvypgaDRQ--ALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14181 238 YQFSSPE--------------------------WD------DRSstVKDLISRLLVVDPEIRLTAEQALQHPFF 279
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
55-347 2.00e-28

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: 115.05  E-value: 2.00e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRT-LRELKILKHFKHDNIIAIkdilrptvpYGEFK-- 131
Cdd:cd05578   2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNvLNELEILQELEHPFLVNL---------WYSFQde 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 -SVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLct 209
Cdd:cd05578  73 eDMYMVVDLLLGgDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKL-- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 210 spaEHQYFMTEYVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhqlqlimmvlgtpspaviqAV 289
Cdd:cd05578 151 ---TDGTLATSTSGTKPYMAPE-VFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHS---------------------RT 205
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 290 GAERVRAYIQSLPPRQPVPWETVypgadrqALSLLGRMLRFEPSARISAAAALR-HPFL 347
Cdd:cd05578 206 SIEEIRAKFETASVLYPAGWSEE-------AIDLINKLLERDPQKRLGDLSDLKnHPYF 257
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
54-347 3.76e-28

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: 114.07  E-value: 3.76e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPnafdvVTNAKRTLR-----ELKILKHFKHDNIIAIKDILRptvpyG 128
Cdd:cd08223   1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLN-----LKNASKRERkaaeqEAKLLSKLKHPNIVSYKESFE-----G 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMES-DLHQII--HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd08223  71 EDGFLYIVMGFCEGgDLYTRLkeQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIAR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 206 GLctspaEHQYFM-TEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVhqlQLIMMVLGTPSPA 284
Cdd:cd08223 151 VL-----ESSSDMaTTLIGTPYYMSPEL-FSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMN---SLVYKILEGKLPP 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 285 ViqavgaervrayiqslpPRQPVPwetvypgadrQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd08223 222 M-----------------PKQYSP----------ELGELIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
55-347 4.59e-28

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: 113.90  E-value: 4.59e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIK-----KIPNAfDVVTNAKRtlrELKILKHFKHDNIIAIKDILR-PTvpyg 128
Cdd:cd14079   4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKilnrqKIKSL-DMEEKIRR---EIQILKLFRHPHIIRLYEVIEtPT---- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 efkSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA--- 204
Cdd:cd14079  76 ---DIFMVMEYVSGgELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSnim 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 ------RGLCTSPaehQYFMTEYVATRWYRAPElmlslheytqaIDLWSVGCIFGEMLARRQLFPGKNYvhqlqlimmvl 278
Cdd:cd14079 153 rdgeflKTSCGSP---NYAAPEVISGKLYAGPE-----------VDVWSCGVILYALLCGSLPFDDEHI----------- 207
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 279 gtpsPAVIQavgaeRVRAYIQSLPprqpvpwETVYPGADrqalSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14079 208 ----PNLFK-----KIKSGIYTIP-------SHLSPGAR----DLIKRMLVVDPLKRITIPEIRQHPWF 256
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
55-347 6.34e-28

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: 115.51  E-value: 6.34e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfdvVTNAKRTLRELKILKHFKHDNIIAIkDILRPTVPYGEFKSVY 134
Cdd:cd14229   2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNH---PSYARQGQIEVGILARLSNENADEF-NFVRAYECFQHRNHTC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMESDLHQIIHSSQ--PLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL----VNENCELKIGDFGMA---- 204
Cdd:cd14229  78 LVFEMLEQNLYDFLKQNKfsPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMlvdpVRQPYRVKVIDFGSAshvs 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RGLCTSpaehqyfmteYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPA 284
Cdd:cd14229 158 KTVCST----------YLQSRYYRAPEIILGL-PFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQGLPGEQ 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 285 VIQA--------------------------------VGAERVRAYI-QSLPPRQPVPWETVYPGAD--------RQALSL 323
Cdd:cd14229 227 LLNVgtktsrffcretdapysswrlktleeheaetgMKSKEARKYIfNSLDDIAHVNMVMDLEGSDllaekadrREFVAL 306
                       330       340
                ....*....|....*....|....
gi 20986497 324 LGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14229 307 LKKMLLIDADLRITPADTLSHPFV 330
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
54-344 9.14e-28

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: 113.62  E-value: 9.14e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIP-NAFDvvTNAKRTLRELKILKHFKHDNIiaikdiLRPTVPYGEFKS 132
Cdd:cd14046   7 DFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKlRSES--KNNSRILREVMLLSRLNHQHV------VRYYQAWIERAN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMESD-LHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR------ 205
Cdd:cd14046  79 LYIQMEYCEKStLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATsnklnv 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 206 GLCTSPAEHQYF--------MTEYVATRWYRAPELMLSLHE-YTQAIDLWSVGCIFGEMlarrqlfpgknyvhqlqliMM 276
Cdd:cd14046 159 ELATQDINKSTSaalgssgdLTGNVGTALYVAPEVQSGTKStYNEKVDMYSLGIIFFEM-------------------CY 219
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 277 VLGTpspaviqavGAERVRAY--IQSLPPRQPVPWETVYpgADRQAlSLLGRMLRFEPSARISAAAALRH 344
Cdd:cd14046 220 PFST---------GMERVQILtaLRSVSIEFPPDFDDNK--HSKQA-KLIRWLLNHDPAKRPSAQELLKS 277
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
59-347 9.36e-28

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: 112.88  E-value: 9.36e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNA---KRTLRELKILKHFKHDNIIAIkdilrptvpYGEFKS--- 132
Cdd:cd06632   6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKSResvKQLEQEIALLSKLRHPNIVQY---------YGTEREedn 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLctsp 211
Cdd:cd06632  77 LYIFLEYVPgGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHV---- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 212 aEHQYFMTEYVATRWYRAPELMLSLHE-YTQAIDLWSVGCIFGEMLArrqlfpGKNYVHQLQLImmvlgtpspAVIQAVG 290
Cdd:cd06632 153 -EAFSFAKSFKGSPYWMAPEVIMQKNSgYGLAVDIWSLGCTVLEMAT------GKPPWSQYEGV---------AAIFKIG 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 291 AERVrayiqsLPprqPVPwETVYPgadrQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd06632 217 NSGE------LP---PIP-DHLSP----DAKDFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
54-347 1.14e-27

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: 113.18  E-value: 1.14e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQ-QVAIKKIpNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTvpygefKS 132
Cdd:cd14202   3 EFSRKDLIGHGAFAVVFKGRHKEKHDlEVAVKCI-NKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEIA------NS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVN---------ENCELKIGDFG 202
Cdd:cd14202  76 VYLVMEYCNGgDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRIKIADFG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 203 MAR---------GLCTSPAehqyfmteyvatrwYRAPELMLSlHEYTQAIDLWSVGCIFgemlarRQLFPGKnyvhqlql 273
Cdd:cd14202 156 FARylqnnmmaaTLCGSPM--------------YMAPEVIMS-QHYDAKADLWSIGTII------YQCLTGK-------- 206
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 274 immvlgtpspAVIQAVGAERVRAYIQ---SLPPRqpVPWETVYPgaDRQalsLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14202 207 ----------APFQASSPQDLRLFYEknkSLSPN--IPRETSSH--LRQ---LLLGLLQRNQKDRMDFDEFFHHPFL 266
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
61-256 1.23e-27

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: 113.08  E-value: 1.23e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNA-KRTLRELKILKHFKHDNIIAIkdilrptvpYGEF---KSVYVV 136
Cdd:cd05579   1 ISRGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQvDSVLAERNILSQAQNPFVVKL---------YYSFqgkKNLYLV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 137 LDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQ 215
Cdd:cd05579  72 MEYLPGgDLYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLVRRQIKL 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 20986497 216 YFMT-----------EYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEML 256
Cdd:cd05579 152 SIQKksngapekedrRIVGTPDYLAPEILLGQ-GHGKTVDWWSLGVILYEFL 202
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
61-262 1.48e-27

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: 112.15  E-value: 1.48e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRltGQQVAIKKIpnafDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPygefksVYVVLDLM 140
Cdd:cd14058   1 VGRGSFGVVCKARWR--NQIVAVKII----ESESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKP------VCLVMEYA 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 E-SDLHQIIHSSQPL---TLEHVRYFLYQLLRGLKYMHSAQ---VIHRDLKPSN-LLVNENCELKIGDFGMArglctspA 212
Cdd:cd14058  69 EgGSLYNVLHGKEPKpiyTAAHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNlLLTNGGTVLKICDFGTA-------C 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 20986497 213 EHQYFMTEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLF 262
Cdd:cd14058 142 DISTHMTNNKGSAAWMAPEVFEGS-KYSEKCDVFSWGIILWEVITRRKPF 190
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
53-347 1.79e-27

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 114.34  E-value: 1.79e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQ-QVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNiiaiKDILRPTVPYGEFK 131
Cdd:cd14214  13 ERYEIVGDLGEGTFGKVVECLDHARGKsQVALKIIRNVGKYREAARLEINVLKKIKEKDKEN----KFLCVLMSDWFNFH 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 S-VYVVLDLMESDLHQIIHSS--QPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL-VN----------ENCE-- 195
Cdd:cd14214  89 GhMCIAFELLGKNTFEFLKENnfQPYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILfVNsefdtlynesKSCEek 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 196 ------LKIGDFGMArglcTSPAEHQyfmTEYVATRWYRAPELMLSLHeYTQAIDLWSVGCIFGEMLARRQLFPGKNYVH 269
Cdd:cd14214 169 svkntsIRVADFGSA----TFDHEHH---TTIVATRHYRPPEVILELG-WAQPCDVWSLGCILFEYYRGFTLFQTHENRE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 270 QLQLIMMVLGtPSPAviQAVGAERVRAYIQslppRQPVPWE----------------TVYPGADR----QALSLLGRMLR 329
Cdd:cd14214 241 HLVMMEKILG-PIPS--HMIHRTRKQKYFY----KGSLVWDenssdgryvsenckplMSYMLGDSlehtQLFDLLRRMLE 313
                       330
                ....*....|....*...
gi 20986497 330 FEPSARISAAAALRHPFL 347
Cdd:cd14214 314 FDPALRITLKEALLHPFF 331
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
55-265 2.14e-27

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: 112.10  E-value: 2.14e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnafDV--VTNAKR--TLRELKILKHFKHDNIIAIKDilrptvPYGEF 130
Cdd:cd08530   2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEV----NLgsLSQKERedSVNEIRLLASVNHPNIIRYKE------AFLDG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVldlME----SDLHQIIHSSQ----PLTLEHV-RYFLyQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDF 201
Cdd:cd08530  72 NRLCIV---MEyapfGDLSKLISKRKkkrrLFPEDDIwRIFI-QMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDL 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 202 GMARGLCTSPAEHQyfmteyVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGK 265
Cdd:cd08530 148 GISKVLKKNLAKTQ------IGTPLYAAPEVWKG-RPYDYKSDIWSLGCLLYEMATFRPPFEAR 204
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
61-262 3.75e-27

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: 111.63  E-value: 3.75e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVV--SSARRRLTGQQVAIKKIPNAFDVVTNA---KRTLRELKILKHFKHDNIIAIKDILRptVPYGEFKSVyv 135
Cdd:cd13994   1 IGKGATSVVriVTKKNPRSGVLYAVKEYRRRDDESKRKdyvKRLTSEYIISSKLHHPNIVKVLDLCQ--DLHGKWCLV-- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 136 vldlME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFG--------- 202
Cdd:cd13994  77 ----MEycpgGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGtaevfgmpa 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 203 -----MARGLCTSPAehqyfmteyvatrwYRAPELMLSLhEYT-QAIDLWSVGCIFGEMLARRQLF 262
Cdd:cd13994 153 ekespMSAGLCGSEP--------------YMAPEVFTSG-SYDgRAVDVWSCGIVLFALFTGRFPW 203
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
55-346 7.45e-27

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: 110.42  E-value: 7.45e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIK-----KIPNAFDVVTNakrtlrELKILKHFKHDNIIAIKDIlrptvpYGE 129
Cdd:cd14185   2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKiidksKLKGKEDMIES------EILIIKSLSHPNIVKLFEV------YET 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE----LKIGDFGMA 204
Cdd:cd14185  70 EKEIYLILEYVRGgDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDksttLKLADFGLA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RgLCTSPaehqyfMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLF--PGKNYVHQLQLIMMvlgtps 282
Cdd:cd14185 150 K-YVTGP------IFTVCGTPTYVAPEI-LSEKGYGLEVDMWAAGVILYILLCGFPPFrsPERDQEELFQIIQL------ 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 283 paviqavgaervrAYIQSLPPRqpvpWETVypgaDRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd14185 216 -------------GHYEFLPPY----WDNI----SEAAKDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
53-352 7.83e-27

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: 110.99  E-value: 7.83e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnafdvVTNAKRTLR----ELKILKHFKHDNIIAIKD--------- 119
Cdd:cd06611   5 DIWEIIGELGDGAFGKVYKAQHKETGLFAAAKII------QIESEEELEdfmvEIDILSECKHPNIVGLYEayfyenklw 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 120 ILRPTVPYGEFKSVYVVLDlmesdlhqiihssQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIG 199
Cdd:cd06611  79 ILIEFCDGGALDSIMLELE-------------RGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLA 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 200 DFGM-ARGLCTSPAEHQYFMTEYvatrWYrAPELML----SLHEYTQAIDLWSVGCIFGEMLARRqlfPGKNYVHQLQLI 274
Cdd:cd06611 146 DFGVsAKNKSTLQKRDTFIGTPY----WM-APEVVAcetfKDNPYDYKADIWSLGITLIELAQME---PPHHELNPMRVL 217
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 275 MMVLGTPSPAVIqavgaervrayiqslpprQPVPWETVYPgadrqalSLLGRMLRFEPSARISAAAALRHPFLAKYHD 352
Cdd:cd06611 218 LKILKSEPPTLD------------------QPSKWSSSFN-------DFLKSCLVKDPDDRPTAAELLKHPFVSDQSD 270
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
51-251 9.09e-27

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: 110.15  E-value: 9.09e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  51 VGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPnafdvvtnaKRTLR--------ELKILKHFKHDNIIAIKDIlr 122
Cdd:cd14083   1 IRDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCID---------KKALKgkedslenEIAVLRKIKHPNIVQLLDI-- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 123 ptvpYGEFKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV---NENCELKI 198
Cdd:cd14083  70 ----YESKSHLYLVMELVTGgELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMI 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 20986497 199 GDFGMarglctSPAEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCI 251
Cdd:cd14083 146 SDFGL------SKMEDSGVMSTACGTPGYVAPEV-LAQKPYGKAVDCWSIGVI 191
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
53-349 9.46e-27

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: 110.89  E-value: 9.46e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdVVTNAKRT-LRELKILKHF-KHDNIIAIKDIlrptvpYGEF 130
Cdd:cd14175   1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVK-------VIDKSKRDpSEEIEILLRYgQHPNIITLKDV------YDDG 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL-VNENCE---LKIGDFGMAR 205
Cdd:cd14175  68 KHVYLVTELMRGgELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAK 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 206 GLctsPAEHQYFMTE-YVATrwYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLF---PGKnyvhqlqlimmvlgTP 281
Cdd:cd14175 148 QL---RAENGLLMTPcYTAN--FVAPEV-LKRQGYDEGCDIWSLGILLYTMLAGYTPFangPSD--------------TP 207
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 282 SpAVIQAVGAERVRAYIQSlpprqpvpWETVYPGADrqalSLLGRMLRFEPSARISAAAALRHPFLAK 349
Cdd:cd14175 208 E-EILTRIGSGKFTLSGGN--------WNTVSDAAK----DLVSKMLHVDPHQRLTAKQVLQHPWITQ 262
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
53-347 9.69e-27

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: 109.95  E-value: 9.69e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKI-PNAFDVVTNAKRTLRELKILKHFKHDNIIAIkdilrptvpYGEFK 131
Cdd:cd14186   1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIdKKAMQKAGMVQRVRNEVEIHCQLKHPSILEL---------YNYFE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 S---VYVVLDLMES-DLHQII-HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARG 206
Cdd:cd14186  72 DsnyVYLVLEMCHNgEMSRYLkNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQ 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 207 LcTSPAEHQYFMteyVATRWYRAPELMlSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMvlgtpspavi 286
Cdd:cd14186 152 L-KMPHEKHFTM---CGTPNYISPEIA-TRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVL---------- 216
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 287 qavGAERVRAYIQslpprqpvpwetvypgadRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14186 217 ---ADYEMPAFLS------------------REAQDLIHQLLRKNPADRLSLSSVLDHPFM 256
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
59-347 1.40e-26

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 109.78  E-value: 1.40e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQVAIKKI---PNAFDVVTNAKRTL-----RELKILKHFKHDNIIA---------IKDIL 121
Cdd:cd06629   7 ELIGKGTYGRVYLAMNATTGEMLAVKQVelpKTSSDRADSRQKTVvdalkSEIDTLKDLDHPNIVQylgfeetedYFSIF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 122 RPTVPYGEFKSVYVVLDLMESDLhqiihssqpltlehVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDF 201
Cdd:cd06629  87 LEYVPGGSIGSCLRKYGKFEEDL--------------VRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 202 GMARGlctspAEHQYFMTEYVATR---WYRAPELMLSLHE-YTQAIDLWSVGCIFGEMLARRQLFPGKnyvHQLQlIMMV 277
Cdd:cd06629 153 GISKK-----SDDIYGNNGATSMQgsvFWMAPEVIHSQGQgYSAKVDIWSLGCVVLEMLAGRRPWSDD---EAIA-AMFK 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 278 LGTPSPAviqavgaervrayiqslPprqPVPWET-VYPGadrqALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd06629 224 LGNKRSA-----------------P---PVPEDVnLSPE----ALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-348 1.41e-26

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: 110.59  E-value: 1.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpNAFDVVTNAKRTL-RELKILKHFKHDNIIAIKDILRptvpygEFK 131
Cdd:cd14086   1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKII-NTKKLSARDHQKLeREARICRLLKHPNIVRLHDSIS------EEG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV---NENCELKIGDFGMArgL 207
Cdd:cd14086  74 FHYLVFDLVTGgELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLA--I 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 CTSPAEHQYFmtEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIfgemlarrqlfpgknyvhqlqLIMMVLGTPSpavIQ 287
Cdd:cd14086 152 EVQGDQQAWF--GFAGTPGYLSPEV-LRKDPYGKPVDIWACGVI---------------------LYILLVGYPP---FW 204
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497 288 AVGAERVRAYIQSLPPRQPVP-WETVYPgadrQALSLLGRMLRFEPSARISAAAALRHPFLA 348
Cdd:cd14086 205 DEDQHRLYAQIKAGAYDYPSPeWDTVTP----EAKDLINQMLTVNPAKRITAAEALKHPWIC 262
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
53-351 1.66e-26

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


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 111.72  E-value: 1.66e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfdvVTNAKRTLRELKILKHFKHDNIIAIkDILRPTVPYGEFKS 132
Cdd:cd14228  15 NSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNH---PSYARQGQIEVSILSRLSSENADEY-NFVRSYECFQHKNH 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMESDLHQIIHSSQ--PLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL----VNENCELKIGDFGMA-- 204
Cdd:cd14228  91 TCLVFEMLEQNLYDFLKQNKfsPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMlvdpVRQPYRVKVIDFGSAsh 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 --RGLCTSpaehqyfmteYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPS 282
Cdd:cd14228 171 vsKAVCST----------YLQSRYYRAPEIILGL-PFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 283 PAVIQA--------------------------------VGAERVRAYI-QSLPPRQPVPWETVYPGAD--------RQAL 321
Cdd:cd14228 240 EYLLSAgtktsrffnrdpnlgyplwrlktpeeheletgIKSKEARKYIfNCLDDMAQVNMSTDLEGTDmlaekadrREYI 319
                       330       340       350
                ....*....|....*....|....*....|
gi 20986497 322 SLLGRMLRFEPSARISAAAALRHPFLAKYH 351
Cdd:cd14228 320 DLLKKMLTIDADKRITPLKTLNHPFVTMTH 349
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
55-267 2.16e-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: 108.89  E-value: 2.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRlTGQQVAIKKIPNafDVVTNAKRTL---RELKILKHFKHDNIIAIKDILRPTvpygefK 131
Cdd:cd14161   5 YEFLETLGKGTYGRVKKARDS-SGRLVAIKSIRK--DRIKDEQDLLhirREIEIMSSLNHPHIISVYEVFENS------S 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLM-ESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA------ 204
Cdd:cd14161  76 KIVIVMEYAsRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSnlynqd 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 205 ---RGLCTSPAehqYFMTEYVATRWYRAPElmlslheytqaIDLWSVGCIFGEMLARRQLFPGKNY 267
Cdd:cd14161 156 kflQTYCGSPL---YASPEIVNGRPYIGPE-----------VDSWSLGVLLYILVHGTMPFDGHDY 207
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
55-347 2.94e-26

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: 108.51  E-value: 2.94e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRptvpygEFKSVY 134
Cdd:cd08225   2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQ------ENGRLF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLME-SDLHQIIHSSQPLTLE--HVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCEL-KIGDFGMARGLCTS 210
Cdd:cd08225  76 IVMEYCDgGDLMKRINRQRGVLFSedQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 211 paehQYFMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYvHQLQLIMmvlgtpspaviqavg 290
Cdd:cd08225 156 ----MELAYTCVGTPYYLSPEICQN-RPYNNKTDIWSLGCVLYELCTLKHPFEGNNL-HQLVLKI--------------- 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 291 aerVRAYIQSlpprqpvpwetVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd08225 215 ---CQGYFAP-----------ISPNFSRDLRSLISQLFKVSPRDRPSITSILKRPFL 257
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
54-283 5.07e-26

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: 107.75  E-value: 5.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKI--PNAFDVVTNAKRtlrELKILKHFKHDNIIAIKDilrptvpygEFK 131
Cdd:cd08219   1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIrlPKSSSAVEDSRK---EAVLLAKMKHPNIVAFKE---------SFE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 S---VYVVLDLMES-DLHQII--HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd08219  69 AdghLYIVMEYCDGgDLMQKIklQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 206 gLCTSPAEhqyFMTEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHqlqLIMMVL-GTPSP 283
Cdd:cd08219 149 -LLTSPGA---YACTYVGTPYYVPPEIWENM-PYNNKSDIWSLGCILYELCTLKHPFQANSWKN---LILKVCqGSYKP 219
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
61-347 5.20e-26

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: 108.39  E-value: 5.20e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTL-------RELKILKHFKHDNIIAIKD---------ILRPT 124
Cdd:cd06628   8 IGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENKDRKKsmldalqREIALLRELQHENIVQYLGsssdanhlnIFLEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 125 VPYGefkSVYVVLDLmesdlhqiiHSSQPLTLehVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA 204
Cdd:cd06628  88 VPGG---SVATLLNN---------YGAFEESL--VRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGIS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RGLctspaEHQYFMTEYVATR-------WYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhQLQLIMMV 277
Cdd:cd06628 154 KKL-----EANSLSTKNNGARpslqgsvFWMAPEVVKQT-SYTRKADIWSLGCLVVEMLTGTHPFPDCT---QMQAIFKI 224
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 278 LGTPSPAviqavgaervrayiqslPPrqpvpwetvyPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd06628 225 GENASPT-----------------IP----------SNISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
55-348 5.86e-26

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: 108.54  E-value: 5.86e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVA---IKKIPNAFDvvtnaKRTLRELKILKHFKHDNIIAIKDILRPTVPYgefk 131
Cdd:cd14166   5 FIFMEVLGSGAFSEVYLVKQRSTGKLYAlkcIKKSPLSRD-----SSLENEIAVLKRIKHENIVTLEDIYESTTHY---- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 svYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV---NENCELKIGDFGMargl 207
Cdd:cd14166  76 --YLVMQLVSGgELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGL---- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 ctSPAEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMmvlgtpspaviq 287
Cdd:cd14166 150 --SKMEQNGIMSTACGTPGYVAPEV-LAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIK------------ 214
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 288 avgaervRAYIQSLPPRqpvpWETVypgaDRQALSLLGRMLRFEPSARISAAAALRHPFLA 348
Cdd:cd14166 215 -------EGYYEFESPF----WDDI----SESAKDFIRHLLEKNPSKRYTCEKALSHPWII 260
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
54-306 7.07e-26

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: 107.51  E-value: 7.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPnaFDVVTNAKRT--LRELKILKHFKHDNIIAIKDilrptvPYGEFK 131
Cdd:cd08220   1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIP--VEQMTKEERQaaLNEVKVLSMLHHPNIIEYYE------SFLEDK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMES-DLHQIIHSSQPLTL--EHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCEL-KIGDFGMARGL 207
Cdd:cd08220  73 ALMIVMEYAPGgTLFEYIQQRKGSLLseEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISKIL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 CT-SPAehqyfmTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMvlGTPSPavI 286
Cdd:cd08220 153 SSkSKA------YTVVGTPCYISPELCEG-KPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMR--GTFAP--I 221
                       250       260
                ....*....|....*....|....
gi 20986497 287 QAVGAERVRAYIQSL----PPRQP 306
Cdd:cd08220 222 SDRYSEELRHLILSMlhldPNKRP 245
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
61-345 7.13e-26

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: 107.35  E-value: 7.13e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRtlrELKILKHFKHDNIIAIKDILRPTvpygefKSVYVVLDLM 140
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKKEAVLR---EISILNQLQHPRIIQLHEAYESP------TELVLILELC 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 ES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE--LKIGDFGMARGLctSPAEHQYF 217
Cdd:cd14006  72 SGgELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSpqIKIIDFGLARKL--NPGEELKE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 218 MT---EYVatrwyrAPElmlsLHEY---TQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVlgtpspaviqavga 291
Cdd:cd14006 150 IFgtpEFV------APE----IVNGepvSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISAC-------------- 205
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 20986497 292 eRVRAyiqslpprQPVPWETVYPGADRQALSLLGRmlrfEPSARISAAAALRHP 345
Cdd:cd14006 206 -RVDF--------SEEYFSSVSQEAKDFIRKLLVK----EPRKRPTAQEALQHP 246
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
46-351 1.10e-25

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


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 109.41  E-value: 1.10e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  46 DVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfdvVTNAKRTLRELKILKHFKHDNIIAIkDILRPTV 125
Cdd:cd14227   8 EVLCSMTNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNH---PSYARQGQIEVSILARLSTESADDY-NFVRAYE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 PYGEFKSVYVVLDLMESDLHQIIHSSQ--PLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV----NENCELKIG 199
Cdd:cd14227  84 CFQHKNHTCLVFEMLEQNLYDFLKQNKfsPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpsRQPYRVKVI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 200 DFGMA----RGLCTSpaehqyfmteYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIM 275
Cdd:cd14227 164 DFGSAshvsKAVCST----------YLQSRYYRAPEIILGL-PFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYIS 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 276 MVLGTPSPAVIQA--------------------------------VGAERVRAYI-QSLPPRQPVPWETVYPGAD----- 317
Cdd:cd14227 233 QTQGLPAEYLLSAgtkttrffnrdtdspyplwrlktpedheaetgIKSKEARKYIfNCLDDMAQVNMTTDLEGSDmlvek 312
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 20986497 318 ---RQALSLLGRMLRFEPSARISAAAALRHPFLAKYH 351
Cdd:cd14227 313 adrREFIDLLKKMLTIDADKRITPIETLNHPFVTMTH 349
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
58-348 1.32e-25

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: 106.80  E-value: 1.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  58 IETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKdilrptvPYGEFKS---VY 134
Cdd:cd05611   1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMMIQGESPYVAK-------LYYSFQSkdyLY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLD-LMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR-GLCTSPA 212
Cdd:cd05611  74 LVMEyLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRnGLEKRHN 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 213 EhqyfmtEYVATRWYRAPELMLSLHEyTQAIDLWSVGCIFGEMLarrqlfpgknyvhqlqlimmvLGTPSpaviqaVGAE 292
Cdd:cd05611 154 K------KFVGTPDYLAPETILGVGD-DKMSDWWSLGCVIFEFL---------------------FGYPP------FHAE 199
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 293 RVRAYIQSLPPRQpVPW-ETVYPGADRQALSLLGRMLRFEPSARISAAAAL---RHPFLA 348
Cdd:cd05611 200 TPDAVFDNILSRR-INWpEEVKEFCSPEAVDLINRLLCMDPAKRLGANGYQeikSHPFFK 258
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
51-347 1.54e-25

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


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 107.02  E-value: 1.54e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  51 VGD-EYEIIETIGNGAYGVVSSAR-RRLTGQQVAIKKIpNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDIlrPTVPyg 128
Cdd:cd14201   3 VGDfEYSRKDLVGHGAFAVVFKGRhRKKTDWEVAIKSI-NKKNLSKSQILLGKEIKILKELQHENIVALYDV--QEMP-- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 efKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVN---------ENCELKI 198
Cdd:cd14201  78 --NSVFLVMEYCNGgDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIKI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 199 GDFGMAR---------GLCTSPAehqyfmteyvatrwYRAPELMLSLHeYTQAIDLWSVGCIFGEMLarrqlfpgknyvh 269
Cdd:cd14201 156 ADFGFARylqsnmmaaTLCGSPM--------------YMAPEVIMSQH-YDAKADLWSIGTVIYQCL------------- 207
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 270 qlqlimmvLGTPSpavIQAVGAERVRAYIQSLPPRQP-VPWETvypgaDRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14201 208 --------VGKPP---FQANSPQDLRMFYEKNKNLQPsIPRET-----SPYLADLLLGLLQRNQKDRMDFEAFFSHPFL 270
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
53-257 1.57e-25

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: 107.28  E-value: 1.57e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfDVVTN--AKRTLRELKILKHFKHDNIIAIkdilrptvpYGEF 130
Cdd:cd05580   1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKA-KIIKLkqVEHVLNEKRILSEVRHPFIVNL---------LGSF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 ---KSVYVVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARG 206
Cdd:cd05580  71 qddRNLYMVMEYVPgGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKR 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 20986497 207 LctspAEHQYFMteyVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLA 257
Cdd:cd05580 151 V----KDRTYTL---CGTPEYLAPEIILS-KGHGKAVDWWALGILIYEMLA 193
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
61-347 1.83e-25

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: 106.62  E-value: 1.83e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIkdilrptvpYGefksVYV----V 136
Cdd:cd06626   8 IGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRY---------YG----VEVhreeV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 137 LDLME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA-----RGL 207
Cdd:cd06626  75 YIFMEycqeGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAvklknNTT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 CTSPAEhqyfMTEYVATRWYRAPELMLS--LHEYTQAIDLWSVGCIFGEMLARRQlfPGKNYVHQLQlIMMVLG---TPs 282
Cdd:cd06626 155 TMAPGE----VNSLVGTPAYMAPEVITGnkGEGHGRAADIWSLGCVVLEMATGKR--PWSELDNEWA-IMYHVGmghKP- 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 283 paviqavgaervrayiqSLPPRQPVpwetvypgaDRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd06626 227 -----------------PIPDSLQL---------SPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
61-345 2.68e-25

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: 105.80  E-value: 2.68e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIK--------KIPNAFDVVTnakrtlRELKILKHFKHDNIIAIKDILrptvpYGEFK- 131
Cdd:cd14119   1 LGEGSYGKVKEVLDTETLCRRAVKilkkrklrRIPNGEANVK------REIQILRRLNHRNVIKLVDVL-----YNEEKq 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQIIHSSQ----PLTLEHvRYFLyQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL 207
Cdd:cd14119  70 KLYMVMEYCVGGLQEMLDSAPdkrlPIWQAH-GYFV-QLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEAL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 CTspaehqyFMTEYVATRWY-----RAPELMLSLHEYT-QAIDLWSVGCIFGEMLARRQLFPGKNyvhqlqlIMMVLGTP 281
Cdd:cd14119 148 DL-------FAEDDTCTTSQgspafQPPEIANGQDSFSgFKVDIWSAGVTLYNMTTGKYPFEGDN-------IYKLFENI 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 282 SPAVIQavgaervrayiqsLPPRQPVPWEtvypgadrqalSLLGRMLRFEPSARISAAAALRHP 345
Cdd:cd14119 214 GKGEYT-------------IPDDVDPDLQ-----------DLLRGMLEKDPEKRFTIEQIRQHP 253
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
54-347 4.08e-25

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: 105.76  E-value: 4.08e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRrLTGQQVAIKKIpnAFDVVTNAKRT--LRELKILKHFKH-DNIIAIKDilrptvpY--- 127
Cdd:cd14131   2 PYEILKQLGKGGSSKVYKVLN-PKKKIYALKRV--DLEGADEQTLQsyKNEIELLKKLKGsDRIIQLYD-------Yevt 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 128 GEFKSVYVVLDLMESDLHQIIHS--SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSN-LLVNENceLKIGDFGMA 204
Cdd:cd14131  72 DEDDYLYMVMECGEIDLATILKKkrPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANfLLVKGR--LKLIDFGIA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RGLCTSPA----EHQyfmteyVATRWYRAPELML--SLHEYTQAI-------DLWSVGCIFGEMLARRQLFPG-KNYVHQ 270
Cdd:cd14131 150 KAIQNDTTsivrDSQ------VGTLNYMSPEAIKdtSASGEGKPKskigrpsDVWSLGCILYQMVYGKTPFQHiTNPIAK 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 271 LQLIMmvlgTPSPAVIQavgaervrayiqslpPRQPVPWetvypgadrqALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14131 224 LQAII----DPNHEIEF---------------PDIPNPD----------LIDVMKRCLQRDPKKRPSIPELLNHPFL 271
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
54-347 6.20e-25

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: 105.26  E-value: 6.20e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVV-----SSARRRLTGQQVAIKKIPNAfDVVTNAK--RTLRELKILKHFKHDNIIAIKDILRPTVP 126
Cdd:cd14076   2 PYILGRTLGEGEFGKVklgwpLPKANHRSGVQVAIKLIRRD-TQQENCQtsKIMREINILKGLTHPNIVRLLDVLKTKKY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 YGefksvyVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd14076  81 IG------IVLEFVSGgELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFAN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 206 GLCTSPAEhqyFMTEYVATRWYRAPELMLSLHEYT-QAIDLWSVGCIFGEMLARRQLFpgknyvhqlqlimmvlgTPSPA 284
Cdd:cd14076 155 TFDHFNGD---LMSTSCGSPCYAAPELVVSDSMYAgRKADIWSCGVILYAMLAGYLPF-----------------DDDPH 214
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 285 VIQAVGAERVRAYIQSLPPRQPvpwETVYPgadrQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14076 215 NPNGDNVPRLYRYICNTPLIFP---EYVTP----KARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
54-266 6.35e-25

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: 104.89  E-value: 6.35e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDilrptvPYGEFKSV 133
Cdd:cd08218   1 KYVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQE------SFEENGNL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMES-DLHQIIHSSQ--PLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLcTS 210
Cdd:cd08218  75 YIVMDYCDGgDLYKRINAQRgvLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVL-NS 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 211 PAEhqyFMTEYVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKN 266
Cdd:cd08218 154 TVE---LARTCIGTPYYLSPE-ICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGN 205
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
54-345 6.96e-25

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: 104.71  E-value: 6.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnafdvvtnAKRTLR--------ELKILKHFKHDNIIA-IKDILRPT 124
Cdd:cd14095   1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKII---------DKAKCKgkehmienEVAILRRVKHPNIVQlIEEYDTDT 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 125 vpygefkSVYVVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE----LKIG 199
Cdd:cd14095  72 -------ELYLVMELVKgGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDgsksLKLA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 200 DFGMARgLCTSPaehqyfMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIfgemlarrqlfpgknyvhqlqLIMMVLG 279
Cdd:cd14095 145 DFGLAT-EVKEP------LFTVCGTPTYVAPEI-LAETGYGLKVDIWAAGVI---------------------TYILLCG 195
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 280 TP---SPAVIQavgaERVRAYIQS-----LPPRqpvpWETVYPGADrqalSLLGRMLRFEPSARISAAAALRHP 345
Cdd:cd14095 196 FPpfrSPDRDQ----EELFDLILAgefefLSPY----WDNISDSAK----DLISRMLVVDPEKRYSAGQVLDHP 257
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
53-346 8.61e-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: 104.34  E-value: 8.61e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfdvVTNAKRTL--RELKILKHFKHDNIIA-IKDILRPTvpyge 129
Cdd:cd14184   1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKA---KCCGKEHLieNEVSILRRVKHPNIIMlIEEMDTPA----- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 fkSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE----LKIGDFGMA 204
Cdd:cd14184  73 --ELYLVMELVKGgDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDgtksLKLGDFGLA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RgLCTSPaehqyfMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQ---LQLIMMVLGTP 281
Cdd:cd14184 151 T-VVEGP------LYTVCGTPTYVAPEI-IAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEdlfDQILLGKLEFP 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 282 SPAviqavgaervrayiqslpprqpvpWETVYPGADRqalsLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd14184 223 SPY------------------------WDNITDSAKE----LISHMLQVNVEARYTAEQILSHPW 259
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
55-251 1.12e-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: 104.03  E-value: 1.12e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEII--ETIGNGAYGVVSSARRRLTGQQVAIKKIpNAFDVVTNAKRTLR-ELKILKHFKHDNIIAIKDILRPTvpygefK 131
Cdd:cd14082   3 YQIFpdEVLGSGQFGIVYGGKHRKTGRDVAIKVI-DKLRFPTKQESQLRnEVAILQQLSHPGVVNLECMFETP------E 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQIIHSSQPLTL-EHV-RYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENC---ELKIGDFGMARG 206
Cdd:cd14082  76 RVFVVMEKLHGDMLEMILSSEKGRLpERItKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARI 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 20986497 207 LctspaEHQYFMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCI 251
Cdd:cd14082 156 I-----GEKSFRRSVVGTPAYLAPEVLRN-KGYNRSLDMWSVGVI 194
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
53-310 1.22e-24

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: 104.81  E-value: 1.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKI---PNAfDVvtnAKRTLRELKILKHFKHDNIIAIkdilrptvpYGE 129
Cdd:cd06621   1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTIttdPNP-DV---QKQILRELEINKSCASPYIVKY---------YGA 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 F-----KSVYVVLDLMES----DLHQIIHSSQPLTLEHV-RYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIG 199
Cdd:cd06621  68 FldeqdSSIGIAMEYCEGgsldSIYKKVKKKGGRIGEKVlGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLC 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 200 DFGMARGLCTSPAehqyfMTeYVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLARRQLFP--GKNYVHQLQLIMMV 277
Cdd:cd06621 148 DFGVSGELVNSLA-----GT-FTGTSYYMAPE-RIQGGPYSITSDVWSLGLTLLEVAQNRFPFPpeGEPPLGPIELLSYI 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 20986497 278 LGTPSPAVIQAVGAERV-----RAYIQSL----PPRQPVPWE 310
Cdd:cd06621 221 VNMPNPELKDEPENGIKwsesfKDFIEKClekdGTRRPGPWQ 262
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
59-324 1.43e-24

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: 104.00  E-value: 1.43e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRltGQQVAIKKIpNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVP--YGefksvyvv 136
Cdd:cd13979   9 EPLGSGGFGSVYKATYK--GETVAVKIV-RRRRKNRASRQSFWAELNAARLRHENIVRVLAAETGTDFasLG-------- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 137 LDLME----SDLHQIIH-SSQPLTLEH-VRYFLyQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLcTS 210
Cdd:cd13979  78 LIIMEycgnGTLQQLIYeGSEPLPLAHrILISL-DIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKL-GE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 211 PAEHQYFMTEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVG 290
Cdd:cd13979 156 GNEVGTPRSHIGGTYTYRAPELLKGE-RVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYAVVAKDLRPDLSGLEDSEF 234
                       250       260       270
                ....*....|....*....|....*....|....
gi 20986497 291 AERVRAYIQSLPPRQPvpweTVYPGADRQALSLL 324
Cdd:cd13979 235 GQRLRSLISRCWSAQP----AERPNADESLLKSL 264
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
52-357 1.82e-24

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: 104.33  E-value: 1.82e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  52 GDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdVVTNAKRT-LRELKILKHF-KHDNIIAIKDIlrptvpYGE 129
Cdd:cd14177   3 TDVYELKEDIGVGSYSVCKRCIHRATNMEFAVK-------IIDKSKRDpSEEIEILMRYgQHPNIITLKDV------YDD 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENC----ELKIGDFGMA 204
Cdd:cd14177  70 GRYVYLVTELMKGgELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSanadSIRICDFGFA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RGLctsPAEHQYFMTE-YVATrwYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFP-GKNyvhqlqlimmvlGTPS 282
Cdd:cd14177 150 KQL---RGENGLLLTPcYTAN--FVAPEVLMR-QGYDAACDIWSLGVLLYTMLAGYTPFAnGPN------------DTPE 211
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 283 PAVIQaVGAERVrayiqSLPPRQpvpWETVYPGADrqalSLLGRMLRFEPSARISAAAALRHPFLA-KYHDPDDEP 357
Cdd:cd14177 212 EILLR-IGSGKF-----SLSGGN---WDTVSDAAK----DLLSHMLHVDPHQRYTAEQVLKHSWIAcRDQLPHYQL 274
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
54-300 2.15e-24

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: 103.74  E-value: 2.15e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQV-AIKKI--PNAFDVVTNAKR------TLRELKILK-HFKHDNIIaikdilRP 123
Cdd:cd08528   1 EYAVLELLGSGAFGCVYKVRKKSNGQTLlALKEInmTNPAFGRTEQERdksvgdIISEVNIIKeQLRHPNIV------RY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 124 TVPYGEFKSVYVVLDLME-SDLHQIIHS----SQPLTLEHVRYFLYQLLRGLKYMH-SAQVIHRDLKPSNLLVNENCELK 197
Cdd:cd08528  75 YKTFLENDRLYIVMELIEgAPLGEHFSSlkekNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 198 IGDFGMARglctSPAEHQYFMTEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhQLQLIMMV 277
Cdd:cd08528 155 ITDFGLAK----QKGPESSKMTSVVGTILYSCPEIVQNE-PYGEKADIWALGCILYQMCTLQPPFYSTN---MLTLATKI 226
                       250       260
                ....*....|....*....|...
gi 20986497 278 LGTPSPAVIQAVGAERVRAYIQS 300
Cdd:cd08528 227 VEAEYEPLPEGMYSDDITFVIRS 249
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
61-275 2.23e-24

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: 103.30  E-value: 2.23e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGefksvyVVLDLM 140
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLG------LVMEYM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 ES-DLHQIIHSSQPLTLEHVRY-FLYQLLRGLKYMHSAQ--VIHRDLKPSNLLVNENCELKIGDFGMAR-GLCTSPAEHQ 215
Cdd:cd13978  75 ENgSLKSLLEREIQDVPWSLRFrIIHEIALGMNFLHNMDppLLHHDLKPENILLDNHFHVKISDFGLSKlGMKSISANRR 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 216 YFMTEYVATRWYRAPELM-LSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKnyVHQLQlIM 275
Cdd:cd13978 155 RGTENLGGTPIYMAPEAFdDFNKKPTSKSDVYSFAIVIWAVLTRKEPFENA--INPLL-IM 212
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
53-350 2.66e-24

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: 103.46  E-value: 2.66e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKR-------TLRELKILKHFK-HDNIIAIKDilrpt 124
Cdd:cd14182   3 EKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGSFSPEEvqelreaTLKEIDILRKVSgHPNIIQLKD----- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 125 vPYGEFKSVYVVLDLM-ESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGM 203
Cdd:cd14182  78 -TYETNTFFFLVFDLMkKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 204 ARGLctSPAEHqyfMTEYVATRWYRAPEL----MLSLHE-YTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIM--- 275
Cdd:cd14182 157 SCQL--DPGEK---LREVCGTPGYLAPEIiecsMDDNHPgYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMsgn 231
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 276 MVLGTPSpaviqavgaervrayiqslpprqpvpWEtvypgaDRQ--ALSLLGRMLRFEPSARISAAAALRHPFLAKY 350
Cdd:cd14182 232 YQFGSPE--------------------------WD------DRSdtVKDLISRFLVVQPQKRYTAEEALAHPFFQQY 276
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
53-347 3.69e-24

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: 104.33  E-value: 3.69e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYG-VVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFK 131
Cdd:cd14215  12 ERYEIVSTLGEGTFGrVVQCIDHRRGGARVALKIIKNVEKYKEAARLEINVLEKINEKDPENKNLCVQMFDWFDYHGHMC 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQIiHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL-VNENCEL-------------- 196
Cdd:cd14215  92 ISFELLGLSTFDFLKE-NNYLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILfVNSDYELtynlekkrdersvk 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 197 ----KIGDFGMArglcTSPAEHQyfmTEYVATRWYRAPELMLSLHeYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQ 272
Cdd:cd14215 171 staiRVVDFGSA----TFDHEHH---STIVSTRHYRAPEVILELG-WSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLA 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 273 LIMMVLGtPSPAviQAVGAERVRAYI-------------------QSLPPRQPVPWETvypGADRQALSLLGRMLRFEPS 333
Cdd:cd14215 243 MMERILG-PIPS--RMIRKTRKQKYFyhgrldwdentsagryvreNCKPLRRYLTSEA---EEHHQLFDLIESMLEYEPS 316
                       330
                ....*....|....
gi 20986497 334 ARISAAAALRHPFL 347
Cdd:cd14215 317 KRLTLAAALKHPFF 330
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
61-348 4.10e-24

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: 102.52  E-value: 4.10e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIpnafDVVTNAKRTL--RELKILKHFKHDNIIAIkdilrptvpYGEF---KSVYV 135
Cdd:cd06648  15 IGEGSTGIVCIATDKSTGRQVAVKKM----DLRKQQRRELlfNEVVIMRDYQHPNIVEM---------YSSYlvgDELWV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 136 VLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGmargLCTSPAEHQ 215
Cdd:cd06648  82 VMEFLEGGALTDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFG----FCAQVSKEV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 216 YFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGcifgemlarrqlfpgknyvhqLQLIMMVLGTP-----SPavIQAVg 290
Cdd:cd06648 158 PRRKSLVGTPYWMAPEV-ISRLPYGTEVDIWSLG---------------------IMVIEMVDGEPpyfnePP--LQAM- 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 291 aERVRayiQSLPPRQPVPwETVYPgadrQALSLLGRMLRFEPSARISAAAALRHPFLA 348
Cdd:cd06648 213 -KRIR---DNEPPKLKNL-HKVSP----RLRSFLDRMLVRDPAQRATAAELLNHPFLA 261
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
53-347 4.68e-24

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: 103.17  E-value: 4.68e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdVVTNAKRT-LRELKIL-KHFKHDNIIAIKDIlrptvpYGEF 130
Cdd:cd14178   3 DGYEIKEDIGIGSYSVCKRCVHKATSTEYAVK-------IIDKSKRDpSEEIEILlRYGQHPNIITLKDV------YDDG 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENC----ELKIGDFGMAR 205
Cdd:cd14178  70 KFVYLVMELMRGgELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESgnpeSIRICDFGFAK 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 206 GLctsPAEHQYFMTE-YVATrwYRAPELmLSLHEYTQAIDLWSVGCIFGEMLArrQLFPGKNYVHQL-QLIMMVLGTPSP 283
Cdd:cd14178 150 QL---RAENGLLMTPcYTAN--FVAPEV-LKRQGYDAACDIWSLGILLYTMLA--GFTPFANGPDDTpEEILARIGSGKY 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 284 AViqaVGAErvrayiqslpprqpvpWETVYPGADrqalSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14178 222 AL---SGGN----------------WDSISDAAK----DIVSKMLHVDPHQRLTAPQVLRHPWI 262
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
55-347 4.69e-24

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: 102.53  E-value: 4.69e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNA-------------KRTLRELKILKHFKHDNIIAIKDIL 121
Cdd:cd14077   3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAGLKKerekrlekeisrdIRTIREAALSSLLNHPHICRLRDFL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 122 RPTVPYgefksvYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGD 200
Cdd:cd14077  83 RTPNHY------YMLFEYVDGgQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIID 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 201 FGMARGLCTSPAEHQYFMTEYVAtrwyrAPELmLSLHEYT-QAIDLWSVGCIFGEMLARRQLFPGKNyvhqlqlimmvlg 279
Cdd:cd14077 157 FGLSNLYDPRRLLRTFCGSLYFA-----APEL-LQAQPYTgPEVDVWSFGVVLYVLVCGKVPFDDEN------------- 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 280 tpSPAVIQAVGAERVRayiqslpprqpvpwetvYPG-ADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14077 218 --MPALHAKIKKGKVE-----------------YPSyLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
59-347 5.09e-24

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: 102.51  E-value: 5.09e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRlTGQQVAIKKIP-NAFDVVTNAK---RTLRELKILKHFKHDNIIAIkdilrptvpYGEFKSVY 134
Cdd:cd06631   7 NVLGKGAYGTVYCGLTS-TGQLIAVKQVElDTSDKEKAEKeyeKLQEEVDLLKTLKHVNIVGY---------LGTCLEDN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLC-- 208
Cdd:cd06631  77 VVSIFMEfvpgGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCin 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQlfPGKNyvhqlqlimmvlgTPSPAVIQA 288
Cdd:cd06631 157 LSSGSQSQLLKSMRGTPYWMAPEV-INETGHGRKSDIWSIGCTVFEMATGKP--PWAD-------------MNPMAAIFA 220
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 289 VGAERvrayiqSLPPRQPVPWETvypgadrQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd06631 221 IGSGR------KPVPRLPDKFSP-------EARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
55-347 5.22e-24

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: 102.08  E-value: 5.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKkIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTvpygefKSVY 134
Cdd:cd14078   5 YELHETIGSGGFAKVKLATHILTGEKVAIK-IMDKKALGDDLPRVKTEIEALKNLSHQHICRLYHVIETD------NKIF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA----RGL-- 207
Cdd:cd14078  78 MVLEYCPGgELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCakpkGGMdh 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 -----CTSPAehqyfmteyvatrwYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhqlqliMMVLgtps 282
Cdd:cd14078 158 hletcCGSPA--------------YAAPELIQGKPYIGSEADVWSMGVLLYALLCGFLPFDDDN--------VMAL---- 211
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 283 paviqavgaervraY--IQSLPPRQPvPWETvypgadRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14078 212 --------------YrkIQSGKYEEP-EWLS------PSSKLLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
61-346 5.41e-24

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: 102.05  E-value: 5.41e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKI---PNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRptvpygEFKSVYVVL 137
Cdd:cd06625   8 LGQGAFGQVYLCYDADTGRELAVKQVeidPINTEASKEVKALECEIQLLKNLQHERIVQYYGCLQ------DEKSLSIFM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 138 DLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL---CTSPAe 213
Cdd:cd06625  82 EYMPGgSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLqtiCSSTG- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 214 hqyfMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQlfPGKNYVHQLQLIMMVLGTPSPaviqavgaer 293
Cdd:cd06625 161 ----MKSVTGTPYWMSPEVING-EGYGRKADIWSVGCTVVEMLTTKP--PWAEFEPMAAIFKIATQPTNP---------- 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 20986497 294 vrayiqSLPprqpvpwetvyPGADRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd06625 224 ------QLP-----------PHVSEDARDFLSLIFVRNKKQRPSAEELLSHSF 259
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
54-347 6.07e-24

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: 102.10  E-value: 6.07e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIET-----IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDvvTNAKRTLRELKILKHFKHDNII---------AIKD 119
Cdd:cd06624   4 EYEYDESgervvLGKGTFGVVYAARDLSTQVRIAIKEIPERDS--REVQPLHEEIALHSRLSHKNIVqylgsvsedGFFK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 120 ILRPTVPYGEFKSvyvvldLMESDLHQIIHSSQPltlehVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNE-NCELKI 198
Cdd:cd06624  82 IFMEQVPGGSLSA------LLRSKWGPLKDNENT-----IGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 199 GDFGMARGL-----CTspaehqyfmTEYVATRWYRAPELMLS-LHEYTQAIDLWSVGCIFGEMLArrqlfpGKNYVHQlq 272
Cdd:cd06624 151 SDFGTSKRLaginpCT---------ETFTGTLQYMAPEVIDKgQRGYGPPADIWSLGCTIIEMAT------GKPPFIE-- 213
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 273 limmvLGTPSPAVIQaVGAERVRAYIqslpPRQpvpwetvypgADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd06624 214 -----LGEPQAAMFK-VGMFKIHPEI----PES----------LSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
54-256 6.20e-24

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: 102.59  E-value: 6.20e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYgefkSV 133
Cdd:cd14049   7 EFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWMEHVQL----ML 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMESDLHQII-----------HSSQPLTLEHVRY---FLYQLLRGLKYMHSAQVIHRDLKPSNLLVN-ENCELKI 198
Cdd:cd14049  83 YIQMQLCELSLWDWIvernkrpceeeFKSAPYTPVDVDVttkILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRI 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 199 GDFGMARGLCTSPAEHQYFM--------TEYVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd14049 163 GDFGLACPDILQDGNDSTTMsrlnglthTSGVGTCLYAAPE-QLEGSHYDFKSDMYSIGVILLELF 227
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
55-347 6.34e-24

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: 101.76  E-value: 6.34e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIP-NAFDVVTNAKRTLRELKILKHFKHDNIIaikdilrptvpygEFKSV 133
Cdd:cd06607   3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSySGKQSTEKWQDIIKEVKFLRQLRHPNTI-------------EYKGC 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLD----LME------SDLHQIiHSsQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGM 203
Cdd:cd06607  70 YLREHtawlVMEyclgsaSDIVEV-HK-KPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGS 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 204 ARGLCtsPAehqyfmTEYVATRWYRAPELMLSLHE--YTQAIDLWSVG--CIfgEMLARRQLFPGKNYVHQLQLIMmvlg 279
Cdd:cd06607 148 ASLVC--PA------NSFVGTPYWMAPEVILAMDEgqYDGKVDVWSLGitCI--ELAERKPPLFNMNAMSALYHIA---- 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 280 tpspaviqavgaervrayiQSLPPR-QPVPWETVYpgadrqaLSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd06607 214 -------------------QNDSPTlSSGEWSDDF-------RNFVDSCLQKIPQDRPSAEDLLKHPFV 256
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
55-347 1.12e-23

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: 100.93  E-value: 1.12e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILrptvpygEFKS-V 133
Cdd:cd14071   2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVM-------ETKDmL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMArglctspa 212
Cdd:cd14071  75 YLVTEYASNgEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFS-------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 213 ehQYFMTEYVATRW-----YRAPELMLSLHEYTQAIDLWSVGCIFgemlarrqlfpgknYVhqlqLIMMVL---GTPSPA 284
Cdd:cd14071 147 --NFFKPGELLKTWcgsppYAAPEVFEGKEYEGPQLDIWSLGVVL--------------YV----LVCGALpfdGSTLQT 206
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 285 VIQAVGAERVRayiqslpprqpVPWetvYPGADRQalSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14071 207 LRDRVLSGRFR-----------IPF---FMSTDCE--HLIRRMLVLDPSKRLTIEQIKKHKWM 253
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
54-256 1.58e-23

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: 101.74  E-value: 1.58e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSAR-RRLTGQQVAIKKIPNA-----FDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPY 127
Cdd:cd14096   2 NYRLINKIGEGAFSNVYKAVpLRNTGKPVAIKVVRKAdlssdNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 128 gefksvYVVLDLMESD--LHQII---HSSQPLTlehvRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL------------- 189
Cdd:cd14096  82 ------YIVLELADGGeiFHQIVrltYFSEDLS----RHVITQVASAVKYLHEIGVVHRDIKPENLLfepipfipsivkl 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 190 ---------VNENC-----------ELKIGDFGMARGLCTSPAehqyfMTEyVATRWYRAPELMLSLHeYTQAIDLWSVG 249
Cdd:cd14096 152 rkadddetkVDEGEfipgvggggigIVKLADFGLSKQVWDSNT-----KTP-CGTVGYTAPEVVKDER-YSKKVDMWALG 224

                ....*..
gi 20986497 250 CIFGEML 256
Cdd:cd14096 225 CVLYTLL 231
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
55-347 1.63e-23

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: 101.01  E-value: 1.63e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIK-----KIPNafDVVTnaKRTLRELKILKHFKHDNIIAIKDILRPTVPYge 129
Cdd:cd14165   3 YILGINLGEGSYAKVKSAYSERLKCNVAIKiidkkKAPD--DFVE--KFLPRELEILARLNHKSIIKTYEIFETSDGK-- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 fksVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLC 208
Cdd:cd14165  77 ---VYIVMELGVQgDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQlimmvlgtpspavIQA 288
Cdd:cd14165 154 RDENGRIVLSKTFCGSAAYAAPEVLQGIPYDPRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLK-------------IQK 220
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 289 vgAERVRayiqsLPPRQPVpwetvypgaDRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14165 221 --EHRVR-----FPRSKNL---------TSECKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
53-347 1.69e-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: 102.79  E-value: 1.69e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdVVTNAKRT-LRELKIL-KHFKHDNIIAIKDIlrptvpYGEF 130
Cdd:cd14176  19 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVK-------IIDKSKRDpTEEIEILlRYGQHPNIITLKDV------YDDG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL-VNE--NCE-LKIGDFGMAR 205
Cdd:cd14176  86 KYVYVVTELMKGgELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDEsgNPEsIRICDFGFAK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 206 GLctsPAEHQYFMTE-YVATrwYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYvhqlqlimmvlGTPSpA 284
Cdd:cd14176 166 QL---RAENGLLMTPcYTAN--FVAPEV-LERQGYDAACDIWSLGVLLYTMLTGYTPFANGPD-----------DTPE-E 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 285 VIQAVGAERVrayiqSLPPRQpvpWETVypgaDRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14176 228 ILARIGSGKF-----SLSGGY---WNSV----SDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 278
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
53-283 1.86e-23

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: 101.36  E-value: 1.86e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIP-NAFDVVTnaKRTLRELKILKHFKHDNIIAIkdilrptvpYGEF- 130
Cdd:cd06620   5 QDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHiDAKSSVR--KQILRELQILHECHSPYIVSF---------YGAFl 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 -KSVYVVLdLME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSA-QVIHRDLKPSNLLVNENCELKIGDFGMA 204
Cdd:cd06620  74 nENNNIII-CMEymdcGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFGVS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RGLCTSPAehqyfMTeYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKN-----YVHQ---LQLIMM 276
Cdd:cd06620 153 GELINSIA-----DT-FVGTSTYMSPERIQG-GKYSVKSDVWSLGLSIIELALGEFPFAGSNddddgYNGPmgiLDLLQR 225

                ....*..
gi 20986497 277 VLGTPSP 283
Cdd:cd06620 226 IVNEPPP 232
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
61-345 2.24e-23

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: 100.58  E-value: 2.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKI------PNAFDVVTNAKRtlRELKILKHFKHDNIIAIkdiLRPTVPYGEFKsvy 134
Cdd:cd06630   8 LGTGAFSSCYQARDVKTGTLMAVKQVsfcrnsSSEQEEVVEAIR--EEIRMMARLNHPNIVRM---LGATQHKSHFN--- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE-LKIGDFGMARGLCTSPA 212
Cdd:cd06630  80 IFVEWMAGgSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQrLRIADFGAAARLASKGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 213 EHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAviqavgae 292
Cdd:cd06630 160 GAGEFQGQLLGTIAFMAPEV-LRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIASATTPP-------- 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 20986497 293 rvrayiqslpprqPVPwETVYPGADRQALsllgRMLRFEPSARISAAAALRHP 345
Cdd:cd06630 231 -------------PIP-EHLSPGLRDVTL----RCLELQPEDRPPARELLKHP 265
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
53-266 2.54e-23

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: 100.94  E-value: 2.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKkIPNAFDVV--TNAKRTLRELKILKHFKHDNIIAIKDILRptvpygEF 130
Cdd:cd14209   1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMK-ILDKQKVVklKQVEHTLNEKRILQAINFPFLVKLEYSFK------DN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVLDL-----MESDLHQIIHSSQPltleHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd14209  74 SNLYMVMEYvpggeMFSHLRRIGRFSEP----HARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAK 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 206 -------GLCTSPaehqyfmtEYVatrwyrAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKN 266
Cdd:cd14209 150 rvkgrtwTLCGTP--------EYL------APEIILS-KGYNKAVDWWALGVLIYEMAAGYPPFFADQ 202
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
50-347 3.20e-23

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: 100.09  E-value: 3.20e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  50 DVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfdVVTNAKRTL------RELKILKHFKHDNIIAIKDIlrp 123
Cdd:cd14194   2 NVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKR--RTKSSRRGVsredieREVSILKEIQHPNVITLHEV--- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 124 tvpYGEFKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSN-LLVNENC---ELKI 198
Cdd:cd14194  77 ---YENKTDVILILELVAGgELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENiMLLDRNVpkpRIKI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 199 GDFGMARGLCTSPAEHQYFMT-EYVatrwyrAPELM----LSLHEytqaiDLWSVGCIFGEMLARRQLFPGKNYVHQLql 273
Cdd:cd14194 154 IDFGLAHKIDFGNEFKNIFGTpEFV------APEIVnyepLGLEA-----DMWSIGVITYILLSGASPFLGDTKQETL-- 220
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 274 immvlgtpspAVIQAVGAERVRAYIQSlpprqpvpwetvypgADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14194 221 ----------ANVSAVNYEFEDEYFSN---------------TSALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
61-347 3.66e-23

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: 99.93  E-value: 3.66e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDIlrptvpYGEFKSVYVVLDLM 140
Cdd:cd14097   9 LGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEV------FETPKRMYLVMELC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 ES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV-------NENCELKIGDFGMARGLCTSPA 212
Cdd:cd14097  83 EDgELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssiidnNDKLNIKVTDFGLSVQKYGLGE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 213 EHqyfMTEYVATRWYRAPELMlSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAViqavgae 292
Cdd:cd14097 163 DM---LQETCGTPIYMAPEVI-SAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSV------- 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 293 rvrayiqslpprqpvpWETVypgaDRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14097 232 ----------------WQSV----SDAAKNVLQQLLKVDPAHRMTASELLDNPWI 266
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
54-284 4.80e-23

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: 99.43  E-value: 4.80e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRlTGQQVAIKKIPNafDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPygefksV 133
Cdd:cd05148   7 EFTLERKLGSGYFGEVWEGLWK-NRVRVAIKILKS--DDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEP------V 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMES-DLHQIIHSS--QPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL--- 207
Cdd:cd05148  78 YIITELMEKgSLLAFLRSPegQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIked 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 208 CTSPAEHQyfmteyVATRWyRAPElMLSLHEYTQAIDLWSVGCIFGEMLARRQL-FPGKNYVHQLQLIMMVLGTPSPA 284
Cdd:cd05148 158 VYLSSDKK------IPYKW-TAPE-AASHGTFSTKSDVWSFGILLYEMFTYGQVpYPGMNNHEVYDQITAGYRMPCPA 227
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
51-348 9.02e-23

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: 98.56  E-value: 9.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  51 VGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfdvVTNAKRTL--RELKILKHFKHDNIIAIKDIlrptvpYG 128
Cdd:cd14167   1 IRDIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKK---ALEGKETSieNEIAVLHKIKHPNIVALDDI------YE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL---VNENCELKIGDFGMA 204
Cdd:cd14167  72 SGGHLYLIMQLVSGgELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RglCTSPAEhqyFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMmvlgtpspa 284
Cdd:cd14167 152 K--IEGSGS---VMSTACGTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQIL--------- 216
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 285 viqavgaervRAYIQSLPPRqpvpWETVYPGADrqalSLLGRMLRFEPSARISAAAALRHPFLA 348
Cdd:cd14167 217 ----------KAEYEFDSPY----WDDISDSAK----DFIQHLMEKDPEKRFTCEQALQHPWIA 262
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
55-345 1.13e-22

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: 98.65  E-value: 1.13e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSAR-RRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFK---HDNIIAIKDIlrptvpYGEF 130
Cdd:cd14052   2 FANVELIGSGEFSQVYKVSeRVPTGKVYAVKKLKPNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIDS------WEYH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVLDLMES-DLHQIIHS-SQPLTLEHVRYF--LYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARG 206
Cdd:cd14052  76 GHLYIQTELCENgSLDVFLSElGLLGRLDEFRVWkiLVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 207 LctsPAEHqyfMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQlimmvlgtpSPAVI 286
Cdd:cd14052 156 W---PLIR---GIEREGDREYIAPEI-LSEHMYDKPADIFSLGLILLEAAANVVLPDNGDAWQKLR---------SGDLS 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 287 QAVGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHP 345
Cdd:cd14052 220 DAPRLSSTDLHSASSPSSNPPPDPPNMPILSGSLDRVVRWMLSPEPDRRPTADDVLATP 278
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
55-347 1.35e-22

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: 98.26  E-value: 1.35e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGV---VSSARRRLTGQQVAIKKIP----NAFDVVtnakRTLRELKILKHFKHDNIIAIKDilrptvPY 127
Cdd:cd08222   2 YRVVRKLGSGNFGTvylVSDLKATADEELKVLKEISvgelQPDETV----DANREAKLLSKLDHPAIVKFHD------SF 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 128 GEFKSVYVVLDLMES-DLHQIIH----SSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCeLKIGDFG 202
Cdd:cd08222  72 VEKESFCIVTEYCEGgDLDDKISeykkSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNV-IKVGDFG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 203 MARGLCTSPAehqyFMTEYVATRWYRAPELMlsLHE-YTQAIDLWSVGCIFGEMLARRQLFPGKNYVhqlqlimmvlgtp 281
Cdd:cd08222 151 ISRILMGTSD----LATTFTGTPYYMSPEVL--KHEgYNSKSDIWSLGCILYEMCCLKHAFDGQNLL------------- 211
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 282 spAVIQAVgaerVRAYIQSLPPRQPVPWETVYpgadrqalsllGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd08222 212 --SVMYKI----VEGETPSLPDKYSKELNAIY-----------SRMLNKDPALRPSAAEILKIPFI 260
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
54-264 1.56e-22

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: 98.18  E-value: 1.56e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpNAFDVVTNAKRT--LRELKILKHFKHDNIIAIKDilrptvPYGEFK 131
Cdd:cd08228   3 NFQIEKKIGRGQFSEVYRATCLLDRKPVALKKV-QIFEMMDAKARQdcVKEIDLLKQLNHPNVIKYLD------SFIEDN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMES-DLHQII---HSSQPLTLEHV--RYFLyQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd08228  76 ELNIVLELADAgDLSQMIkyfKKQKRLIPERTvwKYFV-QLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGR 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497 206 GLCT-SPAEHQyfmteYVATRWYRAPElmlSLHE--YTQAIDLWSVGCIFGEMLARRQLFPG 264
Cdd:cd08228 155 FFSSkTTAAHS-----LVGTPYYMSPE---RIHEngYNFKSDIWSLGCLLYEMAALQSPFYG 208
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
54-256 1.82e-22

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: 98.41  E-value: 1.82e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKI--PNAfdvVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYG--- 128
Cdd:cd14048   7 DFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIrlPNN---ELAREKVLREVRALAKLDHPGIVRYFNAWLERPPEGwqe 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLM---ESDLHQIIHSSQPLTLEHVRYFLY---QLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFG 202
Cdd:cd14048  84 KMDEVYLYIQMQlcrKENLKDWMNRRCTMESRELFVCLNifkQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFG 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 203 MA------------RGLCTSPAEHqyfmTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEML 256
Cdd:cd14048 164 LVtamdqgepeqtvLTPMPAYAKH----TGQVGTRLYMSPEQIHG-NQYSEKVDIFALGLILFELI 224
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
53-363 2.18e-22

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: 99.67  E-value: 2.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdvvtnakrTLRELKILKHFKHDNIIAIKDIL----RPTVP-- 126
Cdd:cd05573   1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMK--------------ILRKSDMLKREQIAHVRAERDILadadSPWIVrl 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 YGEF---KSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFG 202
Cdd:cd05573  67 HYAFqdeDHLYLVMEYMPGgDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 203 MARGLCTSPAEHQYFMTEY-------------------------VATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLA 257
Cdd:cd05573 147 LCTKMNKSGDRESYLNDSVntlfqdnvlarrrphkqrrvraysaVGTPDYIAPE-VLRGTGYGPECDWWSLGVILYEMLY 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 258 RRQLFPGKNyvhqlqlimmvlgtpspaviQAVGAERVRAYIQSL--PPRQPVPWEtvypgadrqALSLLGRMLRfEPSAR 335
Cdd:cd05573 226 GFPPFYSDS--------------------LVETYSKIMNWKESLvfPDDPDVSPE---------AIDLIRRLLC-DPEDR 275
                       330       340
                ....*....|....*....|....*....
gi 20986497 336 I-SAAAALRHPFLAKYhDPDDEPDCAPPF 363
Cdd:cd05573 276 LgSAEEIKAHPFFKGI-DWENLRESPPPF 303
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
53-354 2.90e-22

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: 97.61  E-value: 2.90e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTnAKRTLRELKILKHFKHDNIIAIkdilrptvpYGEF-- 130
Cdd:cd06622   1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESK-FNQIIMELDILHKAVSPYIVDF---------YGAFfi 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 -KSVYVVLDLMESDLHQIIHSSQPLTL---EHV-RYFLYQLLRGLKYMHSA-QVIHRDLKPSNLLVNENCELKIGDFGMA 204
Cdd:cd06622  71 eGAVYMCMEYMDAGSLDKLYAGGVATEgipEDVlRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGVS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RGLCTSPAEHQyfmteyVATRWYRAPELMLSLH-----EYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQL-QLIMMVL 278
Cdd:cd06622 151 GNLVASLAKTN------IGCQSYMAPERIKSGGpnqnpTYTVQSDVWSLGLSILEMALGRYPYPPETYANIFaQLSAIVD 224
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 279 GTpspaviqavgaervrayiqslPPRQPvpwetvyPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPD 354
Cdd:cd06622 225 GD---------------------PPTLP-------SGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNAD 272
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
58-337 3.18e-22

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: 97.45  E-value: 3.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  58 IETIGNGAYGVVSSAR----RRLTGQQVAIKKiPNAfDVVTNAKRTL-RELKILKHFKHDNIIAIKDILRPT-------- 124
Cdd:cd05038   9 IKQLGEGHFGSVELCRydplGDNTGEQVAVKS-LQP-SGEEQHMSDFkREIEILRTLDHEYIVKYKGVCESPgrrslrli 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 125 ---VPYGEFKsvyvvlDLMESDLHQIIHSSQPLtlehvryFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDF 201
Cdd:cd05038  87 meyLPSGSLR------DYLQRHRDQIDLKRLLL-------FASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 202 GMARGLctsPAEHQYfmteYVAT-------RWYrAPElMLSLHEYTQAIDLWSVGCIFGEMLARrqlfpGKNYVHQLQLI 274
Cdd:cd05038 154 GLAKVL---PEDKEY----YYVKepgespiFWY-APE-CLRESRFSSASDVWSFGVTLYELFTY-----GDPSQSPPALF 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 275 MMVLGTPSPAVIQAVGAERVRAYiQSLPPRQPVPWEtVYpgadrqalSLLGRMLRFEPSARIS 337
Cdd:cd05038 220 LRMIGIAQGQMIVTRLLELLKSG-ERLPRPPSCPDE-VY--------DLMKECWEYEPQDRPS 272
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
61-256 4.19e-22

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


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 96.53  E-value: 4.19e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAfdvvTNAKRTLRElKILKHFKHDNIIAIKDILRPTVPYGEFKSVYVVLDLM 140
Cdd:cd14189   9 LGKGGFARCYEMTDLATNKTYAVKVIPHS----RVAKPHQRE-KIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 -ESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLctSPAEHQyfMT 219
Cdd:cd14189  84 sRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARL--EPPEQR--KK 159
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20986497 220 EYVATRWYRAPELMLSLHEYTQAiDLWSVGCIFGEML 256
Cdd:cd14189 160 TICGTPNYLAPEVLLRQGHGPES-DVWSLGCVMYTLL 195
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
54-249 4.68e-22

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: 96.64  E-value: 4.68e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIP----NAFDVVTnakrtlRELKILKHFKHDNIIAIkdilrptvpYGE 129
Cdd:cd06646  10 DYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKlepgDDFSLIQ------QEIFMVKECKHCNIVAY---------FGS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDLME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd06646  75 YLSREKLWICMEycggGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAA 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 20986497 206 GLCTSPAEHQYFmteyVATRWYRAPELMLSLHE--YTQAIDLWSVG 249
Cdd:cd06646 155 KITATIAKRKSF----IGTPYWMAPEVAAVEKNggYNQLCDIWAVG 196
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
58-310 4.76e-22

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: 97.80  E-value: 4.76e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  58 IETIGNGAYGVVSSARRRLTGQQVAIKKIP-NAFDVVTNAKRTLRELKILKHFKHDNIIAIKDIlrptvpYGEFKSVYVV 136
Cdd:cd06633  26 LHEIGHGSFGAVYFATNSHTNEVVAIKKMSySGKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGC------YLKDHTAWLV 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 137 LDLM---ESDLHQIihSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglCTSPAe 213
Cdd:cd06633 100 MEYClgsASDLLEV--HKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSAS--IASPA- 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 214 hqyfmTEYVATRWYRAPELMLSLHE--YTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMvlgTPSPAVIQAVGA 291
Cdd:cd06633 175 -----NSFVGTPYWMAPEVILAMDEgqYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQ---NDSPTLQSNEWT 246
                       250       260
                ....*....|....*....|...
gi 20986497 292 ERVRAYI----QSLPPRQPVPWE 310
Cdd:cd06633 247 DSFRGFVdyclQKIPQERPSSAE 269
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
52-256 4.90e-22

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: 96.79  E-value: 4.90e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  52 GDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKipnafdVVTNAKRTLRELKILKHFKHDNIIAIKDILRPT--VPYGE 129
Cdd:cd14047   5 RQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKR------VKLNNEKAEREVKALAKLDHPNIVRYNGCWDGFdyDPETS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKS--------VYVVLDLMES-DLHQIIHSSQPLTLEHV---RYFlYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELK 197
Cdd:cd14047  79 SSNssrsktkcLFIQMEFCEKgTLESWIEKRNGEKLDKVlalEIF-EQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVK 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 198 IGDFGMARGLcTSPAEhqyfMTEYVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd14047 158 IGDFGLVTSL-KNDGK----RTKSKGTLSYMSPE-QISSQDYGKEVDIYALGLILFELL 210
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
55-348 5.16e-22

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 98.41  E-value: 5.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdvVTNAKRTLRELKILKHFKHDNIIAIKDilrpTVPYGEFKSVy 134
Cdd:PHA03209  68 YTVIKTLTPGSEGRVFVATKPGQPDPVVLK--------IGQKGTTLIEAMLLQNVNHPSVIRMKD----TLVSGAITCM- 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  135 vVLDLMESDLHQII-HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAE 213
Cdd:PHA03209 135 -VLPHYSSDLYTYLtKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPAF 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  214 hqYFMTEYVATrwyRAPELmLSLHEYTQAIDLWSVGCIFGEMLAR-RQLF---------PGKNYVHQLQLIMMVLGTPSP 283
Cdd:PHA03209 214 --LGLAGTVET---NAPEV-LARDKYNSKADIWSAGIVLFEMLAYpSTIFedppstpeeYVKSCHSHLLKIISTLKVHPE 287
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497  284 AVIQAVGAERVRAYIQ-SLPPRQPvpwETVYPGADRQALSLLG-----RMLRFEPSARISAAAALRHPFLA 348
Cdd:PHA03209 288 EFPRDPGSRLVRGFIEyASLERQP---YTRYPCFQRVNLPIDGeflvhKMLTFDAAMRPSAEEILNYPMFA 355
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
55-251 5.29e-22

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: 96.88  E-value: 5.29e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPnafdvvtnaKRTLR--------ELKILKHFKHDNIIAIKDILR-PTv 125
Cdd:cd14169   5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIP---------KKALRgkeamvenEIAVLRRINHENIVSLEDIYEsPT- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 pygefkSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVN---ENCELKIGDF 201
Cdd:cd14169  75 ------HLYLAMELVTGgELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDF 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 20986497 202 GMarglctSPAEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCI 251
Cdd:cd14169 149 GL------SKIEAQGMLSTACGTPGYVAPEL-LEQKPYGKAVDVWAIGVI 191
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
55-300 6.21e-22

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: 97.10  E-value: 6.21e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnAFDVVTNAKRTLR-ELKILKHFKHD-NIIAIKDILRPTVPYGEFKS 132
Cdd:cd06637   8 FELVELVGNGTYGQVYKGRHVKTGQLAAIK----VMDVTGDEEEEIKqEINMLKKYSHHrNIATYYGAFIKKNPPGMDDQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMES-DLHQIIHSSQPLTL--EHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCT 209
Cdd:cd06637  84 LWLVMEFCGAgSVTDLIKNTKGNTLkeEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 210 SPAEHQYFmteyVATRWYRAPELMLSLHE----YTQAIDLWSVGCIFGEMlarRQLFPGKNYVHQLQLIMMVLGTPSPAV 285
Cdd:cd06637 164 TVGRRNTF----IGTPYWMAPEVIACDENpdatYDFKSDLWSLGITAIEM---AEGAPPLCDMHPMRALFLIPRNPAPRL 236
                       250
                ....*....|....*
gi 20986497 286 IQAVGAERVRAYIQS 300
Cdd:cd06637 237 KSKKWSKKFQSFIES 251
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
53-347 6.27e-22

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: 96.18  E-value: 6.27e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLR-ELKILKHFKHDNIIAIkdilrptvpYGEFK 131
Cdd:cd14116   5 EDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRrEVEIQSHLRHPNILRL---------YGYFH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 S---VYVVLDLmeSDLHQIIHSSQPLT-LEHVRYFLY--QLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAr 205
Cdd:cd14116  76 DatrVYLILEY--APLGTVYRELQKLSkFDEQRTATYitELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWS- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 206 glCTSPAEHQyfmTEYVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVlgtpspav 285
Cdd:cd14116 153 --VHAPSSRR---TTLCGTLDYLPPE-MIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRV-------- 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 286 iqavgaervrayiqslpprqpvpwETVYPG-ADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14116 219 ------------------------EFTFPDfVTEGARDLISRLLKHNPSQRPMLREVLEHPWI 257
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
61-260 7.46e-22

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: 96.19  E-value: 7.46e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRlTGQQVAIKKI-PNAFDVVTnaKRTLRELKILKHFKHDNIIAikdiLRPTVPYGEFKSVyvVLDL 139
Cdd:cd14066   1 IGSGGFGTVYKGVLE-NGTVVAVKRLnEMNCAASK--KEFLTELEMLGRLRHPNLVR----LLGYCLESDEKLL--VYEY 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 140 MES-DLHQIIH---SSQPLTLEhVRY-FLYQLLRGLKYMHSA---QVIHRDLKPSNLLVNENCELKIGDFGMARglCTSP 211
Cdd:cd14066  72 MPNgSLEDRLHchkGSPPLPWP-QRLkIAKGIARGLEYLHEEcppPIIHGDIKSSNILLDEDFEPKLTDFGLAR--LIPP 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 20986497 212 AEHQYFMTEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQ 260
Cdd:cd14066 149 SESVSKTSAVKGTIGYLAPEYIRTG-RVSTKSDVYSFGVVLLELLTGKP 196
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
50-347 1.34e-21

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: 95.50  E-value: 1.34e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  50 DVGDEYEIIET-IGNGAYGVVSSARRRLTGQQVA---IKKIPNAFDVvtnAKRTLRELKILKHFK-HDNIIAIKDIlrpt 124
Cdd:cd14106   4 NINEVYTVESTpLGRGKFAVVRKCIHKETGKEYAakfLRKRRRGQDC---RNEILHEIAVLELCKdCPRVVNLHEV---- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 125 vpYGEFKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNE---NCELKIGD 200
Cdd:cd14106  77 --YETRSELILILELAAGgELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSefpLGDIKLCD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 201 FGMARGLCtsPAEHQYfmtEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNY------VHQLQLi 274
Cdd:cd14106 155 FGISRVIG--EGEEIR---EILGTPDYVAPEI-LSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKqetflnISQCNL- 227
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 275 mmvlgtpspaviqavgaervrayiqSLPprqpvpwETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14106 228 -------------------------DFP-------EELFKDVSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
55-347 1.40e-21

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: 95.17  E-value: 1.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNA-FDVVTNAkRTLRELKILKHFKHDNIIAIKDILRPTVpygefkSV 133
Cdd:cd14074   5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTkLDDVSKA-HLFQEVRCMKLVQHPNVVRLYEVIDTQT------KL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMES-DLHQ-IIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCEL-KIGDFGMARGLCts 210
Cdd:cd14074  78 YLILELGDGgDMYDyIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQGLvKLTDFGFSNKFQ-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 211 PAEHqyfMTEYVATRWYRAPELMLSlHEY-TQAIDLWSVGCIfgemlarrqlfpgknyvhqlqLIMMVLGTPSpavIQAV 289
Cdd:cd14074 156 PGEK---LETSCGSLAYSAPEILLG-DEYdAPAVDIWSLGVI---------------------LYMLVCGQPP---FQEA 207
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 290 GAERVRAYIqsLPPRQPVPwetvyPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14074 208 NDSETLTMI--MDCKYTVP-----AHVSPECKDLIRRMLIRDPKKRASLEEIENHPWL 258
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
55-283 1.55e-21

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: 95.23  E-value: 1.55e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKI---PNAFDVvtnaKRTLRELKILKHFKHDniiAIKDILRPTVPYGEFK 131
Cdd:cd06917   3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLnldTDDDDV----SDIQKEVALLSQLKLG---QPKNIIKYYGSYLKGP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSP 211
Cdd:cd06917  76 SLWIIMDYCEGGSIRTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNS 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497 212 AEHQYFmteyVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRqlfPGKNYVHQLQLIMMVLGTPSP 283
Cdd:cd06917 156 SKRSTF----VGTPYWMAPEVITEGKYYDTKADIWSLGITTYEMATGN---PPYSDVDALRAVMLIPKSKPP 220
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
55-347 1.57e-21

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: 94.88  E-value: 1.57e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPN--AFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYgefks 132
Cdd:cd14070   4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKkkAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSY----- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 vYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMArGLCTSP 211
Cdd:cd14070  79 -YLVMELCPGgNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLS-NCAGIL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 212 AEHQYFMTEyVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFpgknyvhqlqlimmvlgTPSPAVIQAVGA 291
Cdd:cd14070 157 GYSDPFSTQ-CGSPAYAAPEL-LARKKYGPKVDVWSIGVNMYAMLTGTLPF-----------------TVEPFSLRALHQ 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 292 ERVRAYIQSLPPrqpvpweTVYPGadrqALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14070 218 KMVDKEMNPLPT-------DLSPG----AISFLRSLLEPDPLKRPNIKQALANRWL 262
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
55-277 1.80e-21

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: 94.67  E-value: 1.80e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRtlrelKILKH--FKHDNIIAIKD-ILRPTvpygefk 131
Cdd:cd14665   2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQR-----EIINHrsLRHPNIVRFKEvILTPT------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENC--ELKIGDFGMARG-- 206
Cdd:cd14665  70 HLAIVMEYAAGgELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGYSKSsv 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 207 LCTSPaehqyfmTEYVATRWYRAPELMLSlHEYTQAI-DLWSVGCIFGEMLARRQLFPG----KNYVHQLQLIMMV 277
Cdd:cd14665 150 LHSQP-------KSTVGTPAYIAPEVLLK-KEYDGKIaDVWSCGVTLYVMLVGAYPFEDpeepRNFRKTIQRILSV 217
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
59-266 1.84e-21

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: 94.69  E-value: 1.84e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfdvvTNAKRTLRElKILKHFKHDNIIAIKDILRPTVPYGEFKSVYVVLD 138
Cdd:cd14188   7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHS----RVSKPHQRE-KIDKEIELHRILHHKHVVQFYHYFEDKENIYILLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 139 LM-ESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLctSPAEHQyf 217
Cdd:cd14188  82 YCsRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARL--EPLEHR-- 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 20986497 218 MTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKN 266
Cdd:cd14188 158 RRTICGTPNYLSPEV-LNKQGHGCESDIWALGCVMYTMLLGRPPFETTN 205
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
61-257 1.86e-21

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: 95.88  E-value: 1.86e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDvvTNAKRTLRELKILKhfKHDNIIAIKDIlrptvpYGEFKSVYVVLDLM 140
Cdd:cd14179  15 LGEGSFSICRKCLHKKTNQEYAVKIVSKRME--ANTQREIAALKLCE--GHPNIVKLHEV------YHDQLHTFLVMELL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 ES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV---NENCELKIGDFGMARglcTSPAEHQY 216
Cdd:cd14179  85 KGgELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFAR---LKPPDNQP 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 20986497 217 FMTEyVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLA 257
Cdd:cd14179 162 LKTP-CFTLHYAAPEL-LNYNGYDESCDLWSLGVILYTMLS 200
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
61-303 2.01e-21

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: 94.10  E-value: 2.01e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVssARRRLTGQQVAIKKipnafdvVTNAKRTlrELKILKHFKHDNIIAIKDILRpTVPygefksVYVVLdlM 140
Cdd:cd14059   1 LGSGAQGAV--FLGKFRGEEVAVKK-------VRDEKET--DIKHLRKLNHPNIIKFKGVCT-QAP------CYCIL--M 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 E----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLctspAEHQY 216
Cdd:cd14059  61 EycpyGQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKEL----SEKST 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 217 FMTeYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRqlFPGKNyvhqlqlimmvlgTPSPAVIQAVGAERVRA 296
Cdd:cd14059 137 KMS-FAGTVAWMAPEVIRN-EPCSEKVDIWSFGVVLWELLTGE--IPYKD-------------VDSSAIIWGVGSNSLQL 199

                ....*..
gi 20986497 297 YIQSLPP 303
Cdd:cd14059 200 PVPSTCP 206
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
53-249 2.45e-21

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: 95.03  E-value: 2.45e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSA---------------RRRLTGQQVAIKKIP-----NAFDVVTNAK----RTLRELKILKH 108
Cdd:cd14199   2 NQYKLKDEIGKGSYGVVKLAyneddntyyamkvlsKKKLMRQAGFPRRPPprgarAAPEGCTQPRgpieRVYQEIAILKK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 109 FKHDNIIAIKDILR-PTVPYgefksVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSN 187
Cdd:cd14199  82 LDHPNVVKLVEVLDdPSEDH-----LYMVFELVKQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSN 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 188 LLVNENCELKIGDFGMARGLCTSPAehqyFMTEYVATRWYRAPELMLSLHEY--TQAIDLWSVG 249
Cdd:cd14199 157 LLVGEDGHIKIADFGVSNEFEGSDA----LLTNTVGTPAFMAPETLSETRKIfsGKALDVWAMG 216
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
55-283 3.29e-21

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 94.69  E-value: 3.29e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnAFDVVTNAKRTLR-ELKILKHFKHD-NIIAIKDILRPTVPYGEFKS 132
Cdd:cd06636  18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIK----VMDVTEDEEEEIKlEINMLKKYSHHrNIATYYGAFIKKSPPGHDDQ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMES-DLHQIIHSSQPLTLEH--VRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCT 209
Cdd:cd06636  94 LWLVMEFCGAgSVTDLVKNTKGNALKEdwIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 210 SPAEHQYFmteyVATRWYRAPELML------SLHEYTQaiDLWSVGCIFGEMlarRQLFPGKNYVHQLQLIMMVLGTPSP 283
Cdd:cd06636 174 TVGRRNTF----IGTPYWMAPEVIAcdenpdATYDYRS--DIWSLGITAIEM---AEGAPPLCDMHPMRALFLIPRNPPP 244
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
50-251 3.46e-21

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: 94.09  E-value: 3.46e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  50 DVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfdVVTNAKRTL------RELKILKHFKHDNIIAIKDIlrp 123
Cdd:cd14105   2 NVEDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKR--RSKASRRGVsredieREVSILRQVLHPNIITLHDV--- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 124 tvpYGEFKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE----LKI 198
Cdd:cd14105  77 ---FENKTDVVLILELVAGgELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVpiprIKL 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497 199 GDFGMA---------RGLCTSPaehqyfmtEYVatrwyrAPELmLSLHEYTQAIDLWSVGCI 251
Cdd:cd14105 154 IDFGLAhkiedgnefKNIFGTP--------EFV------APEI-VNYEPLGLEADMWSIGVI 200
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
55-266 3.49e-21

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: 93.74  E-value: 3.49e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTvpygefKSVY 134
Cdd:cd14072   2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETE------KTLY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR-------- 205
Cdd:cd14072  76 LVMEYASGgEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNeftpgnkl 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497 206 -GLCTSPAehqyfmteyvatrwYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKN 266
Cdd:cd14072 156 dTFCGSPP--------------YAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQN 203
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
55-256 3.82e-21

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: 93.90  E-value: 3.82e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTL-RELKILKHFKHDNIIAIKDILRPTVpygefKSV 133
Cdd:cd14163   2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQRFLpRELQIVERLDHKNIIHVYEMLESAD-----GKI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVnENCELKIGDFGMARGLctsPA 212
Cdd:cd14163  77 YLVMELAEDgDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQL---PK 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 20986497 213 EHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd14163 153 GGRELSQTFCGSTAYAAPEVLQGVPHDSRKGDIWSMGVVLYVML 196
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
59-346 3.94e-21

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: 93.88  E-value: 3.94e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSsARRRLTGQQVAIKKI-PNAFDVVTnakrtlRELKILKHF-KHDNIIAI----KDilrptvpyGEFks 132
Cdd:cd13982   7 KVLGYGSEGTIV-FRGTFDGRPVAVKRLlPEFFDFAD------REVQLLRESdEHPNVIRYfcteKD--------RQF-- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMESDLHQII-----------HSSQPLTLehvryfLYQLLRGLKYMHSAQVIHRDLKPSNLLV-----NENCEL 196
Cdd:cd13982  70 LYIALELCAASLQDLVespresklflrPGLEPVRL------LRQIASGLAHLHSLNIVHRDLKPQNILIstpnaHGNVRA 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 197 KIGDFGMARGLctSPAEHQYFMTEYVA-TRWYRAPELMLS--LHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQL 273
Cdd:cd13982 144 MISDFGLCKKL--DVGRSSFSRRSGVAgTSGWIAPEMLSGstKRRQTRAVDIFSLGCVFYYVLSGGSHPFGDKLEREANI 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 274 ImmvLGTPSPAVIQAVGAERVRAYiqslpprqpvpwetvypgadrqalSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd13982 222 L---KGKYSLDKLLSLGEHGPEAQ------------------------DLIERMIDFDPEKRPSAEEVLNHPF 267
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
53-284 3.98e-21

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: 94.41  E-value: 3.98e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVvTNAKRTLRELkilkhfkhdniiaikDILRPTVP------ 126
Cdd:cd06617   1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATVNS-QEQKRLLMDL---------------DISMRSVDcpytvt 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 -YGE-FKS--VYVVLDLMESDLHQI---IHSSQPLTLEHV-RYFLYQLLRGLKYMHSA-QVIHRDLKPSNLLVNENCELK 197
Cdd:cd06617  65 fYGAlFREgdVWICMEVMDTSLDKFykkVYDKGLTIPEDIlGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVK 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 198 IGDFGMARGLCTSPAEhqyfmTEYVATRWYRAPELM---LSLHEYTQAIDLWSVGCIFGEMLARRqlFPGKNYVHQLQLI 274
Cdd:cd06617 145 LCDFGISGYLVDSVAK-----TIDAGCKPYMAPERInpeLNQKGYDVKSDVWSLGITMIELATGR--FPYDSWKTPFQQL 217
                       250
                ....*....|
gi 20986497 275 MMVLGTPSPA 284
Cdd:cd06617 218 KQVVEEPSPQ 227
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
53-349 4.54e-21

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: 93.96  E-value: 4.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIP----NAFDVVTnakrtlRELKILKHFKHDNIIAIkdilrptvpYG 128
Cdd:cd06645  11 EDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKlepgEDFAVVQ------QEIIMMKDCKHSNIVAY---------FG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA 204
Cdd:cd06645  76 SYLRRDKLWICMEfcggGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RGLCTSPAEHQYFmteyVATRWYRAPELMLSLHE--YTQAIDLWSVGCIFGEMlarRQLFPGKNYVHQLQLIMMVlgtps 282
Cdd:cd06645 156 AQITATIAKRKSF----IGTPYWMAPEVAAVERKggYNQLCDIWAVGITAIEL---AELQPPMFDLHPMRALFLM----- 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 283 paviqavgaerVRAYIQSLPPRQPVPWETVYPGADRQALSLlgrmlrfEPSARISAAAALRHPFLAK 349
Cdd:cd06645 224 -----------TKSNFQPPKLKDKMKWSNSFHHFVKMALTK-------NPKKRPTAEKLLQHPFVTQ 272
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
61-345 5.08e-21

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: 93.96  E-value: 5.08e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSA---------------RRRLTGQQVAIKKIPNAFDVVTNAK------RTLRELKILKHFKHDNIIAIKD 119
Cdd:cd14118   2 IGKGSYGIVKLAyneedntlyamkilsKKKLLKQAGFFRRPPPRRKPGALGKpldpldRVYREIAILKKLDHPNVVKLVE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 120 ILRPTVPygefKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIG 199
Cdd:cd14118  82 VLDDPNE----DNLYMVFELVDKGAVMEVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 200 DFGMARGLCTSPAehqyFMTEYVATRWYRAPELML-SLHEYT-QAIDLWSVGC-----IFGEMlarrqlfPGK-NYVHQL 271
Cdd:cd14118 158 DFGVSNEFEGDDA----LLSSTAGTPAFMAPEALSeSRKKFSgKALDIWAMGVtlycfVFGRC-------PFEdDHILGL 226
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 272 QlimmvlgtpspaviqavgaERVRAYIQSLPPRqpvpwetvyPGADRQALSLLGRMLRFEPSARISAAAALRHP 345
Cdd:cd14118 227 H-------------------EKIKTDPVVFPDD---------PVVSEQLKDLILRMLDKNPSERITLPEIKEHP 272
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
54-347 5.72e-21

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: 93.26  E-value: 5.72e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpNAFDVVTNAKR-TLRELKILKHFKHDNIIAIkdilrptvpYGEFKS 132
Cdd:cd08221   1 HYIPVRVLGRGAFGEAVLYRKTEDNSLVVWKEV-NLSRLSEKERRdALNEIDILSLLNHDNIITY---------YNHFLD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLME----SDLHQII--HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARG 206
Cdd:cd08221  71 GESLFIEMEycngGNLHDKIaqQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 207 LctspaEHQYFMTE-YVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhQLQLIMmvlgtpspAV 285
Cdd:cd08221 151 L-----DSESSMAEsIVGTPYYMSPELVQG-VKYNFKSDIWAVGCVLYELLTLKRTFDATN---PLRLAV--------KI 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497 286 IQAVGAERVRAYIQSLpprqpvpwetvypgadrqaLSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd08221 214 VQGEYEDIDEQYSEEI-------------------IQLVHDCLHQDPEDRPTAEELLERPLL 256
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
18-349 6.01e-21

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 95.28  E-value: 6.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   18 PGPVKAEPAHTAASVAAKNLALLKARSFDvtfdvgdEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKI-PNAFDVVTNa 96
Cdd:PLN00034  46 PLPPPSSSSSSSSSSSASGSAPSAAKSLS-------ELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIyGNHEDTVRR- 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   97 kRTLRELKILKHFKHDNIIAIKDIlrptvpYGEFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYflyQLLRGLKYMHSA 176
Cdd:PLN00034 118 -QICREIEILRDVNHPNVVKCHDM------FDHNGEIQVLLEFMDGGSLEGTHIADEQFLADVAR---QILSGIAYLHRR 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  177 QVIHRDLKPSNLLVNENCELKIGDFGMARGL------CTSPaehqyfmteyVATRWYRAPELM---LSLHEYT-QAIDLW 246
Cdd:PLN00034 188 HIVHRDIKPSNLLINSAKNVKIADFGVSRILaqtmdpCNSS----------VGTIAYMSPERIntdLNHGAYDgYAGDIW 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  247 SVGcifgemlarrqlfpgknyvhqLQLIMMVLGT-PSPAVIQAVGAERVRAYIQSLPPRQPvpwetvyPGADRQALSLLG 325
Cdd:PLN00034 258 SLG---------------------VSILEFYLGRfPFGVGRQGDWASLMCAICMSQPPEAP-------ATASREFRHFIS 309
                        330       340
                 ....*....|....*....|....
gi 20986497  326 RMLRFEPSARISAAAALRHPFLAK 349
Cdd:PLN00034 310 CCLQREPAKRWSAMQLLQHPFILR 333
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
59-347 6.92e-21

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: 93.06  E-value: 6.92e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQVA-----IKKIPNAfdvvtNAKRTLRELKILKHFKHDNIIAIKDILRPtvpyGEFKSV 133
Cdd:cd13983   7 EVLGRGSFKTVYRAFDTEEGIEVAwneikLRKLPKA-----ERQRFKQEIEILKSLKHPNIIKFYDSWES----KSKKEV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQ--VIHRDLKPSNLLVNENC-ELKIGDFGMARGLCT 209
Cdd:cd13983  78 IFITELMTSgTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINGNTgEVKIGDLGLATLLRQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 210 SpaehqyFMTEYVATRWYRAPELMLSlhEYTQAIDLWSVGCIFGEMLARRqlFPGKNYVHQLQLIMMVLGTPSPAVIQAV 289
Cdd:cd13983 158 S------FAKSVIGTPEFMAPEMYEE--HYDEKVDIYAFGMCLLEMATGE--YPYSECTNAAQIYKKVTSGIKPESLSKV 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 290 GAERVRAYIQS-LPPrqpvpwetvypgadrqalsllgrmlrfePSARISAAAALRHPFL 347
Cdd:cd13983 228 KDPELKDFIEKcLKP----------------------------PDERPSARELLEHPFF 258
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
55-347 8.05e-21

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: 92.62  E-value: 8.05e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIK---KIPNAFDVVTnaKRTLRELKILKHFKHDNIIAIKDILRPTVpygefK 131
Cdd:cd14164   2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKivdRRRASPDFVQ--KFLPRELSILRRVNHPNIVQMFECIEVAN-----G 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE-LKIGDFGMARGLcTS 210
Cdd:cd14164  75 RLYIVMEAAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDRkIKIADFGFARFV-ED 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 211 PAEhqyFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyVHQLQLIMMVLGTPSPAVIQavg 290
Cdd:cd14164 154 YPE---LSTTFCGSRAYTPPEVILGTPYDPKKYDVWSLGVVLYVMVTGTMPFDETN-VRRLRLQQRGVLYPSGVALE--- 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 291 aERVRAYIQSLpprqpvpwetvypgadrqalsllgrmLRFEPSARISAAAALRHPFL 347
Cdd:cd14164 227 -EPCRALIRTL--------------------------LQFNPSTRPSIQQVAGNSWL 256
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
51-347 9.19e-21

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: 93.14  E-value: 9.19e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  51 VGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpNAFDVVTNAKRTLRELKILKHFKHDNIIA-IKDILRPTvpyge 129
Cdd:cd14183   4 ISERYKVGRTIGDGNFAVVKECVERSTGREYALKII-NKSKCRGKEHMIQNEVSILRRVKHPNIVLlIEEMDMPT----- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 fkSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE----LKIGDFGMA 204
Cdd:cd14183  78 --ELYLVMELVKGgDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDgsksLKLGDFGLA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RgLCTSPaehqyfMTEYVATRWYRAPELMLSLHeYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQL---QLIMMVLGTP 281
Cdd:cd14183 156 T-VVDGP------LYTVCGTPTYVAPEIIAETG-YGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVlfdQILMGQVDFP 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 282 SPAviqavgaervrayiqslpprqpvpWETVYPGADRqalsLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14183 228 SPY------------------------WDNVSDSAKE----LITMMLQVDVDQRYSALQVLEHPWV 265
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
51-347 1.16e-20

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: 92.30  E-value: 1.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  51 VGD---EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnafDVVTNAKRTL--RELKILKHFKHDNIIAIKDilrptv 125
Cdd:cd06647   2 VGDpkkKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQM----NLQQQPKKELiiNEILVMRENKNPNIVNYLD------ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 PYGEFKSVYVVLD-LMESDLHQIIHSSQpLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFgma 204
Cdd:cd06647  72 SYLVGDELWVVMEyLAGGSLTDVVTETC-MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDF--- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 rGLCTSPAEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLImMVLGTPSpa 284
Cdd:cd06647 148 -GFCAQITPEQSKRSTMVGTPYWMAPEV-VTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATNGTPE-- 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 285 viqavgaervrayiqslpprqpvpwetvYPGADRQAL---SLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd06647 223 ----------------------------LQNPEKLSAifrDFLNRCLEMDVEKRGSAKELLQHPFL 260
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
54-345 1.42e-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: 92.06  E-value: 1.42e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFK-HDNIIAIKDilrptvPYGEFKS 132
Cdd:cd13997   1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKERARALREVEAHAALGqHPNIVRYYS------SWEEGGH 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMES-DLHQIIHSSQPLTL---EHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLC 208
Cdd:cd13997  75 LYIQMELCENgSLQDALEELSPISKlseAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPaehqyfMTEYVATRwYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLqlimmvlgtpspaviqa 288
Cdd:cd13997 155 TSG------DVEEGDSR-YLAPELLNENYTHLPKADIFSLGVTVYEAATGEPLPRNGQQWQQL----------------- 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 289 vgaervRAYIQSLPPRqpvpwetvyPGADRQALSLLGRMLRFEPSARISAAAALRHP 345
Cdd:cd13997 211 ------RQGKLPLPPG---------LVLSQELTRLLKVMLDPDPTRRPTADQLLAHD 252
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
61-374 1.47e-20

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: 93.53  E-value: 1.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTN-AKRTLRELKILKHFKHDNIIAIKdilrptvpYGeFKSVYVVLDL 139
Cdd:cd05595   3 LGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDeVAHTVTESRVLQNTRHPFLTALK--------YA-FQTHDRLCFV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 140 ME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFgmarGLCTSPAEHQ 215
Cdd:cd05595  74 MEyangGELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDF----GLCKEGITDG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 216 YFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMvlgtpspaviqavgaERVR 295
Cdd:cd05595 150 ATMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILM---------------EEIR 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 296 aYIQSLPPrqpvpwetvypgadrQALSLLGRMLRFEPSARI-----SAAAALRHPFLAKYHDPD-DEPDCAPPFDFAFDR 369
Cdd:cd05595 214 -FPRTLSP---------------EAKSLLAGLLKKDPKQRLgggpsDAKEVMEHRFFLSINWQDvVQKKLLPPFKPQVTS 277

                ....*
gi 20986497 370 EALTR 374
Cdd:cd05595 278 EVDTR 282
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
61-253 1.99e-20

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: 92.51  E-value: 1.99e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVT-NAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFKsvyVVLDL 139
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPSDkNRERWCLEVQIMKKLNHPNVVSARDVPPELEKLSPND---LPLLA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 140 ME----SDLHQIIH---SSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNL-LVNENCEL--KIGDFGMARGLct 209
Cdd:cd13989  78 MEycsgGDLRKVLNqpeNCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIvLQQGGGRViyKLIDLGYAKEL-- 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 20986497 210 spaEHQYFMTEYVATRWYRAPELMLSlHEYTQAIDLWSVG-----CIFG 253
Cdd:cd13989 156 ---DQGSLCTSFVGTLQYLAPELFES-KKYTCTVDYWSFGtlafeCITG 200
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
53-266 2.05e-20

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: 91.50  E-value: 2.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPnafdVVTNAKRT-LRELKILKHFKHDNIIAIKDilrptvPYGEFK 131
Cdd:cd14108   2 DYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIP----VRAKKKTSaRRELALLAELDHKSIVRFHD------AFEKRR 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQIIhSSQPLTLE-HVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE--LKIGDFGMARGLc 208
Cdd:cd14108  72 VVIIVTELCHEELLERI-TKRPTVCEsEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTdqVRICDFGNAQEL- 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 209 tSPAEHQYfmTEYvATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKN 266
Cdd:cd14108 150 -TPNEPQY--CKY-GTPEFVAPEI-VNQSPVSKVTDIWPVGVIAYLCLTGISPFVGEN 202
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
54-258 2.34e-20

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 93.00  E-value: 2.34e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnAFDVVTNAKRTLRELKILKHFK--HDNIIAI------KDILRPTV 125
Cdd:cd13977   1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKKI--RCNAPENVELALREFWALSSIQrqHPNVIQLeecvlqRDGLAQRM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 PYGEFKSV------------------------YVVLDLMES-DLHQIIHSSQPlTLEHVRYFLYQLLRGLKYMHSAQVIH 180
Cdd:cd13977  79 SHGSSKSDlylllvetslkgercfdprsacylWFVMEFCDGgDMNEYLLSRRP-DRQTNTSFMLQLSSALAFLHRNQIVH 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 181 RDLKPSNLLVNENCE---LKIGDFGMA---RGLCTSPAE----HQYFMTEYVATRWYRAPELMLSlhEYTQAIDLWSVGC 250
Cdd:cd13977 158 RDLKPDNILISHKRGepiLKVADFGLSkvcSGSGLNPEEpanvNKHFLSSACGSDFYMAPEVWEG--HYTAKADIFALGI 235

                ....*...
gi 20986497 251 IFGEMLAR 258
Cdd:cd13977 236 IIWAMVER 243
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
53-256 2.59e-20

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: 91.54  E-value: 2.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKI--PNAFDVVTNakrTLRELKILKHFKHDNIiaikdilrpTVPYGEF 130
Cdd:cd06609   1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIdlEEAEDEIED---IQQEIQFLSQCDSPYI---------TKYYGSF 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVLDLME-------SDLHQiihsSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGM 203
Cdd:cd06609  69 LKGSKLWIIMEycgggsvLDLLK----PGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGV 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 20986497 204 ARGLCTSPAEHQYFmteyVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd06609 145 SGQLTSTMSKRNTF----VGTPFWMAPEV-IKQSGYDEKADIWSLGITAIELA 192
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
55-277 2.60e-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: 91.37  E-value: 2.60e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRtlrelKILKH--FKHDNIIAIKD-ILRPTvpygefk 131
Cdd:cd14662   2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQR-----EIINHrsLRHPNIIRFKEvVLTPT------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENC--ELKIGDFGMARG-- 206
Cdd:cd14662  70 HLAIVMEYAAGgELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGYSKSsv 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 207 LCTSPaehqyfmTEYVATRWYRAPELmLSLHEYTQAI-DLWSVGCIFGEMLARRQLFPG----KNYVHQLQLIMMV 277
Cdd:cd14662 150 LHSQP-------KSTVGTPAYIAPEV-LSRKEYDGKVaDVWSCGVTLYVMLVGAYPFEDpddpKNFRKTIQRIMSV 217
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
61-346 2.85e-20

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: 91.24  E-value: 2.85e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLR---ELKILKHFKHDNIIAIKDILRPTvpygEFKSVYVVL 137
Cdd:cd06653  10 LGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQETSKEVNAlecEIQLLKNLRHDRIVQYYGCLRDP----EEKKLSIFV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 138 DLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR---GLCTSPAE 213
Cdd:cd06653  86 EYMPGgSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKriqTICMSGTG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 214 hqyfMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRqlfpgknyvhqlqlimmvlgtPSPAVIQAVGAeR 293
Cdd:cd06653 166 ----IKSVTGTPYWMSPEV-ISGEGYGRKADVWSVACTVVEMLTEK---------------------PPWAEYEAMAA-I 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 20986497 294 VRAYIQSLPPRQPvpwetvyPGADRQALSLLgRMLRFEPSARISAAAALRHPF 346
Cdd:cd06653 219 FKIATQPTKPQLP-------DGVSDACRDFL-RQIFVEEKRRPTAEFLLRHPF 263
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
61-264 3.07e-20

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: 91.13  E-value: 3.07e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNA-KRTLRELKILKHFKHDNIIAIkdilrptvpYGEFKSVYVVLDL 139
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQqEHIFSEKEILEECNSPFIVKL---------YRTFKDKKYLYML 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 140 MES----DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL-------- 207
Cdd:cd05572  72 MEYclggELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLgsgrktwt 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 208 -CTSPaehqyfmtEYVatrwyrAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPG 264
Cdd:cd05572 152 fCGTP--------EYV------APEIILN-KGYDFSVDYWSLGILLYELLTGRPPFGG 194
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
61-259 3.40e-20

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: 91.26  E-value: 3.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKI---PNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPygefKSVYVVL 137
Cdd:cd06652  10 LGQGAFGRVYLCYDADTGRELAVKQVqfdPESPETSKEVNALECEIQLLKNLLHERIVQYYGCLRDPQE----RTLSIFM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 138 DLM-ESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL---CTSPAE 213
Cdd:cd06652  86 EYMpGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRLqtiCLSGTG 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 20986497 214 hqyfMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARR 259
Cdd:cd06652 166 ----MKSVTGTPYWMSPEV-ISGEGYGRKADIWSVGCTVVEMLTEK 206
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
9-349 3.86e-20

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 93.37  E-value: 3.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497    9 DGEDGSAEPPGPVKAEPAHTAASVaaknlallkarsfDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQ--VAIKki 86
Cdd:PHA03207  61 DADEESLSPQTDVCQEPCETTSSS-------------DPASVVRMQYNILSSLTPGSEGEVFVCTKHGDEQRkkVIVK-- 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   87 pnafdVVTNAKRTLRELKILKHFKHDNIIAIKDILRptvpygeFKS-VYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQ 165
Cdd:PHA03207 126 -----AVTGGKTPGREIDILKTISHRAIINLIHAYR-------WKStVCMVMPKYKCDLFTYVDRSGPLPLEQAITIQRR 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  166 LLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQYFmtEYVATRWYRAPELmLSLHEYTQAIDL 245
Cdd:PHA03207 194 LLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDAHPDTPQCY--GWSGTLETNSPEL-LALDPYCAKTDI 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  246 WSVGCIFGEMLARRQLFPGK---NYVHQLQLIMMVLGTPSPAVIQAVGAERVRAYIQ-SLPPRQP--VPWETVYPGADRQ 319
Cdd:PHA03207 271 WSAGLVLFEMSVKNVTLFGKqvkSSSSQLRSIIRCMQVHPLEFPQNGSTNLCKHFKQyAIVLRPPytIPPVIRKYGMHMD 350
                        330       340       350
                 ....*....|....*....|....*....|
gi 20986497  320 ALSLLGRMLRFEPSARISAAAALRHPFLAK 349
Cdd:PHA03207 351 VEYLIAKMLTFDQEFRPSAQDILSLPLFTK 380
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
50-349 4.22e-20

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: 91.63  E-value: 4.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  50 DVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPnafdvvTNAKRTLR----ELKILKHFKHDNIIAIKD------ 119
Cdd:cd06644   9 DPNEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIE------TKSEEELEdymvEIEILATCNHPYIVKLLGafywdg 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 120 ---ILRPTVPYGEFKSVYVVLDlmesdlhqiihssQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCEL 196
Cdd:cd06644  83 klwIMIEFCPGGAVDAIMLELD-------------RGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 197 KIGDFGM-ARGLCTSPAEHQYFMTEYvatrwYRAPELML--SLHE--YTQAIDLWSVGCIFGEMlarRQLFPGKNYVHQL 271
Cdd:cd06644 150 KLADFGVsAKNVKTLQRRDSFIGTPY-----WMAPEVVMceTMKDtpYDYKADIWSLGITLIEM---AQIEPPHHELNPM 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 272 QLIMMVLGTPSPAVIqavgaervrayiqslpprQPVPWETVYPgadrqalSLLGRMLRFEPSARISAAAALRHPFLAK 349
Cdd:cd06644 222 RVLLKIAKSEPPTLS------------------QPSKWSMEFR-------DFLKTALDKHPETRPSAAQLLEHPFVSS 274
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
50-354 4.37e-20

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: 91.59  E-value: 4.37e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  50 DVGDEYEIIET---IGNGAYGVVSSARRRLTGQQVAIKKIpnafDVVTNAKRTL--RELKILKHFKHDNIIAI-KDILrp 123
Cdd:cd06659  15 DQGDPRQLLENyvkIGEGSTGVVCIAREKHSGRQVAVKMM----DLRKQQRRELlfNEVVIMRDYQHPNVVEMyKSYL-- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 124 tvpYGEfkSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGm 203
Cdd:cd06659  89 ---VGE--ELWVLMEYLQGGALTDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFG- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 204 argLCTSPAEHQYFMTEYVATRWYRAPELMLSLhEYTQAIDLWSVGcifgemlarrqlfpgknyvhqLQLIMMVLGTP-- 281
Cdd:cd06659 163 ---FCAQISKDVPKRKSLVGTPYWMAPEVISRC-PYGTEVDIWSLG---------------------IMVIEMVDGEPpy 217
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 282 -SPAVIQAVgaERVRayiQSLPPRQPVPWETVYPGADrqalsLLGRMLRFEPSARISAAAALRHPFLAKYHDPD 354
Cdd:cd06659 218 fSDSPVQAM--KRLR---DSPPPKLKNSHKASPVLRD-----FLERMLVRDPQERATAQELLDHPFLLQTGLPE 281
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
50-348 4.86e-20

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: 91.65  E-value: 4.86e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  50 DVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNafDVVTNAKRTLR-ELKILKHFKHDNIIAIKDIlrptvpYG 128
Cdd:cd14168   7 DIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPK--KALKGKESSIEnEIAVLRKIKHENIVALEDI------YE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV---NENCELKIGDFGMA 204
Cdd:cd14168  79 SPNHLYLVMQLVSGgELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RGLCTSPAehqyfMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMmvlgtpspa 284
Cdd:cd14168 159 KMEGKGDV-----MSTACGTPGYVAPEV-LAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQIL--------- 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 285 viqavgaervRAYIQSLPPRqpvpWETVYPGADrqalSLLGRMLRFEPSARISAAAALRHPFLA 348
Cdd:cd14168 224 ----------KADYEFDSPY----WDDISDSAK----DFIRNLMEKDPNKRYTCEQALRHPWIA 269
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
54-256 6.09e-20

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: 90.93  E-value: 6.09e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnafdvvtnAKRTLrelkILKHfKHDNIIAIKDIL----RPTVP--Y 127
Cdd:cd05609   1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKI---------NKQNL----ILRN-QIQQVFVERDILtfaeNPFVVsmY 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 128 GEFKSVYVVLDLME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGM 203
Cdd:cd05609  67 CSFETKRHLCMVMEyvegGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGL 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 204 AR----GLCTSPAEH------QYFMTEYV-ATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEML 256
Cdd:cd05609 147 SKiglmSLTTNLYEGhiekdtREFLDKQVcGTPEYIAPEVILR-QGYGKPVDWWAMGIILYEFL 209
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
16-348 6.96e-20

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 93.99  E-value: 6.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   16 EPPGPVKAEPAHT----AASVAAKNLALLKARsfdvtFDVGDE----YEIIETIGNGAYG-VVSSARRRLTGQQVAIKKI 86
Cdd:PHA03210 108 GPSGAEDSDASHLdfdeAPPDAAGPVPLAQAK-----LKHDDEflahFRVIDDLPAGAFGkIFICALRASTEEAEARRGV 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   87 PNAFDVVTNAKRTL---------------RELKILKHFKHDNIIAIKDILRPTvpygefKSVYVVLDLMESDLHQIIHSS 151
Cdd:PHA03210 183 NSTNQGKPKCERLIakrvkagsraaiqleNEILALGRLNHENILKIEEILRSE------ANTYMITQKYDFDLYSFMYDE 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  152 ------QPLtLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMArglctSPAEHQYFMTEY--VA 223
Cdd:PHA03210 257 afdwkdRPL-LKQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTA-----MPFEKEREAFDYgwVG 330
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  224 TRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLArRQLFP----GKNYVHQLQLIMMVLGT-----PSPAV-----IQAV 289
Cdd:PHA03210 331 TVATNSPE-ILAGDGYCEITDIWSCGLILLDMLS-HDFCPigdgGGKPGKQLLKIIDSLSVcdeefPDPPCklfdyIDSA 408
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497  290 GAERVRAYIQSLPPRQPVPWETVYPgadrqalslLGRMLRFEPSARISAAAALRHPFLA 348
Cdd:PHA03210 409 EIDHAGHSVPPLIRNLGLPADFEYP---------LVKMLTFDWHLRPGAAELLALPLFS 458
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
55-249 7.84e-20

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: 89.68  E-value: 7.84e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKilkhfKHDNIIAIKDILRPTVPYGEFKSVY 134
Cdd:cd14050   3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRKLEEVE-----RHEKLGEHPNCVRFIKAWEEKGILY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEH 214
Cdd:cd14050  78 IQTELCDTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDKEDIHD 157
                       170       180       190
                ....*....|....*....|....*....|....*
gi 20986497 215 QyfmTEYVATrwYRAPELMLSlhEYTQAIDLWSVG 249
Cdd:cd14050 158 A---QEGDPR--YMAPELLQG--SFTKAADIFSLG 185
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
61-374 1.19e-19

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: 90.54  E-value: 1.19e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRL---TGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIkdilrptvpYGEFKS---VY 134
Cdd:cd05582   3 LGQGSFGKVFLVRKITgpdAGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKL---------HYAFQTegkLY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFgmarGLCTSPAE 213
Cdd:cd05582  74 LILDFLRGgDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDF----GLSKESID 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 214 HQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMV-LGTPspaviqavgae 292
Cdd:cd05582 150 HEKKAYSFCGTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAkLGMP----------- 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 293 rvrayiQSLPPrqpvpwetvypgadrQALSLLGRMLRFEPSARISAAAA-----LRHPFLA---------KYHDPDDEPD 358
Cdd:cd05582 218 ------QFLSP---------------EAQSLLRALFKRNPANRLGAGPDgveeiKRHPFFAtidwnklyrKEIKPPFKPA 276
                       330
                ....*....|....*..
gi 20986497 359 CAPPFD-FAFDREALTR 374
Cdd:cd05582 277 VSRPDDtFYFDPEFTSR 293
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
50-347 1.64e-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: 89.29  E-value: 1.64e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  50 DVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfdVVTNAKRTL------RELKILKHFKHDNIIAIKDILRP 123
Cdd:cd14195   2 MVEDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKR--RLSSSRRGVsreeieREVNILREIQHPNIITLHDIFEN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 124 TVpygefkSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNE----NCELKI 198
Cdd:cd14195  80 KT------DVVLILELVSGgELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDknvpNPRIKL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 199 GDFGMARGLCTSPAEHQYFMT-EYVatrwyrAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLqlimmv 277
Cdd:cd14195 154 IDFGIAHKIEAGNEFKNIFGTpEFV------APEI-VNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETL------ 220
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 278 lgtpspAVIQAVGAERVRAYiqslpprqpvpwetvYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14195 221 ------TNISAVNYDFDEEY---------------FSNTSELAKDFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
102-262 1.71e-19

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: 89.22  E-value: 1.71e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 102 ELKILKHFKHDNIIAIKDILRPtvpyGEFksVYVVLDL-MESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIH 180
Cdd:cd14187  57 EIAIHRSLAHQHVVGFHGFFED----NDF--VYVVLELcRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIH 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 181 RDLKPSNLLVNENCELKIGDFGMA----------RGLCTSPAehqyfmteyvatrwYRAPELmLSLHEYTQAIDLWSVGC 250
Cdd:cd14187 131 RDLKLGNLFLNDDMEVKIGDFGLAtkveydgerkKTLCGTPN--------------YIAPEV-LSKKGHSFEVDIWSIGC 195
                       170
                ....*....|..
gi 20986497 251 IFGEMLARRQLF 262
Cdd:cd14187 196 IMYTLLVGKPPF 207
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
51-266 1.82e-19

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: 89.25  E-value: 1.82e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  51 VGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfdvVTNAKR-------TLRELKILKHFKHDNIIAIKDIlrp 123
Cdd:cd14196   3 VEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKR---QSRASRrgvsreeIEREVSILRQVLHPNIITLHDV--- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 124 tvpYGEFKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSN-LLVNENCEL---KI 198
Cdd:cd14196  77 ---YENRTDVVLILELVSGgELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIPIphiKL 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 199 GDFGMARGLCTSPAEHQYFMT-EYVatrwyrAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKN 266
Cdd:cd14196 154 IDFGLAHEIEDGVEFKNIFGTpEFV------APEI-VNYEPLGLEADMWSIGVITYILLSGASPFLGDT 215
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
53-347 1.93e-19

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: 89.91  E-value: 1.93e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIP-NAFDVVT--NAKRTLRELKILKHFKHDNIIAIKDIlrptvpYGE 129
Cdd:cd14094   3 DVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDvAKFTSSPglSTEDLKREASICHMLKHPHIVELLET------YSS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDLME-SDL-HQIIH--SSQPLTLEHV-RYFLYQLLRGLKYMHSAQVIHRDLKPSNLL---VNENCELKIGDF 201
Cdd:cd14094  77 DGMLYMVFEFMDgADLcFEIVKraDAGFVYSEAVaSHYMRQILEALRYCHDNNIIHRDVKPHCVLlasKENSAPVKLGGF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 202 GMARGLctspAEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGknyvhqlqlimmvlgtp 281
Cdd:cd14094 157 GVAIQL----GESGLVAGGRVGTPHFMAPEV-VKREPYGKPVDVWGCGVILFILLSGCLPFYG----------------- 214
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 282 SPAVIQavgaERVrayIQSLPPRQPVPWETVypgaDRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14094 215 TKERLF----EGI---IKGKYKMNPRQWSHI----SESAKDLVRRMLMLDPAERITVYEALNHPWI 269
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
61-363 2.23e-19

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: 89.33  E-value: 2.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIpnafDVVTNAKRTL--RELKILKHFKHDNIIAIKDilrptvPYGEFKSVYVVLD 138
Cdd:cd06658  30 IGEGSTGIVCIATEKHTGKQVAVKKM----DLRKQQRRELlfNEVVIMRDYHHENVVDMYN------SYLVGDELWVVME 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 139 LMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFgmarGLCTSPAEHQYFM 218
Cdd:cd06658 100 FLEGGALTDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDF----GFCAQVSKEVPKR 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 219 TEYVATRWYRAPELMLSLhEYTQAIDLWSVGcifgemlarrqlfpgknyvhqLQLIMMVLGTP---SPAVIQAVgaERVR 295
Cdd:cd06658 176 KSLVGTPYWMAPEVISRL-PYGTEVDIWSLG---------------------IMVIEMIDGEPpyfNEPPLQAM--RRIR 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 296 ayiQSLPPRqpVPWETVYPGADRQALSLlgrMLRFEPSARISAAAALRHPFLaKYHDPddePDCAPPF 363
Cdd:cd06658 232 ---DNLPPR--VKDSHKVSSVLRGFLDL---MLVREPSQRATAQELLQHPFL-KLAGP---PSCIVPL 287
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
55-347 3.29e-19

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: 88.11  E-value: 3.29e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAF---DVVTNakrtlrELKILKHFKHDNIIAIKDILRPTVPYgefk 131
Cdd:cd14113   9 YSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLmkrDQVTH------ELGVLQSLQHPQLVGLLDTFETPTSY---- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 svYVVLDLMESD-LHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE---LKIGDFGMARGL 207
Cdd:cd14113  79 --ILVLEMADQGrLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDAVQL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 CTSPAEHQYFMTEYVAtrwyrAPELMLSlHEYTQAIDLWSVGCIfgemlarrqlfpgkNYVhqlqlimmVLGTPSPAVIQ 287
Cdd:cd14113 157 NTTYYIHQLLGSPEFA-----APEIILG-NPVSLTSDLWSIGVL--------------TYV--------LLSGVSPFLDE 208
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 288 AVgaERVRAYIQSLPPRQPvpwETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14113 209 SV--EETCLNICRLDFSFP---DDYFKGVSQKAKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
61-253 4.23e-19

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: 88.48  E-value: 4.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVvTNAKRTLRELKILKHFKHDNIIAIKDilrptVPYGEFKSVYVVLDL- 139
Cdd:cd14038   2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSP-KNRERWCLEIQIMKRLNHPNVVAARD-----VPEGLQKLAPNDLPLl 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 140 -ME----SDLHQIIHSSQP---LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCEL---KIGDFGMARGLc 208
Cdd:cd14038  76 aMEycqgGDLRKYLNQFENccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRlihKIIDLGYAKEL- 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 tspaEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVG-----CIFG 253
Cdd:cd14038 155 ----DQGSLCTSFVGTLQYLAPEL-LEQQKYTVTVDYWSFGtlafeCITG 199
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
58-259 5.92e-19

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: 88.57  E-value: 5.92e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  58 IETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNA-KRTLRELKILKHFKHDNIIAIKDIlrptvpYGEFKSVYVV 136
Cdd:cd06635  30 LREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKwQDIIKEVKFLQRIKHPNSIEYKGC------YLREHTAWLV 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 137 LDLM---ESDLHQIihSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglCTSPAe 213
Cdd:cd06635 104 MEYClgsASDLLEV--HKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSAS--IASPA- 178
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 20986497 214 hqyfmTEYVATRWYRAPELMLSLHE--YTQAIDLWSVGCIFGEMLARR 259
Cdd:cd06635 179 -----NSFVGTPYWMAPEVILAMDEgqYDGKVDVWSLGITCIELAERK 221
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
54-284 6.73e-19

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


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 87.39  E-value: 6.73e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnAFDVVTNAKRTLRELKILKHF-KHDNIIAIKDilrPTVPYGEFKS 132
Cdd:cd13985   1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKRM--YFNDEEQLRVAIKEIEIMKRLcGHPNIVQYYD---SAILSSEGRK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 -VYVVLDLMESDLHQIIHSS--QPLTLEHVRYFLYQLLRGLKYMHSAQ--VIHRDLKPSNLLVNENCELKIGDFGMArgl 207
Cdd:cd13985  76 eVLLLMEYCPGSLVDILEKSppSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSA--- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 ctSPAEHQYFMTEYVA----------TRWYRAPElMLSLHEY---TQAIDLWSVGCIFGEMLARRQLF---------PGK 265
Cdd:cd13985 153 --TTEHYPLERAEEVNiieeeiqkntTPMYRAPE-MIDLYSKkpiGEKADIWALGCLLYKLCFFKLPFdessklaivAGK 229
                       250       260
                ....*....|....*....|....*.
gi 20986497 266 -------NYVHQLQLIMMVLGTPSPA 284
Cdd:cd13985 230 ysipeqpRYSPELHDLIRHMLTPDPA 255
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
61-287 7.06e-19

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: 87.67  E-value: 7.06e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRltGQQVAIK----KIPNAFDVVT--------------NAKRTLR-ELKILKHFKHDNIIAIKDIl 121
Cdd:cd14000   2 LGDGGFGSVYRASYK--GEPVAVKifnkHTSSNFANVPadtmlrhlratdamKNFRLLRqELTVLSHLHHPSIVYLLGI- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 122 rptvpygEFKSVYVVLDL-----MESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV-----N 191
Cdd:cd14000  79 -------GIHPLMLVLELaplgsLDHLLQQDSRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVwtlypN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 192 ENCELKIGDFGMARGLCTSPAEhqyfmtEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKnyvHQL 271
Cdd:cd14000 152 SAIIIKIADYGISRQCCRMGAK------GSEGTPGFRAPEIARGNVIYNEKVDVFSFGMLLYEILSGGAPMVGH---LKF 222
                       250
                ....*....|....*.
gi 20986497 272 QLIMMVLGTPSPAVIQ 287
Cdd:cd14000 223 PNEFDIHGGLRPPLKQ 238
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
55-347 7.57e-19

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: 86.87  E-value: 7.57e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPnaFDVVTNAkRTLRELKILKHFKHDNIIAIKDIlrptvpYGEFKSVY 134
Cdd:cd14107   4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIP--LRSSTRA-RAFQERDILARLSHRRLTCLLDQ------FETRKTLI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV--NENCELKIGDFGMARGLctSP 211
Cdd:cd14107  75 LILELCSSeELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFAQEI--TP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 212 AEHQYfmTEYvATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMmvlgtpspaviqavga 291
Cdd:cd14107 153 SEHQF--SKY-GSPEFVAPEI-VHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVA---------------- 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 292 ervrayiqslppRQPVPWET-VYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14107 213 ------------EGVVSWDTpEITHLSEDAKDFIKRVLQPDPEKRPSASECLSHEWF 257
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
41-264 8.58e-19

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 87.78  E-value: 8.58e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  41 KARSFDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpNAFDVVTNAKRT--LRELKILKHFKHDNIIaik 118
Cdd:cd08229  12 KALRPDMGYNTLANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKV-QIFDLMDAKARAdcIKEIDLLKQLNHPNVI--- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 119 dilRPTVPYGEFKSVYVVLDLMES-DLHQIIH---SSQPLTLEHV--RYFLyQLLRGLKYMHSAQVIHRDLKPSNLLVNE 192
Cdd:cd08229  88 ---KYYASFIEDNELNIVLELADAgDLSRMIKhfkKQKRLIPEKTvwKYFV-QLCSALEHMHSRRVMHRDIKPANVFITA 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 193 NCELKIGDFGMARGLCT-SPAEHQyfmteYVATRWYRAPElmlSLHE--YTQAIDLWSVGCIFGEMLARRQLFPG 264
Cdd:cd08229 164 TGVVKLGDLGLGRFFSSkTTAAHS-----LVGTPYYMSPE---RIHEngYNFKSDIWSLGCLLYEMAALQSPFYG 230
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
61-265 8.71e-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: 88.00  E-value: 8.71e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVvtNAKRTLRELKILKhfKHDNIIAIKDILrptvpYGEFKSvYVVLDLM 140
Cdd:cd14180  14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRMEA--NTQREVAALRLCQ--SHPNIVALHEVL-----HDQYHT-YLVMELL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 ES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV---NENCELKIGDFGMARglcTSPAEHQY 216
Cdd:cd14180  84 RGgELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYadeSDGAVLKVIDFGFAR---LRPQGSRP 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 20986497 217 FMTEyVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGK 265
Cdd:cd14180 161 LQTP-CFTLQYAAPEL-FSNQGYDESCDLWSLGVILYTMLSGQVPFQSK 207
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
53-256 1.16e-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: 88.14  E-value: 1.16e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdvvtnakrTLRELKILKHFKHDNIIAIKDIL----RPTVP-- 126
Cdd:cd05598   1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMK--------------TLRKKDVLKRNQVAHVKAERDILaeadNEWVVkl 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 YGEFK---SVYVVL------DLMeSDLHQIIHSSQPLTlehvRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELK 197
Cdd:cd05598  67 YYSFQdkeNLYFVMdyipggDLM-SLLIKKGIFEEDLA----RFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIK 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 198 IGDFgmarGLCTS---PAEHQYFMTE-YVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd05598 142 LTDF----GLCTGfrwTHDSKYYLAHsLVGTPNYIAPEV-LLRTGYTQLCDWWSVGVILYEML 199
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
39-347 1.28e-18

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: 87.47  E-value: 1.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  39 LLKARSFDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnafDVVTNAKRTL--RELKILKHFKHDNIIA 116
Cdd:cd06656   5 LEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQM----NLQQQPKKELiiNEILVMRENKNPNIVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 117 IKDilrptvPYGEFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCEL 196
Cdd:cd06656  81 YLD------SYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSV 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 197 KIGDFgmarGLCTSPAEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLImM 276
Cdd:cd06656 155 KLTDF----GFCAQITPEQSKRSTMVGTPYWMAPEV-VTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-A 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 277 VLGTPspaviQAVGAERVRAYIQslpprqpvpwetvypgadrqalSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd06656 229 TNGTP-----ELQNPERLSAVFR----------------------DFLNRCLEMDVDRRGSAKELLQHPFL 272
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
59-356 1.44e-18

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


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 86.86  E-value: 1.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQVAIKKIPnaFDVVTNAKRT-LRELKILkhFKHDNIIAIKDilrptvpYGEF---KSVY 134
Cdd:cd06619   7 EILGHGNGGTVYKAYHLLTRRILAVKVIP--LDITVELQKQiMSELEIL--YKCDSPYIIGF-------YGAFfveNRIS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMES---DLHQIIHssqpltlEHVR-YFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTS 210
Cdd:cd06619  76 ICTEFMDGgslDVYRKIP-------EHVLgRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 211 PAehqyfmTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARR----QLFPGKNYVHQLQLIMMVlgtpspavi 286
Cdd:cd06619 149 IA------KTYVGTNAYMAPERISG-EQYGIHSDVWSLGISFMELALGRfpypQIQKNQGSLMPLQLLQCI--------- 212
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 287 qavgaervrayIQSLPPRQPV-PWETVYpgadrqaLSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDE 356
Cdd:cd06619 213 -----------VDEDPPVLPVgQFSEKF-------VHFITQCMRKQPKERPAPENLMDHPFIVQYNDGNAE 265
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
61-262 1.54e-18

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: 86.81  E-value: 1.54e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIpnafdvvtNAKR---------TLRELKILKHFKHDNIIAIkdilrpTVPYGEFK 131
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKL--------DKKRikkkkgetmALNEKIILEKVSSPFIVSL------AYAFETKD 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMES-DLH-QIIHSSQP-LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMArglC 208
Cdd:cd05577  67 KLCLVLTLMNGgDLKyHIYNVGTRgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLA---V 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 20986497 209 TSPAEHQyfMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLF 262
Cdd:cd05577 144 EFKGGKK--IKGRVGTHGYMAPEVLQKEVAYDFSVDWFALGCMLYEMIAGRSPF 195
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
53-276 1.69e-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: 87.83  E-value: 1.69e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTN-AKRTLRELKILKHFKHDNIIAIKDILRPtvpygEFK 131
Cdd:cd05593  15 NDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDeVAHTLTESRVLKNTRHPFLTSLKYSFQT-----KDR 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSP 211
Cdd:cd05593  90 LCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDA 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 212 AEhqyfMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMM 276
Cdd:cd05593 170 AT----MKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM 229
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
53-266 1.80e-18

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: 86.72  E-value: 1.80e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIK--KIPNAFDV-----VTNAKRTLRELKilkhfkHDNIIAIkdilrptv 125
Cdd:cd05612   1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKvmAIPEVIRLkqeqhVHNEKRVLKEVS------HPFIIRL-------- 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 pYGEFKSVYVVLDLME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDF 201
Cdd:cd05612  67 -FWTEHDQRFLYMLMEyvpgGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDF 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497 202 GMAR-------GLCTSPaehqyfmtEYVatrwyrAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKN 266
Cdd:cd05612 146 GFAKklrdrtwTLCGTP--------EYL------APEVIQS-KGHNKAVDWWALGILIYEMLVGYPPFFDDN 202
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
58-306 2.04e-18

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: 87.00  E-value: 2.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  58 IETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfDVVTNAK--RTLRELKILKHFKHDNIIAIKDIlrptvpYGEFKSVYV 135
Cdd:cd06634  20 LREIGHGSFGAVYFARDVRNNEVVAIKKMSYS-GKQSNEKwqDIIKEVKFLQKLRHPNTIEYRGC------YLREHTAWL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 136 VLDLM---ESDLHQIihSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglCTSPA 212
Cdd:cd06634  93 VMEYClgsASDLLEV--HKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSAS--IMAPA 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 213 ehqyfmTEYVATRWYRAPELMLSLHE--YTQAIDLWSVGCIFGEMLARRqlfPGKNYVHQLQLIMMVLGTPSPAVIQAVG 290
Cdd:cd06634 169 ------NSFVGTPYWMAPEVILAMDEgqYDGKVDVWSLGITCIELAERK---PPLFNMNAMSALYHIAQNESPALQSGHW 239
                       250       260
                ....*....|....*....|
gi 20986497 291 AERVRAYI----QSLPPRQP 306
Cdd:cd06634 240 SEYFRNFVdsclQKIPQDRP 259
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
53-393 2.04e-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: 86.42  E-value: 2.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDvvtnaKRTLR-ELKILKHFKHDNIIAIKDILR-PTvpygef 130
Cdd:cd14085   3 DFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVD-----KKIVRtEIGVLLRLSHPNIIKLKEIFEtPT------ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 kSVYVVLDLMES-DLHQII----HSSQPLTLEHVRyflyQLLRGLKYMHSAQVIHRDLKPSNLLV---NENCELKIGDFG 202
Cdd:cd14085  72 -EISLVLELVTGgELFDRIvekgYYSERDAADAVK----QILEAVAYLHENGIVHRDLKPENLLYatpAPDAPLKIADFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 203 MARGLctspaEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLF---PGKNYVHQLQLimmvlg 279
Cdd:cd14085 147 LSKIV-----DQQVTMKTVCGTPGYCAPEI-LRGCAYGPEVDMWSVGVITYILLCGFEPFydeRGDQYMFKRIL------ 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 280 tpspaviqavgaervRAYIQSLPPRqpvpWETVYPGADrqalSLLGRMLRFEPSARISAAAALRHPFL----AKYHDPDD 355
Cdd:cd14085 215 ---------------NCDYDFVSPW----WDDVSLNAK----DLVKKLIVLDPKKRLTTQQALQHPWVtgkaANFAHMDT 271
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 20986497 356 epdcappfdfafdrealTRERIKEaivaeiedFHARRE 393
Cdd:cd14085 272 -----------------AQKKLQE--------FNARRK 284
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
53-347 2.66e-18

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: 85.69  E-value: 2.66e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLR-ELKILKHFKHDNIiaikdiLRPTVPYGEFK 131
Cdd:cd14117   6 DDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHQLRrEIEIQSHLRHPNI------LRLYNYFHDRK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLM-ESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMArglCTS 210
Cdd:cd14117  80 RIYLILEYApRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWS---VHA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 211 PAEHQYFMteyVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVlgtpspaviqavg 290
Cdd:cd14117 157 PSLRRRTM---CGTLDYLPPE-MIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKV------------- 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 291 aervrayIQSLPPRQPvpwetvypgadRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14117 220 -------DLKFPPFLS-----------DGSRDLISKLLRYHPSERLPLKGVMEHPWV 258
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
59-254 3.44e-18

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: 84.80  E-value: 3.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPygefksVYVVLD 138
Cdd:cd05041   1 EKIGRGNFGDVYRGVLKPDNTEVAVKTCRET-LPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQP------IMIVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 139 LME--SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglctspAEHQy 216
Cdd:cd05041  74 LVPggSLLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSR------EEED- 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 20986497 217 fmTEYVAT--------RWyRAPElMLSLHEYTQAIDLWSVGCIFGE 254
Cdd:cd05041 147 --GEYTVSdglkqipiKW-TAPE-ALNYGRYTSESDVWSFGILLWE 188
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
53-347 4.30e-18

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: 84.94  E-value: 4.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRtlRELKILKHFKHDNIIAIKDilrptvPYGEFKS 132
Cdd:cd14114   2 DHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVR--KEIQIMNQLHHPKLINLHD------AFEDDNE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMESD--LHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL--VNENCELKIGDFGMARGLc 208
Cdd:cd14114  74 MVLILEFLSGGelFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMctTKRSNEVKLIDFGLATHL- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 tSPAEHQYFMTeyvATRWYRAPELM--LSLHEYTqaiDLWSVGCIFGEMLARRQLFPGKNYVHQLQlimmvlgtpspavi 286
Cdd:cd14114 153 -DPKESVKVTT---GTAEFAAPEIVerEPVGFYT---DMWAVGVLSYVLLSGLSPFAGENDDETLR-------------- 211
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 287 qavgaeRVRAyiqslpprqpVPWE---TVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14114 212 ------NVKS----------CDWNfddSAFSGISEEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
53-257 4.57e-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: 86.13  E-value: 4.57e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKipnafdvvtnakrtLRELKILKHFKHDNIIAIKDIL----RPTVP-- 126
Cdd:cd05599   1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKK--------------LRKSEMLEKEQVAHVRAERDILaeadNPWVVkl 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 YGEF---KSVYVVLD----------LMESDLhqiihssqpLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNEN 193
Cdd:cd05599  67 YYSFqdeENLYLIMEflpggdmmtlLMKKDT---------LTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDAR 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 194 CELKIGDFGMARGLCTSpaeHQYFMTeyVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLA 257
Cdd:cd05599 138 GHIKLSDFGLCTGLKKS---HLAYST--VGTPDYIAPEVFLQ-KGYGKECDWWSLGVIMYEMLI 195
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
53-349 6.10e-18

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: 85.57  E-value: 6.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfdvVTNAKRT--LRELKILKHFKHDNIIAIkdilrptvpYGEF 130
Cdd:cd06615   1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLE---IKPAIRNqiIRELKVLHECNSPYIVGF---------YGAF 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVLDLMES----DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSA-QVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd06615  69 YSDGEISICMEHmdggSLDQVLKKAGRIPENILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 206 GLCTSPAehqyfmTEYVATRWYRAPELMLSLHeYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhQLQLIMMvLGTPSPAV 285
Cdd:cd06615 149 QLIDSMA------NSFVGTRSYMSPERLQGTH-YTVQSDIWSLGLSLVEMAIGRYPIPPPD---AKELEAM-FGRPVSEG 217
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 286 IQAVGAERVRAYIQSLPP------------RQPVPwetVYPGA--DRQALSLLGRMLRFEPSARISAAAALRHPFLAK 349
Cdd:cd06615 218 EAKESHRPVSGHPPDSPRpmaifelldyivNEPPP---KLPSGafSDEFQDFVDKCLKKNPKERADLKELTKHPFIKR 292
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
54-249 7.07e-18

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: 85.00  E-value: 7.07e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSA---------------RRRLTGQQVAIKKIP---------NAFDVVTNAKRTLRELKILKHF 109
Cdd:cd14200   1 QYKLQSEIGKGSYGVVKLAynesddkyyamkvlsKKKLLKQYGFPRRPPprgskaaqgEQAKPLAPLERVYQEIAILKKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 110 KHDNIIAIKDILRPTVPygefKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL 189
Cdd:cd14200  81 DHVNIVKLIEVLDDPAE----DNLYMVFDLLRKGPVMEVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLL 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497 190 VNENCELKIGDFGMARGLCTSPAEhqyfMTEYVATRWYRAPE-LMLSLHEYT-QAIDLWSVG 249
Cdd:cd14200 157 LGDDGHVKIADFGVSNQFEGNDAL----LSSTAGTPAFMAPEtLSDSGQSFSgKALDVWAMG 214
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
59-257 1.08e-17

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: 83.87  E-value: 1.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQ---VAIKKIPNAFdvvTNAKRT--LRELKILKHFKHDNIIAIKDILrptvpyGEFKSV 133
Cdd:cd05063  11 KVIGAGEFGEVFRGILKMPGRKevaVAIKTLKPGY---TEKQRQdfLSEASIMGQFSHHNIIRLEGVV------TKFKPA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMESD-LHQIIHSSQPltlEHVRYFLYQLLRG----LKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLC 208
Cdd:cd05063  82 MIITEYMENGaLDKYLRDHDG---EFSSYQLVGMLRGiaagMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLE 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPaEHQYFMT-EYVATRWyRAPElMLSLHEYTQAIDLWSVGCIFGEMLA 257
Cdd:cd05063 159 DDP-EGTYTTSgGKIPIRW-TAPE-AIAYRKFTSASDVWSFGIVMWEVMS 205
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
41-347 1.21e-17

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: 84.39  E-value: 1.21e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  41 KARSFDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnafDVVTNAKRTL--RELKILKHFKHDNIIAIK 118
Cdd:cd06655   7 KLRTIVSIGDPKKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQI----NLQKQPKKELiiNEILVMKELKNPNIVNFL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 119 DilrptvPYGEFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKI 198
Cdd:cd06655  83 D------SFLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 199 GDFgmarGLCTSPAEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLImMVL 278
Cdd:cd06655 157 TDF----GFCAQITPEQSKRSTMVGTPYWMAPEV-VTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI-ATN 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 279 GTPSpaviqavgaervrayIQSLPPRQPVpwetvypgadrqALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd06655 231 GTPE---------------LQNPEKLSPI------------FRDFLNRCLEMDVEKRGSAKELLQHPFL 272
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
57-257 1.34e-17

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 83.76  E-value: 1.34e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  57 IIETIGNGAYGVVSSARRRLTGQQ---VAIKKIPNAFdvvTNAKRT--LRELKILKHFKHDNIIAIKDILRPTVPygefk 131
Cdd:cd05066   8 IEKVIGAGEFGEVCSGRLKLPGKReipVAIKTLKAGY---TEKQRRdfLSEASIMGQFDHPNIIHLEGVVTRSKP----- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 sVYVVLDLMES---DLHQIIHSSQpLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLC 208
Cdd:cd05066  80 -VMIVTEYMENgslDAFLRKHDGQ-FTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLE 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPaEHQYFMT-EYVATRWyRAPElMLSLHEYTQAIDLWSVGCIFGEMLA 257
Cdd:cd05066 158 DDP-EAAYTTRgGKIPIRW-TAPE-AIAYRKFTSASDVWSYGIVMWEVMS 204
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
53-374 1.35e-17

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: 85.08  E-value: 1.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTN-AKRTLRELKILKHFKHDNIIAIKDilrptvpygEFK 131
Cdd:cd05594  25 NDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDeVAHTLTENRVLQNSRHPFLTALKY---------SFQ 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQ-VIHRDLKPSNLLVNENCELKIGDFgmarG 206
Cdd:cd05594  96 THDRLCFVMEyangGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDF----G 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 207 LCTSPAEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMvlgtpspavi 286
Cdd:cd05594 172 LCKEGIKDGATMKTFCGTPEYLAPEV-LEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILM---------- 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 287 qavgaERVRaYIQSLPPrqpvpwetvypgadrQALSLLGRMLRFEPSARI-----SAAAALRHPFLAKYHDPD-DEPDCA 360
Cdd:cd05594 241 -----EEIR-FPRTLSP---------------EAKSLLSGLLKKDPKQRLgggpdDAKEIMQHKFFAGIVWQDvYEKKLV 299
                       330
                ....*....|....
gi 20986497 361 PPFDFAFDREALTR 374
Cdd:cd05594 300 PPFKPQVTSETDTR 313
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
39-281 1.36e-17

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: 84.39  E-value: 1.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  39 LLKARSFDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnafDVVTNAKRTL--RELKILKHFKHDNIIA 116
Cdd:cd06654   6 LEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQM----NLQQQPKKELiiNEILVMRENKNPNIVN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 117 IKDilrptvPYGEFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCEL 196
Cdd:cd06654  82 YLD------SYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 197 KIGDFgmarGLCTSPAEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLImM 276
Cdd:cd06654 156 KLTDF----GFCAQITPEQSKRSTMVGTPYWMAPEV-VTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI-A 229

                ....*
gi 20986497 277 VLGTP 281
Cdd:cd06654 230 TNGTP 234
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
53-348 1.39e-17

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: 83.92  E-value: 1.39e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPnafdvvTNAKRTLR----ELKILKHFKHDNIIAIKDILrptvpYG 128
Cdd:cd06643   5 DFWEIVGELGDGAFGKVYKAQNKETGILAAAKVID------TKSEEELEdymvEIDILASCDHPNIVKLLDAF-----YY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EfKSVYVVLDLMESDLHQ--IIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARG 206
Cdd:cd06643  74 E-NNLWILIEFCAGGAVDavMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 207 LCTSPAEHQYFmteyVATRWYRAPELMLSL----HEYTQAIDLWSVGCIFGEMlarRQLFPGKNYVHQLQLIMMVLGTPS 282
Cdd:cd06643 153 NTRTLQRRDSF----IGTPYWMAPEVVMCEtskdRPYDYKADVWSLGVTLIEM---AQIEPPHHELNPMRVLLKIAKSEP 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 283 PAVIqavgaervrayiqslpprQPVPWETVYPgadrqalSLLGRMLRFEPSARISAAAALRHPFLA 348
Cdd:cd06643 226 PTLA------------------QPSRWSPEFK-------DFLRKCLEKNVDARWTTSQLLQHPFVS 266
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
49-256 2.56e-17

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: 83.32  E-value: 2.56e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  49 FDVGDEYEIIETIGNGAYGVVSSARRrlTGQQVAIKKIPNAFDVVTNAKRTL--RELKILKHFKHDNIIAI----KDILR 122
Cdd:cd14158  11 FDERPISVGGNKLGEGGFGVVFKGYI--NDKNVAVKKLAAMVDISTEDLTKQfeQEIQVMAKCQHENLVELlgysCDGPQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 123 PTVPYgefksVYVVLDLMESDLHQIIHSSqPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFG 202
Cdd:cd14158  89 LCLVY-----TYMPNGSLLDRLACLNDTP-PLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFG 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 203 MARglcTSPAEHQYFMTE-YVATRWYRAPELMlsLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd14158 163 LAR---ASEKFSQTIMTErIVGTTAYMAPEAL--RGEITPKSDIFSFGVVLLEII 212
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
54-257 2.66e-17

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 84.10  E-value: 2.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdvvtnakrTLRELKILKHFKHDNIIAIKDILR----PTV---- 125
Cdd:PTZ00263  19 DFEMGETLGTGSFGRVRIAKHKGTGEYYAIK--------------CLKKREILKMKQVQHVAQEKSILMelshPFIvnmm 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  126 -PYGEFKSVYVVLD-LMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGM 203
Cdd:PTZ00263  85 cSFQDENRVYFLLEfVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGF 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497  204 AR-------GLCTSPaehqyfmtEYVatrwyrAPELMLSlHEYTQAIDLWSVGCIFGEMLA 257
Cdd:PTZ00263 165 AKkvpdrtfTLCGTP--------EYL------APEVIQS-KGHGKAVDWWTMGVLLYEFIA 210
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
61-353 3.07e-17

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: 83.15  E-value: 3.07e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIpnafDVVTNAKRTL--RELKILKHFKHDNIIAIKDilrptvPYGEFKSVYVVLD 138
Cdd:cd06657  28 IGEGSTGIVCIATVKSSGKLVAVKKM----DLRKQQRRELlfNEVVIMRDYQHENVVEMYN------SYLVGDELWVVME 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 139 LMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFgmarGLCTSPAEHQYFM 218
Cdd:cd06657  98 FLEGGALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDF----GFCAQVSKEVPRR 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 219 TEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMmvlgtpspaviqavgaervrayi 298
Cdd:cd06657 174 KSLVGTPYWMAPELISRL-PYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIR----------------------- 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 299 QSLPPRQPvPWETVYPGADrqalSLLGRMLRFEPSARISAAAALRHPFLAKYHDP 353
Cdd:cd06657 230 DNLPPKLK-NLHKVSPSLK----GFLDRLLVRDPAQRATAAELLKHPFLAKAGPP 279
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
58-256 3.08e-17

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: 82.76  E-value: 3.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  58 IETIGNGAYGVVSSAR----RRLTGQQVAIKKIPNAFDvvTNAKRTLRELKILKHFKHDNIIAIKDI-----------LR 122
Cdd:cd14205   9 LQQLGKGNFGSVEMCRydplQDNTGEVVAVKKLQHSTE--EHLRDFEREIEILKSLQHDNIVKYKGVcysagrrnlrlIM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 123 PTVPYGEFKsvyvvlDLMESDLHQIihssqpltlEHVRYFLY--QLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGD 200
Cdd:cd14205  87 EYLPYGSLR------DYLQKHKERI---------DHIKLLQYtsQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGD 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 201 FGMARGLctsPAEHQYFMTEYVATR---WYrAPElMLSLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd14205 152 FGLTKVL---PQDKEYYKVKEPGESpifWY-APE-SLTESKFSVASDVWSFGVVLYELF 205
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
59-258 3.90e-17

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: 81.90  E-value: 3.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKrTLRELKILKHFKHDNIIAIKDILRPTVPygefksVYVVLD 138
Cdd:cd05084   2 ERIGRGNFGEVFSGRLRADNTPVAVKSCRETLPPDLKAK-FLQEARILKQYSHPNIVRLIGVCTQKQP------IYIVME 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 139 LMES-DLHQIIHSSQP-LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglctSPAEHQY 216
Cdd:cd05084  75 LVQGgDFLTFLRTEGPrLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSR----EEEDGVY 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 20986497 217 FMT---EYVATRWyRAPElMLSLHEYTQAIDLWSVGCIFGEMLAR 258
Cdd:cd05084 151 AATggmKQIPVKW-TAPE-ALNYGRYSSESDVWSFGILLWETFSL 193
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
54-257 4.22e-17

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: 84.31  E-value: 4.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnafdvvtnAKRTLRELKILKHfkhdnIIAIKDILRPTvpygefKSV 133
Cdd:cd05600  12 DFQILTQVGQGGYGSVFLARKKDTGEICALKIM---------KKKVLFKLNEVNH-----VLTERDILTTT------NSP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDL------------ME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELK 197
Cdd:cd05600  72 WLVKLLyafqdpenvylaMEyvpgGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 198 IGDFGMARG----------------------LCTSPAEHQYFMTEY-----------VATRWYRAPElMLSLHEYTQAID 244
Cdd:cd05600 152 LTDFGLASGtlspkkiesmkirleevkntafLELTAKERRNIYRAMrkedqnyansvVGSPDYMAPE-VLRGEGYDLTVD 230
                       250
                ....*....|...
gi 20986497 245 LWSVGCIFGEMLA 257
Cdd:cd05600 231 YWSLGCILFECLV 243
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
56-257 4.46e-17

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


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 82.22  E-value: 4.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  56 EIIETIGNGAYGVVSSARRRLTGQQ---VAIKKIPNAFdvvTNAKRT--LRELKILKHFKHDNIIAIKDILRPTVPygef 130
Cdd:cd05065   7 KIEEVIGAGEFGEVCRGRLKLPGKReifVAIKTLKSGY---TEKQRRdfLSEASIMGQFDHPNIIHLEGVVTKSRP---- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 ksVYVVLDLME-----SDLHQiihSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd05065  80 --VMIITEFMEngaldSFLRQ---NDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSR 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 20986497 206 GLCTSPAEHQYF--MTEYVATRWyRAPElMLSLHEYTQAIDLWSVGCIFGEMLA 257
Cdd:cd05065 155 FLEDDTSDPTYTssLGGKIPIRW-TAPE-AIAYRKFTSASDVWSYGIVMWEVMS 206
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
58-337 4.88e-17

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: 82.25  E-value: 4.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  58 IETIGNGAYGVVSSARRRL----TGQQVAIKKIPNafDVVTNAKRTLRELKILKHFKHDNIIAIKDilrptVPYGEFK-S 132
Cdd:cd05081   9 ISQLGKGNFGSVELCRYDPlgdnTGALVAVKQLQH--SGPDQQRDFQREIQILKALHSDFIVKYRG-----VSYGPGRrS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMESD-LHQIIHSSQPlTLEHVRYFLY--QLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLct 209
Cdd:cd05081  82 LRLVMEYLPSGcLRDFLQRHRA-RLDASRLLLYssQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLL-- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 210 sPAEHQYFMTEYVATR---WYrAPElMLSLHEYTQAIDLWSVGCIFGEML--ARRQLFPGKNYVHqlqliMMVLGTPSPA 284
Cdd:cd05081 159 -PLDKDYYVVREPGQSpifWY-APE-SLSDNIFSRQSDVWSFGVVLYELFtyCDKSCSPSAEFLR-----MMGCERDVPA 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 20986497 285 VIQAVgaERVRAyiqslPPRQPVPwetvyPGADRQALSLLGRMLRFEPSARIS 337
Cdd:cd05081 231 LCRLL--ELLEE-----GQRLPAP-----PACPAEVHELMKLCWAPSPQDRPS 271
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
53-347 5.22e-17

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: 82.51  E-value: 5.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEII--ETIGNGAYGVVSSARRRLTGQQVAIKkipnafdVVTNAKRTLRELKIlkHFK---HDNIIAIKDILRPTVPY 127
Cdd:cd14171   4 EEYEVNwtQKLGTGISGPVRVCVKKSTGERFALK-------ILLDRPKARTEVRL--HMMcsgHPNIVQIYDVYANSVQF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 128 -GEF---KSVYVVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE---LKIG 199
Cdd:cd14171  75 pGESsprARLLIVMELMEgGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEdapIKLC 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 200 DFGMAR---GLCTSPAEHQYFMTEYV--ATRWYRAPELMLSLHE----YTQAIDLWSVGCIFGEMLARRQLFPGKnyvhq 270
Cdd:cd14171 155 DFGFAKvdqGDLMTPQFTPYYVAPQVleAQRRHRKERSGIPTSPtpytYDKSCDMWSLGVIIYIMLCGYPPFYSE----- 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 271 lqlimmvlgTPSPAViqavgAERVRAYIQS----LPPRQpvpWETVypgaDRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd14171 230 ---------HPSRTI-----TKDMKRKIMTgsyeFPEEE---WSQI----SEMAKDIVRKLLCVDPEERMTIEEVLHHPW 288

                .
gi 20986497 347 L 347
Cdd:cd14171 289 L 289
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
55-254 5.48e-17

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: 81.66  E-value: 5.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLR------ELKI---LKHFKHDNIIAIKDILRPTV 125
Cdd:cd14004   2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDTWVRDRKlgtvplEIHIldtLNKRSHPNIVKLLDFFEDDE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 PYgefksvYVVLDLMES--DLHQIIhSSQPLTLEH-VRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFG 202
Cdd:cd14004  82 FY------YLVMEKHGSgmDLFDFI-ERKPNMDEKeAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFG 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 203 MARGLCTSPaehqyFMTeYVATRWYRAPELMLSLHEYTQAIDLWSVGC-----IFGE 254
Cdd:cd14004 155 SAAYIKSGP-----FDT-FVGTIDYAAPEVLRGNPYGGKEQDIWALGVllytlVFKE 205
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
61-256 5.49e-17

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: 81.60  E-value: 5.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFdvvTNAKRTLRELKILKHFK-HDNIIAIKDILRPTVPYGEFKSVYVVLdl 139
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPS---TKLKDFLREYNISLELSvHPHIIKTYDVAFETEDYYVFAQEYAPY-- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 140 meSDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSN-LLVNENCE-LKIGDFGMARGLCTspaehqyf 217
Cdd:cd13987  76 --GDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENvLLFDKDCRrVKLCDFGLTRRVGS-------- 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 20986497 218 mTEYVATRW--YRAPELM-LSLHEYTQA---IDLWSVGCIFGEML 256
Cdd:cd13987 146 -TVKRVSGTipYTAPEVCeAKKNEGFVVdpsIDVWAFGVLLFCCL 189
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
45-249 5.74e-17

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: 81.98  E-value: 5.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  45 FDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKhfKHDNIIAIKDIL-RP 123
Cdd:cd06638  10 FDSFPDPSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKALS--DHPNVVKFYGMYyKK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 124 TVPYGEfkSVYVVL---------DLMESDLHQIIHSSQPLtlehVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENC 194
Cdd:cd06638  88 DVKNGD--QLWLVLelcnggsvtDLVKGFLKRGERMEEPI----IAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEG 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 195 ELKIGDFGMARGLCTSpaehQYFMTEYVATRWYRAPELMLSLHE----YTQAIDLWSVG 249
Cdd:cd06638 162 GVKLVDFGVSAQLTST----RLRRNTSVGTPFWMAPEVIACEQQldstYDARCDVWSLG 216
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
57-257 5.88e-17

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: 81.65  E-value: 5.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  57 IIETIGNGAYGVVSSARRRLTGQQ---VAIKKIPNAFDvvTNAKRT-LRELKILKHFKHDNIIAIKDILRPTVPygefks 132
Cdd:cd05033   8 IEKVIGGGEFGEVCSGSLKLPGKKeidVAIKTLKSGYS--DKQRLDfLTEASIMGQFDHPNVIRLEGVVTKSRP------ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMES-DLHQII-HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTS 210
Cdd:cd05033  80 VMIVTEYMENgSLDKFLrENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDS 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 20986497 211 PAEHQYfMTEYVATRWyRAPElMLSLHEYTQAIDLWSVGCIFGEMLA 257
Cdd:cd05033 160 EATYTT-KGGKIPIRW-TAPE-AIAYRKFTSASDVWSFGIVMWEVMS 203
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
61-384 7.60e-17

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: 82.23  E-value: 7.60e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFdVVTNAK--RTLRELKILKHFKHDNIIAIKdilrptVPYGEFKSVYVVLD 138
Cdd:cd05585   2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAH-IVSRSEvtHTLAERTVLAQVDCPFIVPLK------FSFQSPEKLYLVLA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 139 LMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFgmarGLCTSPAEHQYF 217
Cdd:cd05585  75 FINGgELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDF----GLCKLNMKDDDK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 218 MTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhqlqlimmvlgTPspaviqavgaERVRAY 297
Cdd:cd05585 151 TNTFCGTPEYLAPELLLG-HGYTKAVDWWTLGVLLYEMLTGLPPFYDEN-------------TN----------EMYRKI 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 298 IQSlPPRQPvpwetvyPGADRQALSLLGRMLRFEPSARISAAAA---LRHPF---------LAKYHDPDDEPDCAPPFDF 365
Cdd:cd05585 207 LQE-PLRFP-------DGFDRDAKDLLIGLLNRDPTKRLGYNGAqeiKNHPFfdqidwkrlLMKKIQPPFKPAVENAIDT 278
                       330       340
                ....*....|....*....|
gi 20986497 366 A-FDREaLTRERIKEAIVAE 384
Cdd:cd05585 279 SnFDEE-FTREKPIDSVVDD 297
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
55-345 7.70e-17

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: 81.13  E-value: 7.70e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDV----VTNAKRTLRE---LKILKHFKHDNIIAIKDILrptvpy 127
Cdd:cd14005   2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTewamINGPVPVPLEialLLKASKPGVPGVIRLLDWY------ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 128 gEFKSVYVVLdlME-----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVN-ENCELKIGDF 201
Cdd:cd14005  76 -ERPDGFLLI--MErpepcQDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 202 GmarglCTSPAEHQYFmTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRqlFPgknYVHQLQLImmvlgtp 281
Cdd:cd14005 153 G-----CGALLKDSVY-TDFDGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGD--IP---FENDEQIL------- 214
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 282 spaviqavgaervRAYIQslpprqpvpwetVYPGADRQALSLLGRMLRFEPSARISAAAALRHP 345
Cdd:cd14005 215 -------------RGNVL------------FRPRLSKECCDLISRCLQFDPSKRPSLEQILSHP 253
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
55-249 8.43e-17

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: 80.84  E-value: 8.43e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKkIPNAFDVVTNAKRTL-RELKILKHFKHDNIIAIKDILRptvpygEFKSV 133
Cdd:cd14075   4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIK-ILDKTKLDQKTQRLLsREISSMEKLHHPNIIRLYEVVE------TLSKL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVldlME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFG------- 202
Cdd:cd14075  77 HLV---MEyasgGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGfsthakr 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 20986497 203 --MARGLCTSPAehqyfmteyvatrwYRAPELMLSLHEYTQAIDLWSVG 249
Cdd:cd14075 154 geTLNTFCGSPP--------------YAAPELFKDEHYIGIYVDIWALG 188
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
52-264 8.81e-17

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 84.46  E-value: 8.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   52 GDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdvvtnakrTLR-EL----KILKHFK----------HDNIIA 116
Cdd:NF033483   6 GGRYEIGERIGRGGMAEVYLAKDTRLDRDVAVK--------------VLRpDLardpEFVARFRreaqsaaslsHPNIVS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  117 IKDIlrptvpyGEFKSV-YVVldlME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVN 191
Cdd:NF033483  72 VYDV-------GEDGGIpYIV---MEyvdgRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILIT 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  192 ENCELKIGDFGMARGLCTSPAEH--------QYFmteyvatrwyrAPElmlslheytQA--------IDLWSVGCIFGEM 255
Cdd:NF033483 142 KDGRVKVTDFGIARALSSTTMTQtnsvlgtvHYL-----------SPE---------QArggtvdarSDIYSLGIVLYEM 201

                 ....*....
gi 20986497  256 LARRQLFPG 264
Cdd:NF033483 202 LTGRPPFDG 210
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
55-357 1.13e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 82.74  E-value: 1.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdvVTNAKRTLRELKILKHFKHDNIIAIKDilrpTVPYGEFKSVy 134
Cdd:PHA03212  94 FSILETFTPGAEGFAFACIDNKTCEHVVIK--------AGQRGGTATEAHILRAINHPSIIQLKG----TFTYNKFTCL- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  135 vVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEH 214
Cdd:PHA03212 161 -ILPRYKTDLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAACFPVDINANK 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  215 QYFMTEYVATrwyRAPELmLSLHEYTQAIDLWSVGCIFGEM------LARRQLFPGK-NYVHQLQLIMMVLGT-PSPAVI 286
Cdd:PHA03212 240 YYGWAGTIAT---NAPEL-LARDPYGPAVDIWSAGIVLFEMatchdsLFEKDGLDGDcDSDRQIKLIIRRSGThPNEFPI 315
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497  287 QAVGAERvRAYIQSL------PPRQPVpWETVYPgADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEP 357
Cdd:PHA03212 316 DAQANLD-EIYIGLAkkssrkPGSRPL-WTNLYE-LPIDLEYLICKMLAFDAHHRPSAEALLDFAAFQDIPDPYPNP 389
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
60-264 1.86e-16

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 80.73  E-value: 1.86e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  60 TIGNGAYGVVSSARRRL---TGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFKSVYVV 136
Cdd:cd05074  16 MLGKGEFGSVREAQLKSedgSFQKVAVKMLKADIFSSSDIEEFLREAACMKEFDHPNVIKLIGVSLRSRAKGRLPIPMVI 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 137 LDLME-SDLHQIIHSS----QPLTL--EHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCT 209
Cdd:cd05074  96 LPFMKhGDLHTFLLMSrigeEPFTLplQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGLSKKIYS 175
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 210 SPAEHQYFMTEyVATRWYRAPELMLSLheYTQAIDLWSVGCIFGEMLARRQL-FPG 264
Cdd:cd05074 176 GDYYRQGCASK-LPVKWLALESLADNV--YTTHSDVWAFGVTMWEIMTRGQTpYAG 228
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
61-272 2.10e-16

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: 80.73  E-value: 2.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVvTNAKRTLRELKILKHFKHDNIIAIKDIlrPtvPYGEFKSVYVVLDLM 140
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSV-KNKDRWCHEIQIMKKLNHPNVVKACDV--P--EEMNFLVNDVPLLAM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 E----SDLHQIIHSSQP---LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNE-NCEL--KIGDFGMAR----- 205
Cdd:cd14039  76 EycsgGDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEiNGKIvhKIIDLGYAKdldqg 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 206 GLCTSpaehqyfmteYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFpgknyVHQLQ 272
Cdd:cd14039 156 SLCTS----------FVGTLQYLAPELFEN-KSYTVTVDYWSFGTMVFECIAGFRPF-----LHNLQ 206
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
59-347 2.10e-16

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: 79.96  E-value: 2.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQVAIKKIPNafdvvTNAKR---TLRELKILKHFKHDNIIAIKDILRptVPygefKSVYV 135
Cdd:cd14190  10 EVLGGGKFGKVHTCTEKRTGLKLAAKVINK-----QNSKDkemVLLEIQVMNQLNHRNLIQLYEAIE--TP----NEIVL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 136 VLDLMESD--LHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSN-LLVNENCEL-KIGDFGMARGLctSP 211
Cdd:cd14190  79 FMEYVEGGelFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENiLCVNRTGHQvKIIDFGLARRY--NP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 212 AEHqyfMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGA 291
Cdd:cd14190 157 REK---LKVNFGTPEFLSPEV-VNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEETFEHVSD 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 292 ErvrayiqslpprqpvpwetvypgadrqALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14190 233 E---------------------------AKDFVSNLIIKERSARMSATQCLKHPWL 261
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
61-347 2.51e-16

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: 79.58  E-value: 2.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPnafdVVTNAKR--TLRELKILKHFKHDNIIAIKDilrptvPYGEFKSVYVVLD 138
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFIK----CRKAKDRedVRNEIEIMNQLRHPRLLQLYD------AFETPREMVLVME 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 139 LMESD--LHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL-VNENC-ELKIGDFGMARGLCTSPAEH 214
Cdd:cd14103  71 YVAGGelFERVVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGnQIKIIDFGLARKYDPDKKLK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 215 QYFMT-EYVatrwyrAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMvlgtpspaviqavgaer 293
Cdd:cd14103 151 VLFGTpEFV------APEV-VNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTR----------------- 206
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 294 vrayiqslpprqpVPWETVYPGAD---RQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14103 207 -------------AKWDFDDEAFDdisDEAKDFISKLLVKDPRKRMSAAQCLQHPWL 250
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
50-249 2.61e-16

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: 80.42  E-value: 2.61e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  50 DVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnAFDVVTNAKRTLR-ELKILKHF-KHDNIIAIkdilrptvpY 127
Cdd:cd06639  19 DPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVK----ILDPISDVDEEIEaEYNILRSLpNHPNVVKF---------Y 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 128 GEF--------KSVYVVLDLME----SDLHQ-IIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENC 194
Cdd:cd06639  86 GMFykadqyvgGQLWLVLELCNggsvTELVKgLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 195 ELKIGDFGMARGLCTSPAEHQyfmtEYVATRWYRAPELMLSLHEYTQA----IDLWSVG 249
Cdd:cd06639 166 GVKLVDFGVSAQLTSARLRRN----TSVGTPFWMAPEVIACEQQYDYSydarCDVWSLG 220
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
53-372 2.78e-16

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: 80.74  E-value: 2.78e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNafDVV---TNAKRTLRELKILK-HFKHDNIiaikdilrpTVPYG 128
Cdd:cd05619   5 EDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKK--DVVlmdDDVECTMVEKRVLSlAWEHPFL---------THLFC 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA 204
Cdd:cd05619  74 TFQTKENLFFVMEylngGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMC 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RGLCTSPAEHQYFmteyVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMvlgtPSPa 284
Cdd:cd05619 154 KENMLGDAKTSTF----CGTPDYIAPEILLG-QKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRM----DNP- 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 285 viqavgaervrayiqsLPPRqpvpWetvypgADRQALSLLGRMLRFEPSARISAAAALR-HPFLAKYH---------DPD 354
Cdd:cd05619 224 ----------------FYPR----W------LEKEAKDILVKLFVREPERRLGVRGDIRqHPFFREINwealeereiEPP 277
                       330
                ....*....|....*....
gi 20986497 355 DEPDCAPPFDFA-FDREAL 372
Cdd:cd05619 278 FKPKVKSPFDCSnFDKEFL 296
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
53-350 3.07e-16

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: 80.11  E-value: 3.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfDVVTNAKRTLRELKI-LKHFKHDNIIAIkdilrptvpYGEF- 130
Cdd:cd06618  15 NDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRS-GNKEENKRILMDLDVvLKSHDCPYIVKC---------YGYFi 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 --KSVYVVLDLMESDLHQI-IHSSQPL---TLEHVRYFLYQLLRGLKYMHsaQVIHRDLKPSNLLVNENCELKIGDFGMA 204
Cdd:cd06618  85 tdSDVFICMELMSTCLDKLlKRIQGPIpedILGKMTVSIVKALHYLKEKH--GVIHRDVKPSNILLDESGNVKLCDFGIS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RGLCTSPAEhqyfmTEYVATRWYRAPE-LMLSLH-EYTQAIDLWSVGCIFGEmLARRQlFPGKNYVHQLQLIMMVLGTPS 282
Cdd:cd06618 163 GRLVDSKAK-----TRSAGCAAYMAPErIDPPDNpKYDIRADVWSLGISLVE-LATGQ-FPYRNCKTEFEVLTKILNEEP 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 283 PaviqavgaervrayiqSLPPRQpvpwetvypGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKY 350
Cdd:cd06618 236 P----------------SLPPNE---------GFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRY 278
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
61-346 3.25e-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: 79.74  E-value: 3.25e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKI---PNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPtvpYGEfKSVYVVL 137
Cdd:cd06651  15 LGQGAFGRVYLCYDVDTGRELAAKQVqfdPESPETSKEVSALECEIQLLKNLQHERIVQYYGCLRD---RAE-KTLTIFM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 138 DLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL---CTSPAE 213
Cdd:cd06651  91 EYMPGgSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLqtiCMSGTG 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 214 hqyfMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRqlfpgknyvhqlqlimmvlgtPSPAVIQAVGAer 293
Cdd:cd06651 171 ----IRSVTGTPYWMSPEV-ISGEGYGRKADVWSLGCTVVEMLTEK---------------------PPWAEYEAMAA-- 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 20986497 294 vRAYIQSLPPRQPVPWETvypgaDRQALSLLGRMLrFEPSARISAAAALRHPF 346
Cdd:cd06651 223 -IFKIATQPTNPQLPSHI-----SEHARDFLGCIF-VEARHRPSAEELLRHPF 268
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
61-281 3.45e-16

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: 80.10  E-value: 3.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVvTNAKRTLRELK-ILKHFKHDNIIAIkdilrptvpYGE-FKS--VYVV 136
Cdd:cd06616  14 IGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDE-KEQKRLLMDLDvVMRSSDCPYIVKF---------YGAlFREgdCWIC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 137 LDLMESDL---HQIIHSSQPLTL--EHVRYFLYQLLRGLKYMHSA-QVIHRDLKPSNLLVNENCELKIGDFGMARGLCTS 210
Cdd:cd06616  84 MELMDISLdkfYKYVYEVLDSVIpeEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGISGQLVDS 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 211 PAEhqyfmTEYVATRWYRAPELML---SLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQlQLIMMVLGTP 281
Cdd:cd06616 164 IAK-----TRDAGCRPYMAPERIDpsaSRDGYDVRSDVWSLGITLYEVATGKFPYPKWNSVFD-QLTQVVKGDP 231
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
61-258 3.70e-16

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: 79.07  E-value: 3.70e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAfdvvTNAKRTLRELKILKHFKHDNI-----IAIKDilrptvpygefKSVYV 135
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGKVMVMKELKRF----DEQRSFLKEVKLMRRLSHPNIlrfigVCVKD-----------NKLNF 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 136 VLDLMES-DLHQIIHS-SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV---NENCELKIGDFGMARGL--- 207
Cdd:cd14065  66 ITEYVNGgTLEELLKSmDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMpde 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 20986497 208 -CTSPAEHQYFMTeyVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLAR 258
Cdd:cd14065 146 kTKKPDRKKRLTV--VGSPYWMAPE-MLRGESYDEKVDVFSFGIVLCEIIGR 194
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
59-347 5.34e-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: 79.30  E-value: 5.34e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNakRTLRELKILKHFK-HDNIIAIKDIlrptvpYGEFKSVYVVL 137
Cdd:cd14173   8 EVLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRS--RVFREVEMLYQCQgHRNVLELIEF------FEEEDKFYLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 138 DLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV---NENCELKIGDFGMARGLC----T 209
Cdd:cd14173  80 EKMRGgSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCehpNQVSPVKICDFDLGSGIKlnsdC 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 210 SPAEHQYFMTEyVATRWYRAPELMLSLHE----YTQAIDLWSVGCIFGEMLARRQLFPGknyvHQLQLIMMVLGTPSPAV 285
Cdd:cd14173 160 SPISTPELLTP-CGSAEYMAPEVVEAFNEeasiYDKRCDLWSLGVILYIMLSGYPPFVG----RCGSDCGWDRGEACPAC 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497 286 iQAVGAERVRAYIQSLPPRQpvpWETVYPGADrqalSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14173 235 -QNMLFESIQEGKYEFPEKD---WAHISCAAK----DLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
59-347 6.76e-16

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: 78.42  E-value: 6.76e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQVAIKKI----PNAFDVVTNakrtlrELKILKHFKHDNIIAIkdilrptvpYGEFKS-- 132
Cdd:cd14193  10 EILGGGRFGQVHKCEEKSSGLKLAAKIIkarsQKEKEEVKN------EIEVMNQLNHANLIQL---------YDAFESrn 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 --VYVVLDLMESDL-HQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL-VN-ENCELKIGDFGMARGL 207
Cdd:cd14193  75 diVLVMEYVDGGELfDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILcVSrEANQVKIIDFGLARRY 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 ctSPAEHqyfMTEYVATRWYRAPELMlsLHEYTQ-AIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVI 286
Cdd:cd14193 155 --KPREK---LRVNFGTPEFLAPEVV--NYEFVSfPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEEF 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 287 QAVGAErvrayiqslpprqpvpwetvypgadrqALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14193 228 ADISEE---------------------------AKDFISKLLIKEKSWRMSASEALKHPWL 261
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
53-307 7.54e-16

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: 79.71  E-value: 7.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNaKRTLRELKILKHFKHDNIIAIkdilrptvpYGEFKS 132
Cdd:cd06649   5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIR-NQIIRELQVLHECNSPYIVGF---------YGAFYS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 ---VYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSA-QVIHRDLKPSNLLVNENCELKIGDFGMARGL 207
Cdd:cd06649  75 dgeISICMEHMDGgSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 CTSPAehqyfmTEYVATRWYRAPELMLSLHEYTQAiDLWSVGCIFGEMLARRQLFPGKNyVHQLQLImmvLGTPspaVIQ 287
Cdd:cd06649 155 IDSMA------NSFVGTRSYMSPERLQGTHYSVQS-DIWSMGLSLVELAIGRYPIPPPD-AKELEAI---FGRP---VVD 220
                       250       260
                ....*....|....*....|
gi 20986497 288 AVGAERVRAYIQSLPPRQPV 307
Cdd:cd06649 221 GEEGEPHSISPRPRPPGRPV 240
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
53-346 8.21e-16

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: 78.61  E-value: 8.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEII-ETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfdvVTNAK-RTLRELKILKHFK-HDNIIAIkdilrptVPYGE 129
Cdd:cd14090   1 DLYKLTgELLGEGAYASVQTCINLYTGKEYAVKIIEKH---PGHSRsRVFREVETLHQCQgHPNILQL-------IEYFE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSV-YVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL---VNENCELKIGDFGMA 204
Cdd:cd14090  71 DDERfYLVFEKMRGgPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILcesMDKVSPVKICDFDLG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RGL-----CTSPAEHQYFMTEyVATRWYRAPELMLSL----HEYTQAIDLWSVGCIFGEMLARRQLFPGKnyvhqlqlim 275
Cdd:cd14090 151 SGIklsstSMTPVTTPELLTP-VGSAEYMAPEVVDAFvgeaLSYDKRCDLWSLGVILYIMLCGYPPFYGR---------- 219
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 276 mvLGT-------PSPAVIQAVGAERVRAYIQSLPPRQpvpWETVypgaDRQALSLLGRMLRFEPSARISAAAALRHPF 346
Cdd:cd14090 220 --CGEdcgwdrgEACQDCQELLFHSIQEGEYEFPEKE---WSHI----SAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
45-347 1.23e-15

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: 78.04  E-value: 1.23e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  45 FDVTFDVGDEyeiieTIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHD----NIIAIKDI 120
Cdd:cd14198   5 FNNFYILTSK-----ELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKSNprvvNLHEVYET 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 121 LRPTVPYGEFKSVYVVLDLMESDLHQIIHSSQPLTLehvryfLYQLLRGLKYMHSAQVIHRDLKPSNLL---VNENCELK 197
Cdd:cd14198  80 TSEIILILEYAAGGEIFNLCVPDLAEMVSENDIIRL------IRQILEGVYYLHQNNIVHLDLKPQNILlssIYPLGDIK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 198 IGDFGMARGLctspaEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIfgemlarrqlfpgknyvhqlqlIMMV 277
Cdd:cd14198 154 IVDFGMSRKI-----GHACELREIMGTPEYLAPEI-LNYDPITTATDMWNIGVI----------------------AYML 205
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 278 LGTPSPaviqAVGAERVRAYIQSLPPRQPVPWETvYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14198 206 LTHESP----FVGEDNQETFLNISQVNVDYSEET-FSSVSQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
59-375 1.29e-15

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: 78.83  E-value: 1.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQVAIKKIPNafDVV---TNAKRTLRELKILKHFKHDNIIaikdilrpTVPYGEFKS--- 132
Cdd:cd05620   1 KVLGKGSFGKVLLAELKGKGEYFAVKALKK--DVVlidDDVECTMVEKRVLALAWENPFL--------THLYCTFQTkeh 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMarglCTSP 211
Cdd:cd05620  71 LFFVMEFLNGgDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGM----CKEN 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 212 AEHQYFMTEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMvlGTPSpaviqavga 291
Cdd:cd05620 147 VFGDNRASTFCGTPDYIAPEILQGL-KYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRV--DTPH--------- 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 292 ervraYiqslpPRqpvpWETvypgadRQALSLLGRMLRFEPSARISAAAALR-HPFLAKYH---------DPDDEPDCAP 361
Cdd:cd05620 215 -----Y-----PR----WIT------KESKDILEKLFERDPTRRLGVVGNIRgHPFFKTINwtalekrelDPPFKPKVKS 274
                       330
                ....*....|....*
gi 20986497 362 PFDFA-FDREALTRE 375
Cdd:cd05620 275 PSDYSnFDREFLSEK 289
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
61-252 1.34e-15

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


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 78.69  E-value: 1.34e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKkIPNAFDVVTNAKRTLRELKILKHFKHDNII---AIKDIL--RPTVPYGEF---KS 132
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVK-VFNNLSFMRPLDVQMREFEVLKKLNHKNIVklfAIEEELttRHKVLVMELcpcGS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLD-------LMESDLHqiihssqpLTLEHVryflyqlLRGLKYMHSAQVIHRDLKPSNLL--VNEN--CELKIGDF 201
Cdd:cd13988  80 LYTVLEepsnaygLPESEFL--------IVLRDV-------VAGMNHLRENGIVHRDIKPGNIMrvIGEDgqSVYKLTDF 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 202 GMARGLctspAEHQYFMTEYvATRWYRAPEL----MLSLH---EYTQAIDLWSVGCIF 252
Cdd:cd13988 145 GAAREL----EDDEQFVSLY-GTEEYLHPDMyeraVLRKDhqkKYGATVDLWSIGVTF 197
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
54-251 1.49e-15

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 77.33  E-value: 1.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEII-ETIGNGAYGVVSSARRRLTGQQVAIKkipnafdVVTNAKRTLRELKIlkHFK---HDNIIAIKDILRPTvpYGE 129
Cdd:cd14089   1 DYTISkQVLGLGINGKVLECFHKKTGEKFALK-------VLRDNPKARREVEL--HWRasgCPHIVRIIDVYENT--YQG 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDLMES-DLHQII--HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNE---NCELKIGDFGM 203
Cdd:cd14089  70 RKCLLVVMECMEGgELFSRIqeRADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSkgpNAILKLTDFGF 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 20986497 204 AR-----GLCTSPaehQYfmteyvaTRWYRAPELmLSLHEYTQAIDLWSVGCI 251
Cdd:cd14089 150 AKetttkKSLQTP---CY-------TPYYVAPEV-LGPEKYDKSCDMWSLGVI 191
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
61-256 1.62e-15

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: 77.55  E-value: 1.62e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPnafdvvtnakrtlrelkiLKHFKHDNIIAIKDILRPTVP--YGEFKS---VYV 135
Cdd:cd13991  14 IGRGSFGEVHRMEDKQTGFQCAVKKVR------------------LEVFRAEELMACAGLTSPRVVplYGAVREgpwVNI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 136 VLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENC-ELKIGDFGMARGLCTSPAE 213
Cdd:cd13991  76 FMDLKEGgSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHAECLDPDGLG 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 20986497 214 HQYFMTEYV-ATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEML 256
Cdd:cd13991 156 KSLFTGDYIpGTETHMAPEVVLG-KPCDAKVDVWSSCCMMLHML 198
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
55-262 1.79e-15

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: 77.17  E-value: 1.79e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfdvVTNAKRTLRELKILKHFKHDNIIAIKDI-LRPTvpygefksv 133
Cdd:cd14111   5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQ---AEEKQGVLQEYEILKSLHHERIMALHEAyITPR--------- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMESDLHQIIHSsqplTLEHVRY-------FLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARG 206
Cdd:cd14111  73 YLVLIAEFCSGKELLHS----LIDRFRYseddvvgYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQS 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 207 ---LCTSPAEHqyfmteYVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLARRQLF 262
Cdd:cd14111 149 fnpLSLRQLGR------RTGTLEYMAPE-MVKGEPVGPPADIWSIGVLTYIMLSGRSPF 200
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
61-256 1.79e-15

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: 78.47  E-value: 1.79e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKkipnafdvvtnakrTLRELKILKHFKHDNIIAIKDILRPTVPYG-------EFKS- 132
Cdd:cd05603   3 IGKGSFGKVLLAKRKCDGKFYAVK--------------VLQKKTILKKKEQNHIMAERNVLLKNLKHPflvglhySFQTs 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 --VYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFgmarGLCT 209
Cdd:cd05603  69 ekLYFVLDYVNGgELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDF----GLCK 144
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 20986497 210 SPAEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd05603 145 EGMEPEETTSTFCGTPEYLAPEV-LRKEPYDRTVDWWCLGAVLYEML 190
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
59-306 1.80e-15

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: 76.97  E-value: 1.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRlTGQQVAIKK----IPNAFDVvtnakRTLRELKILKHFKHDNIIAIKDILRPTVPygefksVY 134
Cdd:cd05085   2 ELLGKGNFGEVYKGTLK-DKTPVAVKTckedLPQELKI-----KFLSEARILKQYDHPNIVKLIGVCTQRQP------IY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMESD--LHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR----GLC 208
Cdd:cd05085  70 IVMELVPGGdfLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRqeddGVY 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAEHQyfmteyVATRWyRAPElMLSLHEYTQAIDLWSVGCIFGEMLArrqlfpgknyvhqlqlimmvLGT-PSPAVIQ 287
Cdd:cd05085 150 SSSGLKQ------IPIKW-TAPE-ALNYGRYSSESDVWSFGILLWETFS--------------------LGVcPYPGMTN 201
                       250       260
                ....*....|....*....|
gi 20986497 288 AVGAERV-RAYIQSLPPRQP 306
Cdd:cd05085 202 QQAREQVeKGYRMSAPQRCP 221
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
58-364 2.79e-15

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: 77.70  E-value: 2.79e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  58 IETIGNGAYGVVSSARRRLTGQQVAIKKIPNafDVVTNAKRTLRELK----ILKHFKHDNIIAIKDILRPTvpygefKSV 133
Cdd:cd05604   1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQK--KVILNRKEQKHIMAernvLLKNVKHPFLVGLHYSFQTT------DKL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFgmarGLCTSPA 212
Cdd:cd05604  73 YFVLDFVNGgELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDF----GLCKEGI 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 213 EHQYFMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMmvlgtpspaviqavgae 292
Cdd:cd05604 149 SNSDTTTTFCGTPEYLAPEVIRK-QPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENIL----------------- 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 293 rvrayiqslppRQPVpweTVYPGADRQALSLLGRMLRFEPSARISAAAALR----HPFLAKYHDPD-DEPDCAPPFD 364
Cdd:cd05604 211 -----------HKPL---VLRPGISLTAWSILEELLEKDRQLRLGAKEDFLeiknHPFFESINWTDlVQKKIPPPFN 273
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
53-271 2.94e-15

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 80.17  E-value: 2.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497    53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPygefKS 132
Cdd:PTZ00266   13 NEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFLNKAN----QK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   133 VYVVLDLMES-DLHQIIHSSQPL---TLEH-VRYFLYQLLRGLKYMHS-------AQVIHRDLKPSNLLVNENCE----- 195
Cdd:PTZ00266   89 LYILMEFCDAgDLSRNIQKCYKMfgkIEEHaIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTGIRhigki 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   196 ------------LKIGDFGMARGLCTSPAEHQyfmteYVATRWYRAPELMlsLHE---YTQAIDLWSVGCIFGEMLARRQ 260
Cdd:PTZ00266  169 taqannlngrpiAKIGDFGLSKNIGIESMAHS-----CVGTPYYWSPELL--LHEtksYDDKSDMWALGCIIYELCSGKT 241
                         250
                  ....*....|.
gi 20986497   261 LFPGKNYVHQL 271
Cdd:PTZ00266  242 PFHKANNFSQL 252
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
51-347 3.08e-15

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: 76.40  E-value: 3.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  51 VGDEYEIIE-TIGNGAYGVVSSARRRLTGQQVAIKKIPNAfdvvtnaKRTLRELKILKHFKHDNIIAIKDILRPtvpygE 129
Cdd:cd14109   1 VRELYEIGEeDEKRAAQGAPFHVTERSTGRNFLAQLRYGD-------PFLMREVDIHNSLDHPNIVQMHDAYDD-----E 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDL---MESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENcELKIGDFGMARG 206
Cdd:cd14109  69 KLAVTVIDNLastIELVRDNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD-KLKLADFGQSRR 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 207 LCTSP-AEHQYFMTEYVatrwyrAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMmvlgtpsPAV 285
Cdd:cd14109 148 LLRGKlTTLIYGSPEFV------SPEIVNS-YPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVR-------SGK 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 286 IQAVGAervrayiqslpprqpvPWETV-YPGADrqalsLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14109 214 WSFDSS----------------PLGNIsDDARD-----FIKKLLVYIPESRLTVDEALNHPWF 255
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
55-347 3.14e-15

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: 76.50  E-value: 3.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDvvtNAKRTLRELKILKHFKHDNIIAIKD-ILRPTvpygefksv 133
Cdd:cd14110   5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPE---DKQLVLREYQVLRRLSHPRIAQLHSaYLSPR--------- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMESDLHQIIHSSQPLTL---EHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLcts 210
Cdd:cd14110  73 HLVLIEELCSGPELLYNLAERNSyseAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPF--- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 211 pAEHQYFMTE----YVATrwyRAPELMLSLHEYTQAiDLWSVGCifgemlarrqlfpgknyvhqLQLIMMVLGTPspaVI 286
Cdd:cd14110 150 -NQGKVLMTDkkgdYVET---MAPELLEGQGAGPQT-DIWAIGV--------------------TAFIMLSADYP---VS 201
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 287 QAVGAERVRAYIQSLpprqpVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14110 202 SDLNWERDRNIRKGK-----VQLSRCYAGLSGGAVNFLKSTLCAKPWGRPTASECLQNPWL 257
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
53-285 3.23e-15

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: 77.07  E-value: 3.23e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSA------RRRLTGQQVAIKKIP-NAFDvvTNAKRTLRELKILKHF-KHDNIIAI------- 117
Cdd:cd05053  12 DRLTLGKPLGEGAFGQVVKAeavgldNKPNEVVTVAVKMLKdDATE--KDLSDLVSEMEMMKMIgKHKNIINLlgactqd 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 118 ---------------KDILRPTVPYGEFKSvyvvldlmesdLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRD 182
Cdd:cd05053  90 gplyvvveyaskgnlREFLRARRPPGEEAS-----------PDDPRVPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 183 LKPSNLLVNENCELKIGDFGMARGLctspaEHQYFMTEYVATR----WYrAPELMLSlHEYTQAIDLWSVGCIFGEmlar 258
Cdd:cd05053 159 LAARNVLVTEDNVMKIADFGLARDI-----HHIDYYRKTTNGRlpvkWM-APEALFD-RVYTHQSDVWSFGVLLWE---- 227
                       250       260
                ....*....|....*....|....*..
gi 20986497 259 rqlfpgknyvhqlqlIMMVLGTPSPAV 285
Cdd:cd05053 228 ---------------IFTLGGSPYPGI 239
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
59-258 3.47e-15

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: 76.36  E-value: 3.47e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQ---VAIKKIpNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPtvPYGefkSVYV 135
Cdd:cd05058   1 EVIGKGHFGCVYHGTLIDSDGQkihCAVKSL-NRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLP--SEG---SPLV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 136 VLDLME-SDLHQIIHSSQ--PlTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLctspa 212
Cdd:cd05058  75 VLPYMKhGDLRNFIRSEThnP-TVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDI----- 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 20986497 213 ehqyFMTEYVATRWYRAPEL--------MLSLHEYTQAIDLWSVGCIFGEMLAR 258
Cdd:cd05058 149 ----YDKEYYSVHNHTGAKLpvkwmaleSLQTQKFTTKSDVWSFGVLLWELMTR 198
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
58-258 3.66e-15

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: 76.86  E-value: 3.66e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  58 IETIGNGAYGVVSSAR----RRLTGQQVAIKKIpNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTvpyGEfKSV 133
Cdd:cd05080   9 IRDLGEGHFGKVSLYCydptNDGTGEMVAVKAL-KADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQ---GG-KSL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLctsPAE 213
Cdd:cd05080  84 QLIMEYVPLGSLRDYLPKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAV---PEG 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 20986497 214 HQYFMTEYVATR---WYrAPELmLSLHEYTQAIDLWSVGCIFGEMLAR 258
Cdd:cd05080 161 HEYYRVREDGDSpvfWY-APEC-LKEYKFYYASDVWSFGVTLYELLTH 206
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
61-274 3.83e-15

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


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 76.30  E-value: 3.83e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVV--SSARRRL---TG-QQVAIKKI-PNAFDvvTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPygefksV 133
Cdd:cd05044   3 LGSGAFGEVfeGTAKDILgdgSGeTKVAVKTLrKGATD--QEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDP------Q 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLL-------RGLKYMHSAQVIHRDLKPSNLLVNEN----CELKIGDF 201
Cdd:cd05044  75 YIILELMEGgDLLSYLRAARPTAFTPPLLTLKDLLsicvdvaKGCVYLEDMHFVHRDLAARNCLVSSKdyreRVVKIGDF 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 202 GMARGLctspAEHQYFMTE---YVATRWYrAPE-LMLSLheYTQAIDLWSVGCIFGEMLAR-RQLFPGKNYVHQLQLI 274
Cdd:cd05044 155 GLARDI----YKNDYYRKEgegLLPVRWM-APEsLVDGV--FTTQSDVWAFGVLMWEILTLgQQPYPARNNLEVLHFV 225
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
55-337 4.95e-15

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: 76.18  E-value: 4.95e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKI--PNAFDVvtnaKRTLRELKILKHFKHDNIIAIKD--ILRPTvpyGEF 130
Cdd:cd13986   2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKIlcHSKEDV----KEAMREIENYRLFNHPNILRLLDsqIVKEA---GGK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVL---------DLME--SDLHQIIHSSQPLTLEHvryflyQLLRGLKYMHSAQ---VIHRDLKPSNLLVNENCEL 196
Cdd:cd13986  75 KEVYLLLpyykrgslqDEIErrLVKGTFFPEDRILHIFL------GICRGLKAMHEPElvpYAHRDIKPGNVLLSEDDEP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 197 KIGDFG-MARGLCTSPAEHQYFMTEYVA----TRWYRAPELmlsLHEYTQAI-----DLWSVGCIFgemlarrqlfpgkn 266
Cdd:cd13986 149 ILMDLGsMNPARIEIEGRREALALQDWAaehcTMPYRAPEL---FDVKSHCTidektDIWSLGCTL-------------- 211
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 267 YVhqlqliMMVLGTPSPAVIQAVGAerVRAYIQSlpPRQPVPWETVYPgadRQALSLLGRMLRFEPSARIS 337
Cdd:cd13986 212 YA------LMYGESPFERIFQKGDS--LALAVLS--GNYSFPDNSRYS---EELHQLVKSMLVVNPAERPS 269
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
59-264 5.10e-15

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 76.20  E-value: 5.10e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQ--QVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFKSVYVV 136
Cdd:cd05075   6 KTLGEGEFGSVMEGQLNQDDSvlKVAVKTMKIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQNTESEGYPSPVVI 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 137 LDLME-SDLHQIIHSS----QPLTL--EHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCT 209
Cdd:cd05075  86 LPFMKhGDLHSFLLYSrlgdCPVYLptQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKIYN 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 210 SPAEHQYFMTEyVATRWYRAPELMLSLheYTQAIDLWSVGCIFGEMLARRQL-FPG 264
Cdd:cd05075 166 GDYYRQGRISK-MPVKWIAIESLADRV--YTTKSDVWSFGVTMWEIATRGQTpYPG 218
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
53-256 5.12e-15

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: 76.23  E-value: 5.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVV--SSARRRLTGQ---QVAIKKIpnaFDVVTNAKRT--LRELKILKHFKHDNIIAIKDILRPTV 125
Cdd:cd05032   6 EKITLIRELGQGSFGMVyeGLAKGVVKGEpetRVAIKTV---NENASMRERIefLNEASVMKEFNCHHVVRLLGVVSTGQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 PygefksVYVVLDLM-ESDLHQIIHSSQP----------LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENC 194
Cdd:cd05032  83 P------TLVVMELMaKGDLKSYLRSRRPeaennpglgpPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDL 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 195 ELKIGDFGMARGLctspAEHQYFMTE---YVATRWYrAPElmlSLHE--YTQAIDLWSVGCIFGEML 256
Cdd:cd05032 157 TVKIGDFGMTRDI----YETDYYRKGgkgLLPVRWM-APE---SLKDgvFTTKSDVWSFGVVLWEMA 215
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
55-267 5.84e-15

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: 76.10  E-value: 5.84e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIiETIGNGAYGVVSSARRRLTGQQVAIKKIPNA-FDVVTNAKRTLRELKILKHFKHDNIIAIkdilrpTVPYGEFKSV 133
Cdd:cd05607   5 YEF-RVLGKGGFGEVCAVQVKNTGQMYACKKLDKKrLKKKSGEKMALLEKEILEKVNSPFIVSL------AYAFETKTHL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMES-DL-HQIIHSSQP-LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTS 210
Cdd:cd05607  78 CLVMSLMNGgDLkYHIYNVGERgIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEG 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 211 PAehqyfMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQlfPGKNY 267
Cdd:cd05607 158 KP-----ITQRAGTNGYMAPEI-LKEESYSYPVDWFAMGCSIYEMVAGRT--PFRDH 206
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
61-363 6.76e-15

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: 76.63  E-value: 6.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIK----KIPNAFDVVTNakrTLRELKILKHFKHDNIIAIKdilrptvpYgEFKSVYVV 136
Cdd:cd05571   3 LGKGTFGKVILCREKATGELYAIKilkkEVIIAKDEVAH---TLTENRVLQNTRHPFLTSLK--------Y-SFQTNDRL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 137 LDLME----SDLhqIIHSSQP--LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFgmarGLCTS 210
Cdd:cd05571  71 CFVMEyvngGEL--FFHLSRErvFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDF----GLCKE 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 211 PAEHQYFMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMvlgtpspaviqavg 290
Cdd:cd05571 145 EISYGATTKTFCGTPEYLAPEVLED-NDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILM-------------- 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 291 aERVRayiqsLPPRqpvpwetvypgADRQALSLLGRMLRFEPSARI-----SAAAALRHPFLAKYhDPDD--EPDCAPPF 363
Cdd:cd05571 210 -EEVR-----FPST-----------LSPEAKSLLAGLLKKDPKKRLgggprDAKEIMEHPFFASI-NWDDlyQKKIPPPF 271
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
62-264 8.13e-15

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: 74.99  E-value: 8.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  62 GNGAYGVVSSARRRLTGQQVAIKKIpNAFDvvtnakrtlRELKILKHFKHDNIIAIKDILRPTVPYG---EFKSVYVVLD 138
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVKKL-LKIE---------KEAEILSVLSHRNIIQFYGAILEAPNYGivtEYASYGSLFD 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 139 LMESDlhqiihSSQPLTLEHVRYFLYQLLRGLKYMHS---AQVIHRDLKPSNLLVNENCELKIGDFGMARGLctspaEHQ 215
Cdd:cd14060  72 YLNSN------ESEEMDMDQIMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVIAADGVLKICDFGASRFH-----SHT 140
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 20986497 216 YFMTeYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPG 264
Cdd:cd14060 141 THMS-LVGTFPWMAPEVIQSL-PVSETCDTYSYGVVLWEMLTREVPFKG 187
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
61-378 8.17e-15

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: 76.10  E-value: 8.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFdVVTN--AKRTLRELKIL-KHFKHDNIIAIkdilrptvpYGEFKS---VY 134
Cdd:cd05570   3 LGKGSFGKVMLAERKKTDELYAIKVLKKEV-IIEDddVECTMTEKRVLaLANRHPFLTGL---------HACFQTedrLY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVL------DLMesdLHqiIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR-GL 207
Cdd:cd05570  73 FVMeyvnggDLM---FH--IQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKeGI 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 CtspaeHQYFMTEYVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhqlqlimmvlgtpspaviq 287
Cdd:cd05570 148 W-----GGNTTSTFCGTPDYIAPE-ILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDD--------------------- 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 288 avgAERVRAYIQSLPPRQPVpwetvypGADRQALSLLGRMLRFEPSARI----SAAAALR-HPFLaKYHDPDDEPDC--A 360
Cdd:cd05570 201 ---EDELFEAILNDEVLYPR-------WLSREAVSILKGLLTKDPARRLgcgpKGEADIKaHPFF-RNIDWDKLEKKevE 269
                       330       340
                ....*....|....*....|....*..
gi 20986497 361 PPF--------DFA-FDREaLTRERIK 378
Cdd:cd05570 270 PPFkpkvksprDTSnFDPE-FTSESPR 295
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
61-262 1.01e-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: 75.69  E-value: 1.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIpnafdvvtNAKR---------TLRELKILKHFKHDNIIAIkdilrpTVPYGEFK 131
Cdd:cd05608   9 LGKGGFGEVSACQMRATGKLYACKKL--------NKKRlkkrkgyegAMVEKRILAKVHSRFIVSL------AYAFQTKT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMES-DLHQIIHS---SQPLTLEH-VRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARG 206
Cdd:cd05608  75 DLCLVMTIMNGgDLRYHIYNvdeENPGFQEPrACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVE 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 207 LctspAEHQYFMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLF 262
Cdd:cd05608 155 L----KDGQTKTKGYAGTPGFMAPELLLG-EEYDYSVDYFTLGVTLYEMIAARGPF 205
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
97-262 1.08e-14

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: 75.05  E-value: 1.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  97 KRTLRELKILKHFKHDNIIAIKDILrpTVPYGEFKSVyvvldlME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKY 172
Cdd:cd13990  49 KHALREYEIHKSLDHPRIVKLYDVF--EIDTDSFCTV------LEycdgNDLDFYLKQHKSIPEREARSIIMQVVSALKY 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 173 M--HSAQVIHRDLKPSNLLVNENC---ELKIGDFGMARglcTSPAEHQY-----FMTEYVATRWYRAPELMLSLHEY--- 239
Cdd:cd13990 121 LneIKPPIIHYDLKPGNILLHSGNvsgEIKITDFGLSK---IMDDESYNsdgmeLTSQGAGTYWYLPPECFVVGKTPpki 197
                       170       180
                ....*....|....*....|...
gi 20986497 240 TQAIDLWSVGCIFGEMLARRQLF 262
Cdd:cd13990 198 SSKVDVWSVGVIFYQMLYGRKPF 220
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
54-256 1.08e-14

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


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 76.21  E-value: 1.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnafdvvtnAKRTLRELKILKHFKHDNIIAIKDILRPTV-----PYG 128
Cdd:cd05602   8 DFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVL---------QKKAILKKKEEKHIMSERNVLLKNVKHPFLvglhfSFQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFgmarGL 207
Cdd:cd05602  79 TTDKLYFVLDYINGgELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDF----GL 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 20986497 208 CTSPAEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd05602 155 CKENIEPNGTTSTFCGTPEYLAPEV-LHKQPYDRTVDWWCLGAVLYEML 202
pknD PRK13184
serine/threonine-protein kinase PknD;
55-266 1.14e-14

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 78.27  E-value: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNafDVVTNA---KRTLRELKILKHFKHDNIIAI------KDILRPTV 125
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIRE--DLSENPllkKRFLREAKIAADLIHPGIVPVysicsdGDPVYYTM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  126 PYGE-------FKSVYVVlDLMESDLHqiIHSSQPLTLehvRYFlYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKI 198
Cdd:PRK13184  82 PYIEgytlkslLKSVWQK-ESLSKELA--EKTSVGAFL---SIF-HKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  199 GDFGMA-----------------RGLCTSPaehqyfMT---EYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLAR 258
Cdd:PRK13184 155 LDWGAAifkkleeedlldidvdeRNICYSS------MTipgKIVGTPDYMAPERLLG-VPASESTDIYALGVILYQMLTL 227

                 ....*...
gi 20986497  259 RqlFPGKN 266
Cdd:PRK13184 228 S--FPYRR 233
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
53-263 1.25e-14

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: 75.86  E-value: 1.25e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNaKRTLRELKILKHFKHDNIIAIkdilrptvpYGEFKS 132
Cdd:cd06650   5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIR-NQIIRELQVLHECNSPYIVGF---------YGAFYS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 ---VYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSA-QVIHRDLKPSNLLVNENCELKIGDFGMARGL 207
Cdd:cd06650  75 dgeISICMEHMDGgSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQL 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 208 CTSPAehqyfmTEYVATRWYRAPELMLSLHEYTQAiDLWSVGCIFGEMLARRQLFP 263
Cdd:cd06650 155 IDSMA------NSFVGTRSYMSPERLQGTHYSVQS-DIWSMGLSLVEMAVGRYPIP 203
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
81-260 1.29e-14

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


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 75.45  E-value: 1.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  81 VAIKKIPNafDVVTNAKRT-LRELKILKHFKHDNIIAIKDILRPTVPYgefksvYVVLDLMES-DLHQIIHS-------- 150
Cdd:cd05051  49 VAVKMLRP--DASKNAREDfLKEVKIMSQLKDPNIVRLLGVCTRDEPL------CMIVEYMENgDLNQFLQKheaetqga 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 151 ----SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSpaehQYFMTEYVAT-- 224
Cdd:cd05051 121 satnSKTLSYGTLLYMATQIASGMKYLESLNFVHRDLATRNCLVGPNYTIKIADFGMSRNLYSG----DYYRIEGRAVlp 196
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 20986497 225 -RWYrAPELMLsLHEYTQAIDLWSVGCIFGE--MLARRQ 260
Cdd:cd05051 197 iRWM-AWESIL-LGKFTTKSDVWAFGVTLWEilTLCKEQ 233
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
61-260 1.33e-14

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: 75.25  E-value: 1.33e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTgqQVAIKKIPN----AFDVVTNAKRTlrELKILKHFKHDNIIaikDILRPTVPYGEFKSVYVV 136
Cdd:cd14159   1 IGEGGFGCVYQAVMRNT--EYAVKRLKEdselDWSVVKNSFLT--EVEKLSRFRHPNIV---DLAGYSAQQGNYCLIYVY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 137 L--DLMESDLHQIIhSSQPLTLEHVRYFLYQLLRGLKYMHSAQ--VIHRDLKPSNLLVNENCELKIGDFGMARgLCTSPA 212
Cdd:cd14159  74 LpnGSLEDRLHCQV-SCPCLSWSQRLHVLLGTARAIQYLHSDSpsLIHGDVKSSNILLDAALNPKLGDFGLAR-FSRRPK 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 20986497 213 ehQYFMTEYVA-TRWYRA-----PELMLSLHEYTQAIDLWSVGCIFGEMLARRQ 260
Cdd:cd14159 152 --QPGMSSTLArTQTVRGtlaylPEEYVKTGTLSVEIDVYSFGVVLLELLTGRR 203
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
61-251 1.39e-14

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: 74.85  E-value: 1.39e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDvvTNAKRTLRELKILKHFK-HDNIIAI---KDILRPTVPYGEFKsvYVV 136
Cdd:cd14036   8 IAEGGFAFVYEAQDVGTGKEYALKRLLSNEE--EKNKAIIQEINFMKKLSgHPNIVQFcsaASIGKEESDQGQAE--YLL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 137 L-DLMES---DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQ--VIHRDLKPSNLLVNENCELKIGDFGMARGLCTS 210
Cdd:cd14036  84 LtELCKGqlvDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTEAHY 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 20986497 211 P----AEHQYFMTE----YVATRWYRAPEL--MLSLHEYTQAIDLWSVGCI 251
Cdd:cd14036 164 PdyswSAQKRSLVEdeitRNTTPMYRTPEMidLYSNYPIGEKQDIWALGCI 214
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
61-256 1.51e-14

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: 74.25  E-value: 1.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRltGQQVAIKKI---PNAfDVVTNAKRTLRELKILKHFKHDNIIAIKDI-LRP-----TVPYGEFK 131
Cdd:cd14148   2 IGVGGFGKVYKGLWR--GEEVAVKAArqdPDE-DIAVTAENVRQEARLFWMLQHPNIIALRGVcLNPphlclVMEYARGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQIIHssqpltlehvryFLYQLLRGLKYMHS---AQVIHRDLKPSNLLVNE--------NCELKIGD 200
Cdd:cd14148  79 ALNRALAGKKVPPHVLVN------------WAVQIARGMNYLHNeaiVPIIHRDLKSSNILILEpienddlsGKTLKITD 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 201 FGMARglctspAEHQYFMTEYVATRWYRAPELM-LSLheYTQAIDLWSVGCIFGEML 256
Cdd:cd14148 147 FGLAR------EWHKTTKMSAAGTYAWMAPEVIrLSL--FSKSSDVWSFGVLLWELL 195
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
60-256 1.59e-14

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: 75.43  E-value: 1.59e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  60 TIGNGAYGVVSSARRRLTGQQVAIKkipnafdvvtnakrTLRELKILKHFKHDNIIAIKDILRPTV--PY-----GEFKS 132
Cdd:cd05575   2 VIGKGSFGKVLLARHKAEGKLYAVK--------------VLQKKAILKRNEVKHIMAERNVLLKNVkhPFlvglhYSFQT 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 V---YVVLDLM---ESDLHqiihssqpltLEHVRYFLYQLLR--------GLKYMHSAQVIHRDLKPSNLLVNENCELKI 198
Cdd:cd05575  68 KdklYFVLDYVnggELFFH----------LQRERHFPEPRARfyaaeiasALGYLHSLNIIYRDLKPENILLDSQGHVVL 137
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 199 GDFgmarGLCTSPAEHQYFMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEML 256
Cdd:cd05575 138 TDF----GLCKEGIEPSDTTSTFCGTPEYLAPEVLRK-QPYDRTVDWWCLGAVLYEML 190
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
51-347 1.66e-14

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: 75.84  E-value: 1.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  51 VGD----EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAkrtLRELKILKHFKHDN--------IIAIK 118
Cdd:cd14216   4 IGDlfngRYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSAEHYTETA---LDEIKLLKSVRNSDpndpnremVVQLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 119 DILRPTVPYGefKSVYVVLDLMESDLHQ-IIHSS-QPLTLEHVRYFLYQLLRGLKYMHS-AQVIHRDLKPSNLLVN---- 191
Cdd:cd14216  81 DDFKISGVNG--THICMVFEVLGHHLLKwIIKSNyQGLPLPCVKKIIRQVLQGLDYLHTkCRIIHTDIKPENILLSvneq 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 192 --------------------------ENCELKIGDFGMArglCTSpaeHQYFmTEYVATRWYRAPELMLSlHEYTQAIDL 245
Cdd:cd14216 159 yirrlaaeatewqrnflvnplepknaEKLKVKIADLGNA---CWV---HKHF-TEDIQTRQYRSLEVLIG-SGYNTPADI 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 246 WSVGCIFGEMLARRQLF---PGKNYVH---QLQLIMMVLG-TPSPAVIQAVGAERVRAYIQSLPPRQPV-PW-------- 309
Cdd:cd14216 231 WSTACMAFELATGDYLFephSGEDYSRdedHIALIIELLGkVPRKLIVAGKYSKEFFTKKGDLKHITKLkPWglfevlve 310
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 20986497 310 ETVYPGADRQALS-LLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14216 311 KYEWSQEEAAGFTdFLLPMLELIPEKRATAAECLRHPWL 349
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
55-349 1.88e-14

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: 74.34  E-value: 1.88e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKI--PNAFDVVTNAKRtlrELKILKHFKHDNIiaikdilrpTVPYGEF-- 130
Cdd:cd06641   6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIdlEEAEDEIEDIQQ---EITVLSQCDSPYV---------TKYYGSYlk 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 -KSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCT 209
Cdd:cd06641  74 dTKLWIIMEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 210 SPAEHQYFmteyVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEmLARRQlfPGKNYVHQLQLIMMVLGTpSPAVIQAV 289
Cdd:cd06641 154 TQIKRN*F----VGTPFWMAPEV-IKQSAYDSKADIWSLGITAIE-LARGE--PPHSELHPMKVLFLIPKN-NPPTLEGN 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 290 GAERVRAYIQSLpprqpvpwetvypgadrqalsllgrmLRFEPSARISAAAALRHPFLAK 349
Cdd:cd06641 225 YSKPLKEFVEAC--------------------------LNKEPSFRPTAKELLKHKFILR 258
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
54-255 2.13e-14

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: 74.02  E-value: 2.13e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRltGQ-QVAIKKIPNAfdvVTNAKRTLRELKILKHFKHDNIIAIkdilrptvpYG---E 129
Cdd:cd05059   5 ELTFLKELGSGQFGVVHLGKWR--GKiDVAIKMIKEG---SMSEDDFIEEAKVMMKLSHPKLVQL---------YGvctK 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDLMESD--LHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL 207
Cdd:cd05059  71 QRPIFIVTEYMANGclLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYV 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 20986497 208 ctspAEHQYfmTEYVATRW---YRAPELmLSLHEYTQAIDLWSVGCIFGEM 255
Cdd:cd05059 151 ----LDDEY--TSSVGTKFpvkWSPPEV-FMYSKFSSKSDVWSFGVLMWEV 194
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
58-256 2.31e-14

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: 74.20  E-value: 2.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  58 IETIGNGAYGVVSSARRRL----TGQQVAIK--KIPNAFDVVTNAKRtlrELKILKHFKHDNIIAIKDILRPtvpyGEFK 131
Cdd:cd05079   9 IRDLGEGHFGKVELCRYDPegdnTGEQVAVKslKPESGGNHIADLKK---EIEILRNLYHENIVKYKGICTE----DGGN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMES-DLHQII-HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCT 209
Cdd:cd05079  82 GIKLIMEFLPSgSLKEYLpRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIET 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 210 SpaehqyfmTEYVATR--------WYrAPELMLSLHEYTqAIDLWSVGCIFGEML 256
Cdd:cd05079 162 D--------KEYYTVKddldspvfWY-APECLIQSKFYI-ASDVWSFGVTLYELL 206
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
54-277 3.12e-14

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: 73.51  E-value: 3.12e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVssARRRLTGQqVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDIL-RPT----VPYG 128
Cdd:cd14150   1 EVSMLKRIGTGSFGTV--FRGKWHGD-VAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMtRPNfaiiTQWC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMES--DLHQIIHSSQpltlehvryflyQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARg 206
Cdd:cd14150  78 EGSSLYRHLHVTETrfDTMQLIDVAR------------QTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLAT- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 207 lctspaehqyfmteyVATRW--------------YRAPEL--MLSLHEYTQAIDLWSVGCIFGEMLArrQLFPGKNYVHQ 270
Cdd:cd14150 145 ---------------VKTRWsgsqqveqpsgsilWMAPEVirMQDTNPYSFQSDVYAYGVVLYELMS--GTLPYSNINNR 207

                ....*..
gi 20986497 271 LQLIMMV 277
Cdd:cd14150 208 DQIIFMV 214
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
59-255 3.32e-14

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


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 73.53  E-value: 3.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVV------SSARRRLtgqQVAIK-------KIPNAFDvvtnakRTLRELKILKHFKHDNIIAIkdilrptv 125
Cdd:cd05040   1 EKLGDGSFGVVrrgewtTPSGKVI---QVAVKclksdvlSQPNAMD------DFLKEVNAMHSLDHPNLIRL-------- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 pYGefksvyVVLD---LMESDLHQI------IHSSQPLTLEHVRY-FLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE 195
Cdd:cd05040  64 -YG------VVLSsplMMVTELAPLgslldrLRKDQGHFLISTLCdYAVQIANGMAYLESKRFIHRDLAARNILLASKDK 136
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 196 LKIGDFGMARGLctsPAEHQYF-MTEY--VATRWYrAPELMLSLHeYTQAIDLWSVGCIFGEM 255
Cdd:cd05040 137 VKIGDFGLMRAL---PQNEDHYvMQEHrkVPFAWC-APESLKTRK-FSHASDVWMFGVTLWEM 194
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
61-263 3.67e-14

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 73.28  E-value: 3.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIK--KIPnafdvvTNAKRTLRELKILKHFKHDNIIAIKDIlrpTVPYGEFKSVYVVLD 138
Cdd:cd14155   1 IGSGFFSEVYKVRHRTSGQVMALKmnTLS------SNRANMLREVQLMNRLSHPNILRFMGV---CVHQGQLHALTEYIN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 139 lmESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV---NENCELKIGDFGMARGLCTSPAEHQ 215
Cdd:cd14155  72 --GGNLEQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrdENGYTAVVGDFGLAEKIPDYSDGKE 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 20986497 216 YFmtEYVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLARRQLFP 263
Cdd:cd14155 150 KL--AVVGSPYWMAPE-VLRGEPYNEKADVFSYGIILCEIIARIQADP 194
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
56-250 3.71e-14

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 73.47  E-value: 3.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  56 EIIETIGNGAYGVVSSARRRLTGQQVAIKKI--PNAFDVVTnAKRTLRELKILKhfKHDNIIAIKDILRPTVPYGEFKsV 133
Cdd:cd14037   6 TIEKYLAEGGFAHVYLVKTSNGGNRAALKRVyvNDEHDLNV-CKREIEIMKRLS--GHKNIVGYIDSSANRSGNGVYE-V 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YV---------VLDLMESDLHQIIHSSQPLTLehvryfLYQLLRGLKYMHSAQ--VIHRDLKPSNLLVNENCELKIGDFG 202
Cdd:cd14037  82 LLlmeyckgggVIDLMNQRLQTGLTESEILKI------FCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFG 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 203 MARGLCTSPAEHQYFMteYVA-------TRWYRAPElMLSLH---EYTQAIDLWSVGC 250
Cdd:cd14037 156 SATTKILPPQTKQGVT--YVEedikkytTLQYRAPE-MIDLYrgkPITEKSDIWALGC 210
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
59-256 4.41e-14

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: 73.87  E-value: 4.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVV----SSARRRLTGQQVAIKKIPNA----------FDVVTNAKRT-LRELKILKHFKHDNIIAIKDILRP 123
Cdd:cd05095  11 EKLGEGQFGEVhlceAEGMEKFMDKDFALEVSENQpvlvavkmlrADANKNARNDfLKEIKIMSRLKDPNIIRLLAVCIT 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 124 TVPygefksVYVVLDLMES-DLHQIIHSSQP------------LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV 190
Cdd:cd05095  91 DDP------LCMITEYMENgDLNQFLSRQQPegqlalpsnaltVSYSDLRFMAAQIASGMKYLSSLNFVHRDLATRNCLV 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 191 NENCELKIGDFGMARGLCTSpaehQYFMTEYVAT---RWYRAPELMLSlhEYTQAIDLWSVGCIFGEML 256
Cdd:cd05095 165 GKNYTIKIADFGMSRNLYSG----DYYRIQGRAVlpiRWMSWESILLG--KFTTASDVWAFGVTLWETL 227
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
53-256 4.78e-14

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: 74.33  E-value: 4.78e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKhfkhdNIIAIKD---ILRPTVPYGE 129
Cdd:cd05633   5 NDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIML-----SLVSTGDcpfIVCMTYAFHT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMArglC 208
Cdd:cd05633  80 PDKLCFILDLMNGgDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLA---C 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 20986497 209 TSPAEHQYfmtEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd05633 157 DFSKKKPH---ASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLL 201
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
51-347 4.85e-14

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: 73.10  E-value: 4.85e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  51 VGDEYEII-ETIGNGAYGVVSSARRRLTGQQVAIKkipnafdVVTNAKRTLRELKIlkHFKHD---NIIAIKDILRpTVP 126
Cdd:cd14172   1 VTDDYKLSkQVLGLGVNGKVLECFHRRTGQKCALK-------LLYDSPKARREVEH--HWRASggpHIVHILDVYE-NMH 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 YGEfKSVYVVLDLMES-DLHQIIHS--SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLV---NENCELKIGD 200
Cdd:cd14172  71 HGK-RCLLIIMECMEGgELFSRIQErgDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 201 FGMARGLCTSPAEHQYFMTEYvatrwYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFpgknYVHQLQLImmvlgt 280
Cdd:cd14172 150 FGFAKETTVQNALQTPCYTPY-----YVAPEV-LGPEKYDKSCDMWSLGVIMYILLCGFPPF----YSNTGQAI------ 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 281 pSPAViqavgAERVRAYIQSLPPRQpvpWETVypgaDRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14172 214 -SPGM-----KRRIRMGQYGFPNPE---WAEV----SEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
43-306 4.97e-14

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 75.29  E-value: 4.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   43 RSFDVTFDV--------GDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNI 114
Cdd:PTZ00283  14 RTFPDTFAKdeatakeqAKKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADKNRAQAEVCCLLNCDFFSI 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  115 IAIKDILRPTVPYGE--FKSVYVVLDLMES-DLHQIIHS----SQPLTlEHVRYFLY-QLLRGLKYMHSAQVIHRDLKPS 186
Cdd:PTZ00283  94 VKCHEDFAKKDPRNPenVLMIALVLDYANAgDLRQEIKSraktNRTFR-EHEAGLLFiQVLLAVHHVHSKHMIHRDIKSA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  187 NLLVNENCELKIGDFGMA------------RGLCTSPAehqyfmteYVATR-WYRAPelmlslheYTQAIDLWSVGCIFG 253
Cdd:PTZ00283 173 NILLCSNGLVKLGDFGFSkmyaatvsddvgRTFCGTPY--------YVAPEiWRRKP--------YSKKADMFSLGVLLY 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 20986497  254 EMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGAERVRAYIQSLPPRQP 306
Cdd:PTZ00283 237 ELLTLKRPFDGENMEEVMHKTLAGRYDPLPPSISPEMQEIVTALLSSDPKRRP 289
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
61-256 5.14e-14

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 72.68  E-value: 5.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRltGQQVAIKkipnAFDVVTNAKRTLRELKILKHFKHDNIIAIKDI-LRPTVPYGEFKSVYVVLDL 139
Cdd:cd14068   2 LGDGGFGSVYRAVYR--GEDVAVK----IFNKHTSFRLLRQELVVLSHLHHPSLVALLAAgTAPRMLVMELAPKGSLDAL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 140 MESDlhqiiHSSQPLTLEHvRYFLyQLLRGLKYMHSAQVIHRDLKPSNLL---VNENCEL--KIGDFGMARGLCtspaeh 214
Cdd:cd14068  76 LQQD-----NASLTRTLQH-RIAL-HVADGLRYLHSAMIIYRDLKPHNVLlftLYPNCAIiaKIADYGIAQYCC------ 142
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 20986497 215 QYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd14068 143 RMGIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDIL 184
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
54-255 5.16e-14

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: 72.77  E-value: 5.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRltGQQVAIKKIPnafDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPygefksV 133
Cdd:cd05039   7 DLKLGELIGKGEFGDVMLGDYR--GQKVAVKCLK---DDSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNG------L 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLMES-DLHQIIHS--SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTS 210
Cdd:cd05039  76 YIVTEYMAKgSLVDYLRSrgRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEASSN 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 20986497 211 PAEHQYfmteyvATRWyRAPElMLSLHEYTQAIDLWSVGCIFGEM 255
Cdd:cd05039 156 QDGGKL------PIKW-TAPE-ALREKKFSTKSDVWSFGILLWEI 192
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
61-266 5.23e-14

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: 72.70  E-value: 5.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTgQQVAIKKI------PNAFdvvtnakrtLRELKILKHFKHDNIIAIKDILRPTVPygefksVY 134
Cdd:cd05034   3 LGAGQFGEVWMGVWNGT-TKVAVKTLkpgtmsPEAF---------LQEAQIMKKLRHDKLVQLYAVCSDEEP------IY 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLMesdlhqiIHSS----------QPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA 204
Cdd:cd05034  67 IVTELM-------SKGSlldylrtgegRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLA 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RGLCTSpaehqyfmtEYVA-------TRWyRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQL-FPGKN 266
Cdd:cd05034 140 RLIEDD---------EYTAregakfpIKW-TAPEAALY-GRFTIKSDVWSFGILLYEIVTYGRVpYPGMT 198
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
61-262 6.75e-14

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


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 73.13  E-value: 6.75e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNA-FDVVTNAKRTLRELKILKHFKHDNIIAIkdilrpTVPYGEFKSVYVVLDL 139
Cdd:cd05630   8 LGKGGFGEVCACQVRATGKMYACKKLEKKrIKKRKGEAMALNEKQILEKVNSRFVVSL------AYAYETKDALCLVLTL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 140 MES-DLHQIIHSSQPLTLEHVRYFLY--QLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMArglcTSPAEHQY 216
Cdd:cd05630  82 MNGgDLKFHIYHMGQAGFPEARAVFYaaEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLA----VHVPEGQT 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 20986497 217 FMTEyVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLF 262
Cdd:cd05630 158 IKGR-VGTVGYMAPEVVKN-ERYTFSPDWWALGCLLYEMIAGQSPF 201
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
55-205 7.36e-14

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: 72.49  E-value: 7.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnaFDVVTNAKRTL-RELKILKHFKhdNIIAIkdilrPTV-PYG-EFK 131
Cdd:cd14016   2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIK-----IEKKDSKHPQLeYEAKVYKLLQ--GGPGI-----PRLyWFGqEGD 69
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 132 SVYVVLDLMESDLHQI-IHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL--VNENC-ELKIGDFGMAR 205
Cdd:cd14016  70 YNVMVMDLLGPSLEDLfNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLmgLGKNSnKVYLIDFGLAK 147
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
61-277 9.29e-14

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: 72.04  E-value: 9.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTgqqVAIKKIpnafDVVTNAKRTLRELK----ILKHFKHDNII-----AIKDILRPTVPYGEFK 131
Cdd:cd14062   1 IGSGSFGTVYKGRWHGD---VAVKKL----NVTDPTPSQLQAFKnevaVLRKTRHVNILlfmgyMTKPQLAIVTQWCEGS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMES--DLHQIIHSSQpltlehvryflyQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglct 209
Cdd:cd14062  74 SLYKHLHVLETkfEMLQLIDIAR------------QTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLAT---- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 210 spaehqyfmteyVATRW--------------YRAPEL--MLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvHQLQL 273
Cdd:cd14062 138 ------------VKTRWsgsqqfeqptgsilWMAPEVirMQDENPYSFQSDVYAFGIVLYELLTGQLPYSHIN--NRDQI 203

                ....
gi 20986497 274 IMMV 277
Cdd:cd14062 204 LFMV 207
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
61-347 9.31e-14

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: 71.96  E-value: 9.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPnafdvVTNAKRTlrELKILKHFKHDNIIAikdiLRPTVPYGEfkSVYVVLDLM 140
Cdd:cd13995  12 IPRGAFGKVYLAQDTKTKKRMACKLIP-----VEQFKPS--DVEIQACFRHENIAE----LYGALLWEE--TVHLFMEAG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 ES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIgDFgmarGLCTSPAEHQYFMT 219
Cdd:cd13995  79 EGgSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLV-DF----GLSVQMTEDVYVPK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 220 EYVATRWYRAPELMLSLHEYTQAiDLWSVGCifgemlarrqlfpgknyvhqlQLIMMVLGTPSPAVIQAVGAERVRAYI- 298
Cdd:cd13995 154 DLRGTEIYMSPEVILCRGHNTKA-DIYSLGA---------------------TIIHMQTGSPPWVRRYPRSAYPSYLYIi 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 20986497 299 -QSLPPRQPVPwETVYPGADRqalsLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd13995 212 hKQAPPLEDIA-QDCSPAMRE----LLEAALERNPNHRSSAAELLKHEAL 256
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
61-255 9.55e-14

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: 73.37  E-value: 9.55e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTN-AKRTLRELKILKHFKHDN---IIAIKdilrptVPYGEFKSVYVV 136
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKeVAHTIGERNILVRTALDEspfIVGLK------FSFQTPTDLYLV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 137 LDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQ 215
Cdd:cd05586  75 TDYMSGgELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTN 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 20986497 216 YFmteyVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEM 255
Cdd:cd05586 155 TF----CGTTEYLAPEVLLDEKGYTKMVDFWSLGVLVFEM 190
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
61-258 9.91e-14

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 72.16  E-value: 9.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDvvtNAKRT-LRELKILKHFKHDNIIAIKDILrptvpYGEFKSVYVVLDL 139
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGEVMVMKELIRFDE---EAQRNfLKEVKVMRSLDHPNVLKFIGVL-----YKDKKLNLITEYI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 140 MESDLHQIIHS-SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL----------- 207
Cdd:cd14154  73 PGGTLKDVLKDmARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIveerlpsgnms 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 208 -------CTSPAEHQYFMTeyVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLAR 258
Cdd:cd14154 153 psetlrhLKSPDRKKRYTV--VGNPYWMAPE-MLNGRSYDEKVDIFSFGIVLCEIIGR 207
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
81-256 1.12e-13

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 72.70  E-value: 1.12e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  81 VAIKKIPNafDVVTNAKRT-LRELKILKHFKHDNIIAIKDILRPTVPygefksVYVVLDLMES-DLHQIIHSSQ------ 152
Cdd:cd05097  47 VAVKMLRA--DVTKTARNDfLKEIKIMSRLKNPNIIRLLGVCVSDDP------LCMITEYMENgDLNQFLSQREiestft 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 153 ------PLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSpaehQYFMTEYVAT-- 224
Cdd:cd05097 119 hannipSVSIANLLYMAVQIASGMKYLASLNFVHRDLATRNCLVGNHYTIKIADFGMSRNLYSG----DYYRIQGRAVlp 194
                       170       180       190
                ....*....|....*....|....*....|...
gi 20986497 225 -RWYRAPELMLSlhEYTQAIDLWSVGCIFGEML 256
Cdd:cd05097 195 iRWMAWESILLG--KFTTASDVWAFGVTLWEMF 225
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
58-350 1.14e-13

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: 72.01  E-value: 1.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  58 IETIGNGAYGVVSSARRRLTGQQVAIKKI--PNAFDVVTNAKRtlrELKILKHFKHDNIIaikdilRPTVPYGEFKSVYV 135
Cdd:cd06642   9 LERIGKGSFGEVYKGIDNRTKEVVAIKIIdlEEAEDEIEDIQQ---EITVLSQCDSPYIT------RYYGSYLKGTKLWI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 136 VLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQ 215
Cdd:cd06642  80 IMEYLGGGSALDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 216 YFmteyVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEmLARRQlfPGKNYVHQLQLIMMVLGTpSPAVIQAVGAERVR 295
Cdd:cd06642 160 TF----VGTPFWMAPEV-IKQSAYDFKADIWSLGITAIE-LAKGE--PPNSDLHPMRVLFLIPKN-SPPTLEGQHSKPFK 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 296 AYIQSLPPRQPvpwetvypgadrqalsllgrmlRFEPSARisaaAALRHPFLAKY 350
Cdd:cd06642 231 EFVEACLNKDP----------------------RFRPTAK----ELLKHKFITRY 259
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
55-354 1.16e-13

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: 72.34  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARR---RLTGQQVAIKKIPNAfDVVTNAK---RTLRELKILKHFKHDNIIAikdilrpTVPYG 128
Cdd:cd05613   2 FELLKVLGTGAYGKVFLVRKvsgHDAGKLYAMKVLKKA-TIVQKAKtaeHTRTERQVLEHIRQSPFLV-------TLHYA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 eFKS---VYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA 204
Cdd:cd05613  74 -FQTdtkLHLILDYINGgELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 205 RGLCTSPAEHQYfmtEYVATRWYRAPELML---SLHEytQAIDLWSVGCIFGEMLARRQLFP--GKNYVHqlqlimmvlg 279
Cdd:cd05613 153 KEFLLDENERAY---SFCGTIEYMAPEIVRggdSGHD--KAVDWWSLGVLMYELLTGASPFTvdGEKNSQ---------- 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 280 tpspaviqavgAERVRAYIQSLPPrqpvpwetvYPgADRQALS--LLGRMLRFEPSARI-----SAAAALRHPFLAKYHD 352
Cdd:cd05613 218 -----------AEISRRILKSEPP---------YP-QEMSALAkdIIQRLLMKDPKKRLgcgpnGADEIKKHPFFQKINW 276

                ..
gi 20986497 353 PD 354
Cdd:cd05613 277 DD 278
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
136-277 1.23e-13

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 72.09  E-value: 1.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 136 VLDLMES-DLHqiIHSSQP--LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMArglC--TS 210
Cdd:cd05606  76 ILDLMNGgDLH--YHLSQHgvFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLA---CdfSK 150
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497 211 PAEHQyfmteYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLA-----RRQLFPGKNYVHQLQLIMMV 277
Cdd:cd05606 151 KKPHA-----SVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLYKLLKghspfRQHKTKDKHEIDRMTLTMNV 217
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
53-257 1.24e-13

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


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 71.52  E-value: 1.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRrLTGQQVAIKKIPNAFdvvTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPygefks 132
Cdd:cd05112   4 SELTFVQEIGSGQFGLVHLGYW-LNKDKVAIKTIREGA---MSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAP------ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMESD-LHQIIHSSQ-PLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCts 210
Cdd:cd05112  74 ICLVFEFMEHGcLSDYLRTQRgLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVL-- 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 20986497 211 paEHQYfmTEYVATRW---YRAPELmLSLHEYTQAIDLWSVGCIFGEMLA 257
Cdd:cd05112 152 --DDQY--TSSTGTKFpvkWSSPEV-FSFSRYSSKSDVWSFGVLMWEVFS 196
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
57-255 1.31e-13

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: 72.11  E-value: 1.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  57 IIETIGNGAYGVV--SSARRRLTGQ---QVAIKKIPNAfdVVTNAKRTL-RELKILKHFKHDNIIAIKDILrptvpyGEF 130
Cdd:cd05049   9 LKRELGEGAFGKVflGECYNLEPEQdkmLVAVKTLKDA--SSPDARKDFeREAELLTNLQHENIVKFYGVC------TEG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVLDLMES-DLHQIIHSSQP--------------LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE 195
Cdd:cd05049  81 DPLLMVFEYMEHgDLNKFLRSHGPdaaflasedsapgeLTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLV 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 196 LKIGDFGMARGLCTSpaehQYFMTE---YVATRWYrAPELMLsLHEYTQAIDLWSVGCIFGEM 255
Cdd:cd05049 161 VKIGDFGMSRDIYST----DYYRVGghtMLPIRWM-PPESIL-YRKFTTESDVWSFGVVLWEI 217
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
61-258 1.42e-13

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: 71.53  E-value: 1.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNaFDVVTnaKRT-LRELKILKHFKHDNIIAIKDILrptvpYGEFKSVYVVLDL 139
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGEVMVMKELIR-FDEET--QRTfLKEVKVMRCLEHPNVLKFIGVL-----YKDKRLNFITEYI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 140 MESDLHQIIHS--SQPLTLEHVRyFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQYF 217
Cdd:cd14221  73 KGGTLRGIIKSmdSHYPWSQRVS-FAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQPEGL 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 20986497 218 MTEYVATR----------WYRAPElMLSLHEYTQAIDLWSVGCIFGEMLAR 258
Cdd:cd14221 152 RSLKKPDRkkrytvvgnpYWMAPE-MINGRSYDEKVDVFSFGIVLCEIIGR 201
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
54-335 1.44e-13

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: 72.64  E-value: 1.44e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARR---RLTGQQVAIKKIPNAfDVVTNAK---RTLRELKILKHFKHDNIIAikdilrpTVPY 127
Cdd:cd05614   1 NFELLKVLGTGAYGKVFLVRKvsgHDANKLYAMKVLRKA-ALVQKAKtveHTRTERNVLEHVRQSPFLV-------TLHY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 128 GeFKS---VYVVLDL-----MESDLHQIIHSSQpltlEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIG 199
Cdd:cd05614  73 A-FQTdakLHLILDYvsggeLFTHLYQRDHFSE----DEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLT 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 200 DFGMARGLCTSPAEHQYfmtEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFP---GKNYVHQLQLIMM 276
Cdd:cd05614 148 DFGLSKEFLTEEKERTY---SFCGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFTlegEKNTQSEVSRRIL 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 277 VLGTPSPAVIQAVGAERVRAYIQSLPPR---------QPVPWETVYPGADRQALSLLGRMLRFEPSAR 335
Cdd:cd05614 225 KCDPPFPSFIGPVARDLLQKLLCKDPKKrlgagpqgaQEIKEHPFFKGLDWEALALRKVNPPFRPSIR 292
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
58-286 1.59e-13

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: 71.62  E-value: 1.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  58 IETIGNGAYGVVSSARRRLTGQQVAIKKI--PNAFDVVTNAKRtlrELKILKHFKHDNIiaikdilrpTVPYGEF---KS 132
Cdd:cd06640   9 LERIGKGSFGEVFKGIDNRTQQVVAIKIIdlEEAEDEIEDIQQ---EITVLSQCDSPYV---------TKYYGSYlkgTK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPA 212
Cdd:cd06640  77 LWIIMEYLGGGSALDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQI 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 213 EHQYFmteyVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEmLARRQlfPGKNYVHQLQLIMMVLGTPSPAVI 286
Cdd:cd06640 157 KRNTF----VGTPFWMAPEV-IQQSAYDSKADIWSLGITAIE-LAKGE--PPNSDMHPMRVLFLIPKNNPPTLV 222
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
55-256 1.74e-13

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: 71.14  E-value: 1.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPnafdvvtnaKRTLRELKILKHFkhdnIIAIKDILRPTVPYGeFKSVY 134
Cdd:cd14102   2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVV---------KERVTEWGTLNGV----MVPLEIVLLKKVGSG-FRGVI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLME---------------SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVN-ENCELKI 198
Cdd:cd14102  68 KLLDWYErpdgflivmerpepvKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKL 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 199 GDFGMARGLctspaeHQYFMTEYVATRWYRAPElMLSLHEY-TQAIDLWSVGCIFGEML 256
Cdd:cd14102 148 IDFGSGALL------KDTVYTDFDGTRVYSPPE-WIRYHRYhGRSATVWSLGVLLYDMV 199
PTZ00284 PTZ00284
protein kinase; Provisional
55-362 1.88e-13

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 73.46  E-value: 1.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRptvpYGEFKSVY 134
Cdd:PTZ00284 131 FKILSLLGEGTFGKVVEAWDRKRKEYCAVKIVRNVPKYTRDAKIEIQFMEKVRQADPADRFPLMKIQR----YFQNETGH 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  135 --VVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSA-QVIHRDLKPSNLLVN----------------ENCE 195
Cdd:PTZ00284 207 mcIVMPKYGPCLLDWIMKHGPFSHRHLAQIIFQTGVALDYFHTElHLMHTDLKPENILMEtsdtvvdpvtnralppDPCR 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  196 LKIGDFGmarGLCtspaEHQYFMTEYVATRWYRAPELMLSLHeYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIM 275
Cdd:PTZ00284 287 VRICDLG---GCC----DERHSRTAIVSTRHYRSPEVVLGLG-WMYSTDMWSMGCIIYELYTGKLLYDTHDNLEHLHLME 358
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  276 MVLGTPSPAVIQAVGAERVRAYIQSLPPRQPV-------------PWETVYpgADRQALSLLGRMLRFEPSARISAAAAL 342
Cdd:PTZ00284 359 KTLGRLPSEWAGRCGTEEARLLYNSAGQLRPCtdpkhlariararPVREVI--RDDLLCDLIYGLLHYDRQKRLNARQMT 436
                        330       340
                 ....*....|....*....|....*...
gi 20986497  343 RHPFLAKYHD--------PDDEPDCAPP 362
Cdd:PTZ00284 437 THPYVLKYYPecrqhpnyPDNRSMLRPT 464
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
55-256 1.91e-13

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 71.15  E-value: 1.91e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnAFDVVT------NAKRTLRELKILKHFKHdniiAIKDILRPTVPYG 128
Cdd:cd14100   2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHV--EKDRVSewgelpNGTRVPMEIVLLKKVGS----GFRGVIRLLDWFE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLME--SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENC-ELKIGDFGMAR 205
Cdd:cd14100  76 RPDSFVLVLERPEpvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTgELKLIDFGSGA 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 20986497 206 GLctspaeHQYFMTEYVATRWYRAPElMLSLHEY-TQAIDLWSVGCIFGEML 256
Cdd:cd14100 156 LL------KDTVYTDFDGTRVYSPPE-WIRFHRYhGRSAAVWSLGILLYDMV 200
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
53-257 2.10e-13

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: 71.75  E-value: 2.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSA-----RRRLTGQQVAIKKIPNAfDVVTNAKRTLRELKILKHF-KHDNIIAI-------KD 119
Cdd:cd05054   7 DRLKLGKPLGRGAFGKVIQAsafgiDKSATCRTVAVKMLKEG-ATASEHKALMTELKILIHIgHHLNVVNLlgactkpGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 120 ILRPTVPYGEFKSVYVVL-----------DLMESDLHQIIHSS----QPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLK 184
Cdd:cd05054  86 PLMVIVEFCKFGNLSNYLrskreefvpyrDKGARDVEEEEDDDelykEPLTLEDLICYSFQVARGMEFLASRKCIHRDLA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 185 PSNLLVNENCELKIGDFGMARGLCTSPaehqyfmtEYVAT-------RWYrAPELMLSlHEYTQAIDLWSVGCIFGEMLA 257
Cdd:cd05054 166 ARNILLSENNVVKICDFGLARDIYKDP--------DYVRKgdarlplKWM-APESIFD-KVYTTQSDVWSFGVLLWEIFS 235
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
61-261 2.11e-13

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: 70.84  E-value: 2.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYG-VVSSARRRLTGQQ--VAIKKIPNAfDVVTNAKRTLRELKILKHFKHDNIIAIKDILRptvpyGEfkSVYVVL 137
Cdd:cd05060   3 LGHGNFGsVRKGVYLMKSGKEveVAVKTLKQE-HEKAGKKEFLREASVMAQLDHPCIVRLIGVCK-----GE--PLMLVM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 138 DLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSN-LLVNENcELKIGDFGMARGLCTSPaehq 215
Cdd:cd05060  75 ELAPlGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNvLLVNRH-QAKISDFGMSRALGAGS---- 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 20986497 216 yfmTEYVAT-------RWYrAPElMLSLHEYTQAIDLWSVGCIFGEMLARRQL 261
Cdd:cd05060 150 ---DYYRATtagrwplKWY-APE-CINYGKFSSKSDVWSYGVTLWEAFSYGAK 197
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
53-256 2.15e-13

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: 72.41  E-value: 2.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKkIPNAFDVVtnaKRT-----LRELKILKHFKHDNIIAIkdilrptvpY 127
Cdd:cd05596  26 EDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMK-LLSKFEMI---KRSdsaffWEERDIMAHANSEWIVQL---------H 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 128 GEF---KSVYVVLDLMES-DLHQIIhSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGM 203
Cdd:cd05596  93 YAFqddKYLYMVMDYMPGgDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGT 171
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 204 -----ARGLCTSPAEhqyfmteyVATRWYRAPELMLS---LHEYTQAIDLWSVGCIFGEML 256
Cdd:cd05596 172 cmkmdKDGLVRSDTA--------VGTPDYISPEVLKSqggDGVYGRECDWWSVGVFLYEML 224
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
61-346 2.17e-13

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 72.05  E-value: 2.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLT---GQQVAIKKIPNAfDVVTNAKRTLR---ELKILKHFKHDNIIAIKdilrptvpYGeFKS-- 132
Cdd:cd05584   4 LGKGGYGKVFQVRKTTGsdkGKIFAMKVLKKA-SIVRNQKDTAHtkaERNILEAVKHPFIVDLH--------YA-FQTgg 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 -VYVVLD-LMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFgmarGLCTS 210
Cdd:cd05584  74 kLYLILEyLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDF----GLCKE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 211 PAEHQYFMTEYVATRWYRAPE-LMLSLHEytQAIDLWSVGCIFGEMLARRQLFPGKNyvhQLQLIMMVLgtpspaviqav 289
Cdd:cd05584 150 SIHDGTVTHTFCGTIEYMAPEiLTRSGHG--KAVDWWSLGALMYDMLTGAPPFTAEN---RKKTIDKIL----------- 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497 290 gaervRAYIqSLPPrqpvpwetvYPGADrqALSLLGRMLRFEPSARI-----SAAAALRHPF 346
Cdd:cd05584 214 -----KGKL-NLPP---------YLTNE--ARDLLKKLLKRNVSSRLgsgpgDAEEIKAHPF 258
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
53-266 2.79e-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: 70.84  E-value: 2.79e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRlTGQQVAIKKI-PNAFDVvtnaKRTLRELKILKHFKHDNIIAIKDILRPTVPY---G 128
Cdd:cd05072   7 ESIKLVKKLGAGQFGEVWMGYYN-NSTKVAVKTLkPGTMSV----QAFLEEANLMKTLQHDKLVRLYAVVTKEEPIyiiT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMESDlhqiihSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLc 208
Cdd:cd05072  82 EYMAKGSLLDFLKSD------EGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVI- 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 209 tspAEHQYFMTE--YVATRWyRAPElMLSLHEYTQAIDLWSVGCIFGEMLARRQL-FPGKN 266
Cdd:cd05072 155 ---EDNEYTAREgaKFPIKW-TAPE-AINFGSFTIKSDVWSFGILLYEIVTYGKIpYPGMS 210
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
61-256 2.86e-13

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: 70.50  E-value: 2.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRltGQQVAIK--KIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDI-LRP-----TVPYGEFKS 132
Cdd:cd14061   2 IGVGGFGKVYRGIWR--GEEVAVKaaRQDPDEDISVTLENVRQEARLFWMLRHPNIIALRGVcLQPpnlclVMEYARGGA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMESDLHQIIHssqpltlehvryFLYQLLRGLKYMHS---AQVIHRDLKPSNLLVNENCE--------LKIGDF 201
Cdd:cd14061  80 LNRVLAGRKIPPHVLVD------------WAIQIARGMNYLHNeapVPIIHRDLKSSNILILEAIEnedlenktLKITDF 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 202 GMARglctspaEHqYFMTEYVA--TRWYRAPELmLSLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd14061 148 GLAR-------EW-HKTTRMSAagTYAWMAPEV-IKSSTFSKASDVWSYGVLLWELL 195
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
54-275 3.69e-13

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: 71.18  E-value: 3.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNafDVVT---NAKRTLRELKILKhfkhdniiaikdiLRPTVPY-GE 129
Cdd:cd05616   1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKK--DVVIqddDVECTMVEKRVLA-------------LSGKPPFlTQ 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLD----LME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDF 201
Cdd:cd05616  66 LHSCFQTMDrlyfVMEyvngGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADF 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 202 GMarglCTSPAEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIM 275
Cdd:cd05616 146 GM----CKENIWDGVTTKTFCGTPDYIAPEI-IAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIM 214
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
53-275 3.81e-13

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: 71.95  E-value: 3.81e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRlTGQQVAIKKIPNAFDVVTNAKRTLrelkilkHFKHDNIIAIKD---ILRPTVPYGE 129
Cdd:cd05621  52 EDYDVVKVIGRGAFGEVQLVRHK-ASQKVYAMKLLSKFEMIKRSDSAF-------FWEERDIMAFANspwVVQLFCAFQD 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDLMES-DLHQIIhSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLC 208
Cdd:cd05621 124 DKYLYMVMEYMPGgDLVNLM-SNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMD 202
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAEHqyfMTEYVATRWYRAPELMLSL---HEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIM 275
Cdd:cd05621 203 ETGMVH---CDTAVGTPDYISPEVLKSQggdGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIM 269
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
53-275 3.87e-13

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: 72.35  E-value: 3.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTgQQVAIKKIPNAFDVVTNAKRT-LRELKilkhfkhdNIIAIKDILRPTVPYGEFK 131
Cdd:cd05624  72 DDFEIIKVIGRGAFGEVAVVKMKNT-ERIYAMKILNKWEMLKRAETAcFREER--------NVLVNGDCQWITTLHYAFQ 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 S---VYVVLDL-MESDLHQIIHS-SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMarg 206
Cdd:cd05624 143 DenyLYLVMDYyVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGS--- 219
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 207 lCTSPAEHQYFMTEY-VATRWYRAPELMLSLHE----YTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIM 275
Cdd:cd05624 220 -CLKMNDDGTVQSSVaVGTPDYISPEILQAMEDgmgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIM 292
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
61-262 4.99e-13

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: 70.46  E-value: 4.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIpnafdvvtnakrtlrELKILKHFKHDNIIAI-KDILRP-------TVPYG-EFK 131
Cdd:cd05605   8 LGKGGFGEVCACQVRATGKMYACKKL---------------EKKRIKKRKGEAMALNeKQILEKvnsrfvvSLAYAyETK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 -SVYVVLDLMES-DLHQIIHS-SQP-LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA--- 204
Cdd:cd05605  73 dALCLVLTIMNGgDLKFHIYNmGNPgFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAvei 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 205 ------RGlctspaehqyfmteYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLF 262
Cdd:cd05605 153 pegetiRG--------------RVGTVGYMAPEVVKN-ERYTFSPDWWGLGCLIYEMIEGQAPF 201
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
61-266 6.50e-13

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: 69.56  E-value: 6.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTgQQVAIKKI------PNAFdvvtnakrtLRELKILKHFKHDNIIAIKDIL--RPTVPYGEFKS 132
Cdd:cd14203   3 LGQGCFGEVWMGTWNGT-TKVAIKTLkpgtmsPEAF---------LEEAQIMKKLRHDKLVQLYAVVseEPIYIVTEFMS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMESDlhqiihSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglCTSPA 212
Cdd:cd14203  73 KGSLLDFLKDG------EGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLAR--LIEDN 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 213 EHQYFMTEYVATRWyRAPELMLsLHEYTQAIDLWSVGCIFGEMLAR-RQLFPGKN 266
Cdd:cd14203 145 EYTARQGAKFPIKW-TAPEAAL-YGRFTIKSDVWSFGILLTELVTKgRVPYPGMN 197
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
138-264 6.99e-13

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: 70.49  E-value: 6.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 138 DLMesdLHqiIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMarglCTSPAEHQYF 217
Cdd:cd05592  82 DLM---FH--IQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGM----CKENIYGENK 152
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 20986497 218 MTEYVATRWYRAPELMLSLHeYTQAIDLWSVGCIFGEMLARRQLFPG 264
Cdd:cd05592 153 ASTFCGTPDYIAPEILKGQK-YNQSVDWWSFGVLLYEMLIGQSPFHG 198
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
51-347 8.13e-13

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: 70.82  E-value: 8.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  51 VGD----EYEIIETIGNGAYGVV----SSARRRLtgqqVAIKKIPNAFDVVTNAkrtLRELKILKHF--------KHDNI 114
Cdd:cd14218   4 IGDlfngRYHVVRKLGWGHFSTVwlcwDIQRKRF----VALKVVKSAVHYTETA---VDEIKLLKCVrdsdpsdpKRETI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 115 IAIKDILRPTVPYGefKSVYVVLDLMESDLHQ-IIHSS-QPLTLEHVRYFLYQLLRGLKYMHS-AQVIHRDLKP------ 185
Cdd:cd14218  77 VQLIDDFKISGVNG--VHVCMVLEVLGHQLLKwIIKSNyQGLPLPCVKSILRQVLQGLDYLHTkCKIIHTDIKPenilmc 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 186 ---------------------------------SNLLVN-------ENCELKIGDFGMArglCTSpaeHQYFmTEYVATR 225
Cdd:cd14218 155 vdegyvrrlaaeatiwqqagapppsgssvsfgaSDFLVNplepqnaDKIRVKIADLGNA---CWV---HKHF-TEDIQTR 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 226 WYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLF---PGKNYVH---QLQLIMMVLGTPSPAViqAVGAERVRAY-- 297
Cdd:cd14218 228 QYRALEVLIGA-EYGTPADIWSTACMAFELATGDYLFephSGEDYTRdedHIAHIVELLGDIPPHF--ALSGRYSREYfn 304
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 298 -------IQSLPP---------RQPVPWETVypgadRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14218 305 rrgelrhIKNLKHwglyevlveKYEWPLEQA-----AQFTDFLLPMMEFLPEKRATAAQCLQHPWL 365
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
53-266 8.69e-13

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: 69.96  E-value: 8.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTN-AKRTLRELKILKHFKHdniiaikdilrPTVP--YGE 129
Cdd:cd05574   1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNkVKRVLTEREILATLDH-----------PFLPtlYAS 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKS---VYVVLDL-MESDLHQIIHSsQP---LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDF- 201
Cdd:cd05574  70 FQTsthLCFVMDYcPGGELFRLLQK-QPgkrLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFd 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 202 -----------------GMARGLCTSPAEHQYFMTE-------YVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLA 257
Cdd:cd05574 149 lskqssvtpppvrkslrKGSRRSSVKSIEKETFVAEpsarsnsFVGTEEYIAPEV-IKGDGHGSAVDWWTLGILLYEMLY 227

                ....*....
gi 20986497 258 RRQLFPGKN 266
Cdd:cd05574 228 GTTPFKGSN 236
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
53-363 1.05e-12

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: 70.00  E-value: 1.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNA-FDVVTNAKRTLRELKILKHFKHDNIIAIkdilrpTVPYGEFK 131
Cdd:cd05632   2 NTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKrIKKRKGESMALNEKQILEKVNSQFVVNL------AYAYETKD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLY--QLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLC 208
Cdd:cd05632  76 ALCLVLTIMNGgDLKFHIYNMGNPGFEEERALFYaaEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAehqyfMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhqlqlimmvlgtpspaviQA 288
Cdd:cd05632 156 EGES-----IRGRVGTVGYMAPEV-LNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRK--------------------EK 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 289 VGAERVRAYIQSLpprqpvpwETVYPGA-DRQALSLLGRMLRFEPSARI-----SAAAALRHPFLAKYHDPDDEPD-CAP 361
Cdd:cd05632 210 VKREEVDRRVLET--------EEVYSAKfSEEAKSICKMLLTKDPKQRLgcqeeGAGEVKRHPFFRNMNFKRLEAGmLDP 281

                ..
gi 20986497 362 PF 363
Cdd:cd05632 282 PF 283
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
64-285 1.09e-12

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: 69.07  E-value: 1.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  64 GAYGVVSSARRRLTGQqVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGefksvyVVLDLMESD 143
Cdd:cd14027   4 GGFGKVSLCFHRTQGL-VVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYS------LVMEYMEKG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 144 --LHQIIHSSQPLTLEHvrYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA-----RGLCTSPAEHQY 216
Cdd:cd14027  77 nlMHVLKKVSVPLSVKG--RIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwSKLTKEEHNEQR 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 217 FMTEYVA----TRWYRAPELMLSLH-EYTQAIDLWSVGCIFGEMLARRQlfPGKNYVHQLQLIMMVLGTPSPAV 285
Cdd:cd14027 155 EVDGTAKknagTLYYMAPEHLNDVNaKPTEKSDVYSFAIVLWAIFANKE--PYENAINEDQIIMCIKSGNRPDV 226
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
54-264 1.16e-12

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: 68.92  E-value: 1.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSsaRRRLTGQQVAIKKI---PNAfDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTvpygef 130
Cdd:cd14145   7 ELVLEEIIGIGGFGKVY--RAIWIGDEVAVKAArhdPDE-DISQTIENVRQEAKLFAMLKHPNIIALRGVCLKE------ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHS---AQVIHRDLKPSNLLVNENCE--------LKIG 199
Cdd:cd14145  78 PNLCLVMEFARGGPLNRVLSGKRIPPDILVNWAVQIARGMNYLHCeaiVPVIHRDLKSSNILILEKVEngdlsnkiLKIT 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 200 DFGMARglctspAEHQYFMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQLFPG 264
Cdd:cd14145 158 DFGLAR------EWHRTTKMSAAGTYAWMAPEVIRS-SMFSKGSDVWSYGVLLWELLTGEVPFRG 215
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
61-254 1.33e-12

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: 68.45  E-value: 1.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSA--RRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILrptvpygEFKSVYVVLD 138
Cdd:cd05116   3 LGSGNFGTVKKGyyQMKKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGIC-------EAESWMLVME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 139 LME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQYF 217
Cdd:cd05116  76 MAElGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQ 155
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 20986497 218 MTEYVATRWYrAPELMlSLHEYTQAIDLWSVGCIFGE 254
Cdd:cd05116 156 THGKWPVKWY-APECM-NYYKFSSKSDVWSFGVLMWE 190
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
99-345 1.38e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 70.69  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   99 TLRELKILKHFKHDNIIAIKDiLRPTVPYgefksVYVVLDLMESDLHQIIHS-SQPLTLEHVRYFLYQLLRGLKYMHSAQ 177
Cdd:PHA03211 207 SVHEARLLRRLSHPAVLALLD-VRVVGGL-----TCLVLPKYRSDLYTYLGArLRPLGLAQVTAVARQLLSAIDYIHGEG 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  178 VIHRDLKPSNLLVNENCELKIGDFGMA---RGLCTSPAehQYFMTEYVATrwyRAPELmLSLHEYTQAIDLWSVG-CIFG 253
Cdd:PHA03211 281 IIHRDIKTENVLVNGPEDICLGDFGAAcfaRGSWSTPF--HYGIAGTVDT---NAPEV-LAGDPYTPSVDIWSAGlVIFE 354
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  254 EMLARRQLFPG------KNYVHQLQLIMM-----VLGTPSPAVIQAVGAERVRAYIQSLPPRQPVPWeTVYPGADRQALS 322
Cdd:PHA03211 355 AAVHTASLFSAsrgderRPYDAQILRIIRqaqvhVDEFPQHAGSRLVSQYRHRAARNRRPAYTRPAW-TRYYKLDLDVEY 433
                        250       260
                 ....*....|....*....|...
gi 20986497  323 LLGRMLRFEPSARISAAAALRHP 345
Cdd:PHA03211 434 LVCRALTFDGARRPSAAELLRLP 456
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
55-347 1.39e-12

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: 68.84  E-value: 1.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEI--IETIGNGAYGVVSSARRRLTGQQVAIKKIPnafdvVTNAKR---TLRELKILKHFKHDNIIAIKDILRPTvpyge 129
Cdd:cd14192   4 YAVcpHEVLGGGRFGQVHKCTELSTGLTLAAKIIK-----VKGAKEreeVKNEINIMNQLNHVNLIQLYDAFESK----- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 fKSVYVVLDLMESD--LHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL-VNENC-ELKIGDFGMAR 205
Cdd:cd14192  74 -TNLTLIMEYVDGGelFDRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGnQIKIIDFGLAR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 206 GLctSPAEHqyfMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMvlgtpspav 285
Cdd:cd14192 153 RY--KPREK---LKVNFGTPEFLAPEV-VNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVN--------- 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 286 iqavgaervrayiqslpprqpVPWE---TVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14192 218 ---------------------CKWDfdaEAFENLSEEAKDFISRLLVKEKSCRMSATQCLKHEWL 261
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
54-277 1.42e-12

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: 69.69  E-value: 1.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKhfkhdNIIAIKD---ILRPTVPYGEF 130
Cdd:cd14223   1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIML-----SLVSTGDcpfIVCMSYAFHTP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMArglCT 209
Cdd:cd14223  76 DKLSFILDLMNGgDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLA---CD 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 210 SPAEHQYfmtEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLA-----RRQLFPGKNYVHQLQLIMMV 277
Cdd:cd14223 153 FSKKKPH---ASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRghspfRQHKTKDKHEIDRMTLTMAV 222
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
138-257 1.60e-12

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: 69.62  E-value: 1.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 138 DLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPaehqyf 217
Cdd:cd05103 160 DVEEEEAGQEDLYKDFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDP------ 233
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 20986497 218 mtEYV-------ATRWYrAPELMLSlHEYTQAIDLWSVGCIFGEMLA 257
Cdd:cd05103 234 --DYVrkgdarlPLKWM-APETIFD-RVYTIQSDVWSFGVLLWEIFS 276
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
61-256 1.70e-12

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: 68.53  E-value: 1.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRltGQQVAIK---KIPNAfDVVTNAKRTLRELKILKHFKHDNIIAIKDI------LRPTVPYGEFK 131
Cdd:cd14146   2 IGVGGFGKVYRATWK--GQEVAVKaarQDPDE-DIKATAESVRQEAKLFSMLRHPNIIKLEGVcleepnLCLVMEFARGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESDLHQIIHSSQPltlEHVRY-FLYQLLRGLKYMHS---AQVIHRDLKPSNLLVNENCE--------LKIG 199
Cdd:cd14146  79 TLNRALAAANAAPGPRRARRIP---PHILVnWAVQIARGMLYLHEeavVPILHRDLKSSNILLLEKIEhddicnktLKIT 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 200 DFGMARglctspAEHQYFMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEML 256
Cdd:cd14146 156 DFGLAR------EWHRTTKMSAAGTYAWMAPEVIKS-SLFSKGSDIWSYGVLLWELL 205
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
101-282 1.79e-12

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 68.16  E-value: 1.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 101 RELKILKHFKHDNIIAIKD--ILRPTVPYGefKSVYVVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQ 177
Cdd:cd14012  47 KELESLKKLRHPNLVSYLAfsIERRGRSDG--WKVYLLTEYAPgGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNG 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 178 VIHRDLKPSNLLVNENCE---LKIGDFGMARGL---CTSPAehqyfMTEYVATRWyRAPELMLSLHEYTQAIDLWSVGCI 251
Cdd:cd14012 125 VVHKSLHAGNVLLDRDAGtgiVKLTDYSLGKTLldmCSRGS-----LDEFKQTYW-LPPELAQGSKSPTRKTDVWDLGLL 198
                       170       180       190
                ....*....|....*....|....*....|.
gi 20986497 252 FGEMLarrqlfPGKNYVHQLQLIMMVLGTPS 282
Cdd:cd14012 199 FLQML------FGLDVLEKYTSPNPVLVSLD 223
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
61-256 1.93e-12

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: 68.45  E-value: 1.93e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSAR-RRLTGQQ----VAIKKIPnafDVVTNAKRTL-RELKILKHFKHDNIIAIkdilrptvpYG---EFK 131
Cdd:cd05092  13 LGEGAFGKVFLAEcHNLLPEQdkmlVAVKALK---EATESARQDFqREAELLTVLQHQHIVRF---------YGvctEGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLME-SDLHQIIHSSQP---------------LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE 195
Cdd:cd05092  81 PLIMVFEYMRhGDLNRFLRSHGPdakildggegqapgqLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLV 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 196 LKIGDFGMARGLctspaehqyFMTEY--------VATRWYrAPELMLsLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd05092 161 VKIGDFGMSRDI---------YSTDYyrvggrtmLPIRWM-PPESIL-YRKFTTESDIWSFGVVLWEIF 218
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
159-347 2.22e-12

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 68.04  E-value: 2.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 159 VRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCEL---KIGDFGMARGLCTSPAehqyfMTEYVATRWYRAPELmLS 235
Cdd:cd14197 113 VKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLgdiKIVDFGLSRILKNSEE-----LREIMGTPEYVAPEI-LS 186
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 236 LHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSpaviqavgaervrayiqslpprqpvpwETVYPG 315
Cdd:cd14197 187 YEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYS---------------------------EEEFEH 239
                       170       180       190
                ....*....|....*....|....*....|..
gi 20986497 316 ADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14197 240 LSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
52-275 2.54e-12

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 69.65  E-value: 2.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  52 GDEYEIIETIGNGAYGVVSSARRRLTgQQVAIKKIPNAFDVVTNAKRTLrelkilkHFKHDNIIAIKD---ILRPTVPYG 128
Cdd:cd05622  72 AEDYEVVKVIGRGAFGEVQLVRHKST-RKVYAMKLLSKFEMIKRSDSAF-------FWEERDIMAFANspwVVQLFYAFQ 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMES-DLHQIIhSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL 207
Cdd:cd05622 144 DDRYLYMVMEYMPGgDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM 222
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 208 ctsPAEHQYFMTEYVATRWYRAPELMLSL---HEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIM 275
Cdd:cd05622 223 ---NKEGMVRCDTAVGTPDYISPEVLKSQggdGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIM 290
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
78-263 2.81e-12

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


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 67.80  E-value: 2.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  78 GQQVAIKKIPNAFdvvTNAKRTLRELKILKHFKHDNI-------IAIKDILRPTvpygEFKSVYVVLDLMESD---LHQI 147
Cdd:cd13992  25 GRTVAIKHITFSR---TEKRTILQELNQLKELVHDNLnkfigicINPPNIAVVT----EYCTRGSLQDVLLNReikMDWM 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 148 IHSSqpltlehvryFLYQLLRGLKYMHSAQVI-HRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQYFMTEYVATRW 226
Cdd:cd13992  98 FKSS----------FIKDIVKGMNYLHSSSIGyHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNHQLDEDAQHKKLLW 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 20986497 227 YrAPELM---LSLHEYTQAIDLWSVGCIFGEMLARRQLFP 263
Cdd:cd13992 168 T-APELLrgsLLEVRGTQKGDVYSFAIILYEILFRSDPFA 206
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
53-256 3.70e-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: 68.93  E-value: 3.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdvvtnakrTLRELKILKHFKHDNIIAIKDIL---------RP 123
Cdd:cd05627   2 DDFESLKVIGRGAFGEVRLVQKKDTGHIYAMK--------------ILRKADMLEKEQVAHIRAERDILveadgawvvKM 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 124 TVPYGEFKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFG 202
Cdd:cd05627  68 FYSFQDKRNLYLIMEFLPGgDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 203 MARGLCTS-------------PAE--HQYFMTEYVATRW----------------YRAPELMLSLHeYTQAIDLWSVGCI 251
Cdd:cd05627 148 LCTGLKKAhrtefyrnlthnpPSDfsFQNMNSKRKAETWkknrrqlaystvgtpdYIAPEVFMQTG-YNKLCDWWSLGVI 226

                ....*
gi 20986497 252 FGEML 256
Cdd:cd05627 227 MYEML 231
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
59-264 4.08e-12

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 67.56  E-value: 4.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRR---LTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFKSVYV 135
Cdd:cd05035   5 KILGEGEFGSVMEAQLKqddGSQLKVAVKTMKVDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTASDLNKPPSPMV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 136 VLDLME-SDLHQIIHSS----QP--LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLc 208
Cdd:cd05035  85 ILPFMKhGDLHSYLLYSrlggLPekLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKI- 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497 209 tspaehqYFMTEYVATRWYRAPELMLSLHE-----YTQAIDLWSVGCIFGEMLARRQL-FPG 264
Cdd:cd05035 164 -------YSGDYYRQGRISKMPVKWIALESladnvYTSKSDVWSFGVTMWEIATRGQTpYPG 218
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
152-257 4.19e-12

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: 68.49  E-value: 4.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 152 QPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPaehqyfmtEYV-------AT 224
Cdd:cd14207 175 RPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNP--------DYVrkgdarlPL 246
                        90       100       110
                ....*....|....*....|....*....|...
gi 20986497 225 RWYrAPELMLSlHEYTQAIDLWSVGCIFGEMLA 257
Cdd:cd14207 247 KWM-APESIFD-KIYSTKSDVWSYGVLLWEIFS 277
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
59-257 4.47e-12

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: 67.37  E-value: 4.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQV--AIKKIpNAFDVVTNAKRTLRELKIL-KHFKHDNIIAIKD---------ILRPTVP 126
Cdd:cd05047   1 DVIGEGNFGQVLKARIKKDGLRMdaAIKRM-KEYASKDDHRDFAGELEVLcKLGHHPNIINLLGacehrgylyLAIEYAP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 YGEFKSVYVVLDLMESD-LHQIIHSS-QPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA 204
Cdd:cd05047  80 HGNLLDFLRKSRVLETDpAFAIANSTaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 205 RGlctspaEHQYFMTEY--VATRWYRAPELMLSLheYTQAIDLWSVGCIFGEMLA 257
Cdd:cd05047 160 RG------QEVYVKKTMgrLPVRWMAIESLNYSV--YTTNSDVWSYGVLLWEIVS 206
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
55-264 4.94e-12

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: 68.10  E-value: 4.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfDVVT-NAKRTL----RELKILKHFKHDNIIAIkdilrptvpYGE 129
Cdd:cd05589   1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKG-DIIArDEVESLmcekRIFETVNSARHPFLVNL---------FAC 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDLME----SDLHQIIHS---SQPLTlehvRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFg 202
Cdd:cd05589  71 FQTPEHVCFVMEyaagGDLMMHIHEdvfSEPRA----VFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADF- 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497 203 marGLCTSPAEHQYFMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPG 264
Cdd:cd05589 146 ---GLCKEGMGFGDRTSTFCGTPEFLAPEV-LTDTSYTRAVDWWGLGVLIYEMLVGESPFPG 203
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
53-349 5.47e-12

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: 67.37  E-value: 5.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEII-ETIGNGAYGVVSSARRRLTGQQVAIKkipnafdVVTNAKRTLRELKIlkHFKHD---NIIAIKDILRPTvpYG 128
Cdd:cd14170   1 DDYKVTsQVLGLGINGKVLQIFNKRTQEKFALK-------MLQDCPKARREVEL--HWRASqcpHIVRIVDVYENL--YA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMES-DLHQIIHS--SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNE---NCELKIGDFG 202
Cdd:cd14170  70 GRKCLLIVMECLDGgELFSRIQDrgDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 203 MARGLCTspaeHQYFMTEyVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARrqlFPGKNYVHQLQLimmvlgtpS 282
Cdd:cd14170 150 FAKETTS----HNSLTTP-CYTPYYVAPEV-LGPEKYDKSCDMWSLGVIMYILLCG---YPPFYSNHGLAI--------S 212
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 283 PAViqavgAERVRAYIQSLPPRQpvpWETVypgaDRQALSLLGRMLRFEPSARISAAAALRHPFLAK 349
Cdd:cd14170 213 PGM-----KTRIRMGQYEFPNPE---WSEV----SEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQ 267
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
61-257 5.57e-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: 5.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAfdvVTNAKRTLRELKILKHFKHDNIIAIKDIlrptvpYGEFKSVYVVLDLM 140
Cdd:cd14115   1 IGRGRFSIVKKCLHKATRKDVAVKFVSKK---MKKKEQAAHEAALLQHLQHPQYITLHDT------YESPTSYILVLELM 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 ESD-LHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENC---ELKIGDFGMARGLCTspaehQY 216
Cdd:cd14115  72 DDGrLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQISG-----HR 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 20986497 217 FMTEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLA 257
Cdd:cd14115 147 HVHHLLGNPEFAAPEVIQGT-PVSLATDIWSIGVLTYVMLS 186
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
59-338 5.77e-12

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: 67.08  E-value: 5.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRltGQQVAIKKIpnafdvVTNAKRT-LRELKILK--HFKHDNIIAI-----KDIlrptvpyGEF 130
Cdd:cd14143   1 ESIGKGRFGEVWRGRWR--GEDVAVKIF------SSREERSwFREAEIYQtvMLRHENILGFiaadnKDN-------GTW 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVldlmeSDLHQiiHSSQPLTLEHVRYFLYQLLR-------GLKYMH--------SAQVIHRDLKPSNLLVNENCE 195
Cdd:cd14143  66 TQLWLV-----SDYHE--HGSLFDYLNRYTVTVEGMIKlalsiasGLAHLHmeivgtqgKPAIAHRDLKSKNILVKKNGT 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 196 LKIGDFGMARGLCTSPAEHQYFMTEYVATRWYRAPEL------MLSLHEYTQAiDLWSVGCIFGEmLARRQLFPGKNYVH 269
Cdd:cd14143 139 CCIADLGLAVRHDSATDTIDIAPNHRVGTKRYMAPEVlddtinMKHFESFKRA-DIYALGLVFWE-IARRCSIGGIHEDY 216
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 270 QLQLIMMVLGTPSPAVIQAVGAErvrayiQSLPPRQPVPWETVypgadrQALSLLGRMLR----FEPSARISA 338
Cdd:cd14143 217 QLPYYDLVPSDPSIEEMRKVVCE------QKLRPNIPNRWQSC------EALRVMAKIMRecwyANGAARLTA 277
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
53-347 5.81e-12

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: 66.97  E-value: 5.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFKS 132
Cdd:cd14088   1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKR-DGRKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMESDLHQIIHSSQPlTLEHVRyflyQLLRGLKYMHSAQVIHRDLKPSNLLVN---ENCELKIGDFGMAR---G 206
Cdd:cd14088  80 LATGREVFDWILDQGYYSERD-TSNVIR----QVLEAVAYLHSLKIVHRNLKLENLVYYnrlKNSKIVISDFHLAKlenG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 207 LCTSPAehqyfmteyvATRWYRAPELmLSLHEYTQAIDLWSVGcifgemlarrqlfpgknyvhqlqLIMMVLGTPSPAVI 286
Cdd:cd14088 155 LIKEPC----------GTPEYLAPEV-VGRQRYGRPVDCWAIG-----------------------VIMYILLSGNPPFY 200
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 287 QAVGAERVRAYIQSLPPR---------QPVpWETVYPGADrqalSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14088 201 DEAEEDDYENHDKNLFRKilagdyefdSPY-WDDISQAAK----DLVTRLMEVEQDQRITAEEAISHEWI 265
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
127-306 6.31e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 68.89  E-value: 6.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  127 YGEFKSVYVVLDLME----SDLH----QIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKI 198
Cdd:PTZ00267 131 FDDFKSDDKLLLIMEygsgGDLNkqikQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKL 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  199 GDFGMARGLCTSPAEHqyFMTEYVATRWYRAPELMlSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVL 278
Cdd:PTZ00267 211 GDFGFSKQYSDSVSLD--VASSFCGTPYYLAPELW-ERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGK 287
                        170       180
                 ....*....|....*....|....*...
gi 20986497  279 GTPSPAVIqavgAERVRAYIQSLPPRQP 306
Cdd:PTZ00267 288 YDPFPCPV----SSGMKALLDPLLSKNP 311
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
54-266 6.49e-12

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: 66.99  E-value: 6.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSsaRRRLTGQqVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNII----AIKDilRPTVPyge 129
Cdd:cd14063   1 ELEIKEVIGKGRFGRVH--RGRWHGD-VAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVlfmgACMD--PPHLA--- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 fksvyVVLDLMESD-LHQIIHSSQ-PLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVnENCELKIGDFG---MA 204
Cdd:cd14063  73 -----IVTSLCKGRtLYSLIHERKeKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL-ENGRVVITDFGlfsLS 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 205 RGLCTSPAEHQYFMTEYvatrW--YRAPELMLSLH---------EYTQAIDLWSVGCIFGEMLARRqlFPGKN 266
Cdd:cd14063 147 GLLQPGRREDTLVIPNG----WlcYLAPEIIRALSpdldfeeslPFTKASDVYAFGTVWYELLAGR--WPFKE 213
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
61-256 8.37e-12

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


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 66.26  E-value: 8.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRL---TGQQVAIKKIPNAfDVVTNAK---RTLRELKILKHFKHDNIIAikdilrpTVPYGeFKS-- 132
Cdd:cd05583   2 LGTGAYGKVFLVRKVGghdAGKLYAMKVLKKA-TIVQKAKtaeHTMTERQVLEAVRQSPFLV-------TLHYA-FQTda 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 -VYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTS 210
Cdd:cd05583  73 kLHLILDYVNGgELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPG 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 20986497 211 PAEHQYfmtEYVATRWYRAPELMLSLHE-YTQAIDLWSVGCIFGEML 256
Cdd:cd05583 153 ENDRAY---SFCGTIEYMAPEVVRGGSDgHDKAVDWWSLGVLTYELL 196
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
53-264 8.90e-12

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: 66.28  E-value: 8.90e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEI-------IETIGNGAYGVVSSARRRLTgQQVAIKKIPNAfdvVTNAKRTLRELKILKHFKHDNIIAIKDILRPTV 125
Cdd:cd05068   1 DQWEIdrkslklLRKLGSGQFGEVWEGLWNNT-TPVAVKTLKPG---TMDPEDFLREAQIMKKLRHPKLIQLYAVCTLEE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 PygefksVYVVLDLM--ESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGM 203
Cdd:cd05068  77 P------IYIITELMkhGSLLEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGL 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 204 ARGLctsPAEHQYfmTEYVATRW---YRAPELMLSlHEYTQAIDLWSVGCIFGEMLARRQL-FPG 264
Cdd:cd05068 151 ARVI---KVEDEY--EAREGAKFpikWTAPEAANY-NRFSIKSDVWSFGILLTEIVTYGRIpYPG 209
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
59-263 9.45e-12

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: 66.05  E-value: 9.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARrrLTGQQVAIKKIpnAFDVvtNAKRTLRELKILKHFKHDNIIAIKDILRptvpygeFKSVYVVLD 138
Cdd:cd05083  12 EIIGEGEFGAVLQGE--YMGQKVAVKNI--KCDV--TAQAFLEETAVMTKLQHKNLVRLLGVIL-------HNGLYIVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 139 LM-ESDLHQIIHSSQPLTLEhvryfLYQLLR-------GLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglcts 210
Cdd:cd05083  79 LMsKGNLVNFLRSRGRALVP-----VIQLLQfsldvaeGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAK----- 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 20986497 211 pAEHQYFMTEYVATRWyRAPElMLSLHEYTQAIDLWSVGCIFGEMLAR-RQLFP 263
Cdd:cd05083 149 -VGSMGVDNSRLPVKW-TAPE-ALKNKKFSSKSDVWSYGVLLWEVFSYgRAPYP 199
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
60-257 9.57e-12

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 66.74  E-value: 9.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  60 TIGNGAYG-VVSSARRRLTGQQVAIK---KIPNAFDVVTNAKRTLRELKILKHF-KHDNIIaikDILRPTVPYGefkSVY 134
Cdd:cd05055  42 TLGAGAFGkVVEATAYGLSKSDAVMKvavKMLKPTAHSSEREALMSELKIMSHLgNHENIV---NLLGACTIGG---PIL 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDL-MESDLHQIIHSSQP--LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTsp 211
Cdd:cd05055 116 VITEYcCYGDLLNFLRRKREsfLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIMN-- 193
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 20986497 212 aEHQYFM--TEYVATRWYrAPElmlSLHE--YTQAIDLWSVGCIFGEMLA 257
Cdd:cd05055 194 -DSNYVVkgNARLPVKWM-APE---SIFNcvYTFESDVWSYGILLWEIFS 238
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
59-258 1.03e-11

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


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 66.29  E-value: 1.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSA-RRRLTGQ--QVAIKKIPNAFDVvTNAKRTLRELKILKHFKHDNIIAIKDILrptvpygEFKSVYV 135
Cdd:cd05056  12 RCIGEGQFGDVYQGvYMSPENEkiAVAVKTCKNCTSP-SVREKFLQEAYIMRQFDHPHIVKLIGVI-------TENPVWI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 136 VLDL-----MESDLHQiihSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLcts 210
Cdd:cd05056  84 VMELaplgeLRSYLQV---NKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYM--- 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 20986497 211 pAEHQYfmteYVATR------WYrAPElMLSLHEYTQAIDLWSVGCIFGEMLAR 258
Cdd:cd05056 158 -EDESY----YKASKgklpikWM-APE-SINFRRFTSASDVWMFGVCMWEILML 204
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
53-266 1.06e-11

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: 66.18  E-value: 1.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQqVAIKKIPNAFDvvTNAKRTLR-ELKILKHFKHDNIIAIKDilrptvPYGEFK 131
Cdd:cd14191   2 DFYDIEERLGSGKFGQVFRLVEKKTKK-VWAGKFFKAYS--AKEKENIRqEISIMNCLHHPKLVQCVD------AFEEKA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLDLMESD--LHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL-VNEN-CELKIGDFGMARGL 207
Cdd:cd14191  73 NIVMVLEMVSGGelFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTgTKIKLIDFGLARRL 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 CTSPAEHQYFMT-EYVatrwyrAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKN 266
Cdd:cd14191 153 ENAGSLKVLFGTpEFV------APEV-INYEPIGYATDMWSIGVICYILVSGLSPFMGDN 205
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
150-256 1.07e-11

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: 66.91  E-value: 1.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 150 SSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLctspaeHQ---YFMTE--YVAT 224
Cdd:cd05099 127 PEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDNVMKIADFGLARGV------HDidyYKKTSngRLPV 200
                        90       100       110
                ....*....|....*....|....*....|..
gi 20986497 225 RWYrAPELMLSlHEYTQAIDLWSVGCIFGEML 256
Cdd:cd05099 201 KWM-APEALFD-RVYTHQSDVWSFGILMWEIF 230
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
53-256 1.12e-11

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: 67.37  E-value: 1.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdvvtnakrTLRELKILKHFKHDNIIAIKDIL---------RP 123
Cdd:cd05628   1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMK--------------ILRKADMLEKEQVGHIRAERDILveadslwvvKM 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 124 TVPYGEFKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFG 202
Cdd:cd05628  67 FYSFQDKLNLYLIMEFLPGgDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 203 MARGLCTS-------------PAE--HQYFMTEYVATRWYR----------------APELMLSlHEYTQAIDLWSVGCI 251
Cdd:cd05628 147 LCTGLKKAhrtefyrnlnhslPSDftFQNMNSKRKAETWKRnrrqlafstvgtpdyiAPEVFMQ-TGYNKLCDWWSLGVI 225

                ....*
gi 20986497 252 FGEML 256
Cdd:cd05628 226 MYEML 230
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
53-283 1.13e-11

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


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 66.25  E-value: 1.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVssARRRLTGQ-QVAIKKIPNAfdvVTNAKRTLRELKILKHFKHDNIIAIKDIL--RPTVPYGE 129
Cdd:cd05070   9 ESLQLIKRLGNGQFGEV--WMGTWNGNtKVAIKTLKPG---TMSPESFLEEAQIMKKLKHDKLVQLYAVVseEPIYIVTE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDLMESDlhqiihSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglCT 209
Cdd:cd05070  84 YMSKGSLLDFLKDG------EGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLAR--LI 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 210 SPAEHQYFMTEYVATRWyRAPELMLsLHEYTQAIDLWSVGCIFGEMLAR-RQLFPGKNYVHQLQLIMMVLGTPSP 283
Cdd:cd05070 156 EDNEYTARQGAKFPIKW-TAPEAAL-YGRFTIKSDVWSFGILLTELVTKgRVPYPGMNNREVLEQVERGYRMPCP 228
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
61-258 1.24e-11

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: 65.62  E-value: 1.24e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDvvtnAKRTLRELKILKHFKHDNI-----IAIKDilRPTVPYGEFKSVYV 135
Cdd:cd14156   1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDVD----QHKIVREISLLQKLSHPNIvrylgICVKD--EKLHPILEYVSGGC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 136 VLDLMESdlhqiihSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENC---ELKIGDFGMARGLCTSPA 212
Cdd:cd14156  75 LEELLAR-------EELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPrgrEAVVTDFGLAREVGEMPA 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 20986497 213 EHQYFMTEYVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLAR 258
Cdd:cd14156 148 NDPERKLSLVGSAFWMAPE-MLRGEPYDRKVDVFSFGIVLCEILAR 192
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
59-258 1.28e-11

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 66.20  E-value: 1.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARrrLTGQQVAIKKIPnafdvVTNAKRTLRELKI--LKHFKHDNI---IAIKDILRPTVP------- 126
Cdd:cd14053   1 EIKARGRFGAVWKAQ--YLNRLVAVKIFP-----LQEKQSWLTEREIysLPGMKHENIlqfIGAEKHGESLEAeywlite 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 YGEFKSVYVVL---DLMESDLHQIIHSsqpltlehvryflyqLLRGLKYMHS----------AQVIHRDLKPSNLLVNEN 193
Cdd:cd14053  74 FHERGSLCDYLkgnVISWNELCKIAES---------------MARGLAYLHEdipatngghkPSIAHRDFKSKNVLLKSD 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 194 CELKIGDFGMAR----GLCTSPAEHQyfmteyVATRWYRAPELMLSLHEYTQ----AIDLWSVGCIFGEMLAR 258
Cdd:cd14053 139 LTACIADFGLALkfepGKSCGDTHGQ------VGTRRYMAPEVLEGAINFTRdaflRIDMYAMGLVLWELLSR 205
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
55-347 1.32e-11

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: 66.04  E-value: 1.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  55 YEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnaFDVVTNAKRTL--RELKILKHFKHDNIIAIKDI---LRPTVPYGE 129
Cdd:cd14104   2 YMIAEELGRGQFGIVHRCVETSSKKTYMAK-----FVKVKGADQVLvkKEISILNIARHRNILRLHESfesHEELVMIFE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVyvvLDLMEsdlhQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL--VNENCELKIGDFGMARGL 207
Cdd:cd14104  77 FISG---VDIFE----RITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIycTRRGSYIKIIEFGQSRQL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 ctSPAehQYFMTEYVATRWYrAPELMLSlHEYTQAIDLWSVGCifgemlarrqlfpgknyvhqlqLIMMVLGTPSPAViq 287
Cdd:cd14104 150 --KPG--DKFRLQYTSAEFY-APEVHQH-ESVSTATDMWSLGC----------------------LVYVLLSGINPFE-- 199
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 288 avgAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14104 200 ---AETNQQTIENIRNAEYAFDDEAFKNISIEALDFVDRLLVKERKSRMTAQEALNHPWL 256
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
61-255 1.47e-11

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: 65.79  E-value: 1.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPyGEfKSVYVVLDLM 140
Cdd:cd14033   9 IGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKSTVR-GH-KCIILVTELM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 ES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHS--AQVIHRDLKPSNLLVN-ENCELKIGDFGMArglctsPAEHQY 216
Cdd:cd14033  87 TSgTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSrcPPILHRDLKCDNIFITgPTGSVKIGDLGLA------TLKRAS 160
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 20986497 217 FMTEYVATRWYRAPELMlsLHEYTQAIDLWSVGCIFGEM 255
Cdd:cd14033 161 FAKSVIGTPEFMAPEMY--EEKYDEAVDVYAFGMCILEM 197
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
60-256 1.49e-11

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: 66.14  E-value: 1.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  60 TIGNGAYG-VVSSARRRLTGQ----QVAIKKIPNAFDVVtNAKRTLRELKILKHFKHDNIIAIKDILRPTVP-------- 126
Cdd:cd05045   7 TLGEGEFGkVVKATAFRLKGRagytTVAVKMLKENASSS-ELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPllliveya 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 -YGEFKSV----------YVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE 195
Cdd:cd05045  86 kYGSLRSFlresrkvgpsYLGSDGNRNSSYLDNPDERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEGRK 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 196 LKIGDFGMARGLCTSPAEHQYfMTEYVATRWYrAPELMLSlHEYTQAIDLWSVGCIFGEML 256
Cdd:cd05045 166 MKISDFGLSRDVYEEDSYVKR-SKGRIPVKWM-AIESLFD-HIYTTQSDVWSFGVLLWEIV 223
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
54-256 1.51e-11

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: 65.90  E-value: 1.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQ----VAIKKIPNAFDVVTNaKRTLRELKILKHFKHDNIIAIkdilrptvpyge 129
Cdd:cd05057   8 ELEKGKVLGSGAFGTVYKGVWIPEGEKvkipVAIKVLREETGPKAN-EEILDEAYVMASVDHPHLVRL------------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 fksvyvvLDLMESDLHQIIHSSQPL--TLEHVRY------------FLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCE 195
Cdd:cd05057  75 -------LGICLSSQVQLITQLMPLgcLLDYVRNhrdnigsqlllnWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNH 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497 196 LKIGDFGMARGLctSPAEHQYFMTE-YVATRWYrAPELMLsLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd05057 148 VKITDFGLAKLL--DVDEKEYHAEGgKVPIKWM-ALESIQ-YRIYTHKSDVWSYGVTVWELM 205
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
150-256 1.67e-11

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: 1.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 150 SSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLcTSPAEHQYFMTEYVATRWYrA 229
Cdd:cd05101 139 PEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDI-NNIDYYKKTTNGRLPVKWM-A 216
                        90       100
                ....*....|....*....|....*..
gi 20986497 230 PELMLSlHEYTQAIDLWSVGCIFGEML 256
Cdd:cd05101 217 PEALFD-RVYTHQSDVWSFGVLMWEIF 242
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
71-347 1.70e-11

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 65.81  E-value: 1.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  71 SARRRLTGQQVAI----KKIPnafdvvTNAKRTLRELKI---------LKHFKHDNIIAIKDilrptvPYGE-------- 129
Cdd:cd14011  14 NGSKKSTKQEVSVfvfeKKQL------EEYSKRDREQILellkrgvkqLTRLRHPRILTVQH------PLEEsreslafa 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 ----FKSVYVVL---DLMESDLHQIihSSQPLTLEHVRYFLYQLLRGLKYMH-SAQVIHRDLKPSNLLVNENCELKIGDF 201
Cdd:cd14011  82 tepvFASLANVLgerDNMPSPPPEL--QDYKLYDVEIKYGLLQISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 202 GMArGLCTSPAEHQYFMTEYVATRW--------YRAPELMLSlHEYTQAIDLWSVGCIFGEMLARR-QLFPGKNYVHQLQ 272
Cdd:cd14011 160 DFC-ISSEQATDQFPYFREYDPNLPplaqpnlnYLAPEYILS-KTCDPASDMFSLGVLIYAIYNKGkPLFDCVNNLLSYK 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 273 LIMMVLGTPSPAVIQAVGAErVRAYIQSLpprqpvpwetvypgadrqalsllgrmLRFEPSARISAAAALRHPFL 347
Cdd:cd14011 238 KNSNQLRQLSLSLLEKVPEE-LRDHVKTL--------------------------LNVTPEVRPDAEQLSKIPFF 285
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
91-256 1.82e-11

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: 66.11  E-value: 1.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  91 DVVTNAKRT-LRELKILKHFKHDNIIAI------KDILRPTVPYGE------FKSVYVVLDLMESDLHQIIHSSQPLTLE 157
Cdd:cd05096  57 DANKNARNDfLKEVKILSRLKDPNIIRLlgvcvdEDPLCMITEYMEngdlnqFLSSHHLDDKEENGNDAVPPAHCLPAIS 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 158 H--VRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSpaehQYFMTEYVAT---RWYrAPEL 232
Cdd:cd05096 137 YssLLHVALQIASGMKYLSSLNFVHRDLATRNCLVGENLTIKIADFGMSRNLYAG----DYYRIQGRAVlpiRWM-AWEC 211
                       170       180
                ....*....|....*....|....
gi 20986497 233 MLsLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd05096 212 IL-MGKFTTASDVWAFGVTLWEIL 234
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
61-363 1.89e-11

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 66.08  E-value: 1.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNafDVV---TNAKRTLRELKILKHFKHDNIIaikdilrpTVPYGEFKSVYVVL 137
Cdd:cd05590   3 LGKGSFGKVMLARLKESGRLYAVKVLKK--DVIlqdDDVECTMTEKRILSLARNHPFL--------TQLYCCFQTPDRLF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 138 DLME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMarglCTSPAE 213
Cdd:cd05590  73 FVMEfvngGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGM----CKEGIF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 214 HQYFMTEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKNyvhQLQLIMMVLGTpspaviqavgaer 293
Cdd:cd05590 149 NGKTTSTFCGTPDYIAPEILQEM-LYGPSVDWWAMGVLLYEMLCGHAPFEAEN---EDDLFEAILND------------- 211
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 294 vrayiqslpprqpvpwETVYPG-ADRQALSLLGRMLRFEPSARISA------AAALRHPFLAKYH-DPDDEPDCAPPF 363
Cdd:cd05590 212 ----------------EVVYPTwLSQDAVDILKAFMTKNPTMRLGSltlggeEAILRHPFFKELDwEKLNRRQIEPPF 273
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
61-262 2.03e-11

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 65.40  E-value: 2.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNA-FDVVTNAKRTLRELKILKHFKHDNIIAIkdilrpTVPYGEFKSVYVVLDL 139
Cdd:cd05631   8 LGKGGFGEVCACQVRATGKMYACKKLEKKrIKKRKGEAMALNEKRILEKVNSRFVVSL------AYAYETKDALCLVLTI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 140 MES-DLHQIIHSSQPLTLEHVRYFLY--QLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMArglcTSPAEHQY 216
Cdd:cd05631  82 MNGgDLKFHIYNMGNPGFDEQRAIFYaaELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLA----VQIPEGET 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 20986497 217 FMTEyVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLF 262
Cdd:cd05631 158 VRGR-VGTVGYMAPEV-INNEKYTFSPDWWGLGCLIYEMIQGQSPF 201
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
54-256 2.21e-11

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: 64.87  E-value: 2.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPN----AFDVVTNAKRTLRELKILKHF----KHDNIIAIKDILRptV 125
Cdd:cd14101   1 QYTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRnrvqQWSKLPGVNPVPNEVALLQSVgggpGHRGVIRLLDWFE--I 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 PYGEFksvyVVLDLME--SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVN-ENCELKIGDFG 202
Cdd:cd14101  79 PEGFL----LVLERPQhcQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLIDFG 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 20986497 203 MARGLCTSPaehqyfMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd14101 155 SGATLKDSM------YTDFDGTRVYSPPEWILYHQYHALPATVWSLGILLYDMV 202
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
61-338 2.56e-11

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: 65.19  E-value: 2.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRltGQQVAIKKIpnafdVVTNAKRTLRELKILKH--FKHDNIIA-IKDILRPTvpyGEFKSVYVVL 137
Cdd:cd14144   3 VGKGRYGEVWKGKWR--GEKVAVKIF-----FTTEEASWFRETEIYQTvlMRHENILGfIAADIKGT---GSWTQLYLIT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 138 DLMES-DLHQIIHSSQpLTLEHVRYFLYQLLRGLKYMHS--------AQVIHRDLKPSNLLVNENCELKIGDFGMARGLC 208
Cdd:cd14144  73 DYHENgSLYDFLRGNT-LDTQSMLKLAYSAACGLAHLHTeifgtqgkPAIAHRDIKSKNILVKKNGTCCIADLGLAVKFI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 209 TSPAEHQYFMTEYVATRWYRAPELML------SLHEYTQAiDLWSVGCIFGEMlARRQLFPGKNYVHQLQLIMMVLGTPS 282
Cdd:cd14144 152 SETNEVDLPPNTRVGTKRYMAPEVLDeslnrnHFDAYKMA-DMYSFGLVLWEI-ARRCISGGIVEEYQLPYYDAVPSDPS 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20986497 283 -PAVIQAVGAERVRayiqslpPRQPVPWETvypgadRQALSLLGRMLR----FEPSARISA 338
Cdd:cd14144 230 yEDMRRVVCVERRR-------PSIPNRWSS------DEVLRTMSKLMSecwaHNPAARLTA 277
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
53-283 2.61e-11

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: 65.08  E-value: 2.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIE-------TIGNGAYGVVSSARRRltgQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIkdilrptV 125
Cdd:cd14151   1 DDWEIPDgqitvgqRIGSGSFGTVYKGKWH---GDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLF-------M 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 PYGEFKSVYVVLDLME-SDLHQIIHSSQ-PLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGM 203
Cdd:cd14151  71 GYSTKPQLAIVTQWCEgSSLYHHLHIIEtKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 204 ARGLCTSPAEHQYfmTEYVATRWYRAPEL--MLSLHEYTQAIDLWSVGCIFGEMLARRqlFPGKNYVHQLQLIMMV-LGT 280
Cdd:cd14151 151 ATVKSRWSGSHQF--EQLSGSILWMAPEVirMQDKNPYSFQSDVYAFGIVLYELMTGQ--LPYSNINNRDQIIFMVgRGY 226

                ...
gi 20986497 281 PSP 283
Cdd:cd14151 227 LSP 229
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
58-262 2.75e-11

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


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 66.19  E-value: 2.75e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  58 IETIGNGAYGVVSSARRRLTGQQVAIKkipnafdvvtnakrTLRELKILKHFKHDNIIAIKDIL---------RPTVPYG 128
Cdd:cd05626   6 IKTLGIGAFGEVCLACKVDTHALYAMK--------------TLRKKDVLNRNQVAHVKAERDILaeadnewvvKLYYSFQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL 207
Cdd:cd05626  72 DKDNLYFVMDYIPGgDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 ------------------CTSPA------------------------EHQYFMTE-YVATRWYRAPELMLSlHEYTQAID 244
Cdd:cd05626 152 rwthnskyyqkgshirqdSMEPSdlwddvsncrcgdrlktleqratkQHQRCLAHsLVGTPNYIAPEVLLR-KGYTQLCD 230
                       250
                ....*....|....*...
gi 20986497 245 LWSVGCIFGEMLARRQLF 262
Cdd:cd05626 231 WWSVGVILFEMLVGQPPF 248
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
54-256 2.95e-11

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: 64.67  E-value: 2.95e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRltGQQVAIK---KIPNAfDVVTNAKRTLRELKILKHFKHDNIIAIKDILrptvpygef 130
Cdd:cd14147   4 ELRLEEVIGIGGFGKVYRGSWR--GELVAVKaarQDPDE-DISVTAESVRQEARLFAMLAHPNIIALKAVC--------- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 ksvyvvldLMESDLHQIIH--SSQPLTLE--------HVRY-FLYQLLRGLKYMHS---AQVIHRDLKPSNLL-----VN 191
Cdd:cd14147  72 --------LEEPNLCLVMEyaAGGPLSRAlagrrvppHVLVnWAVQIARGMHYLHCealVPVIHRDLKSNNILllqpiEN 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 192 ENCE---LKIGDFGMARglctspAEHQYFMTEYVATRWYRAPELMLSlHEYTQAIDLWSVGCIFGEML 256
Cdd:cd14147 144 DDMEhktLKITDFGLAR------EWHKTTQMSAAGTYAWMAPEVIKA-STFSKGSDVWSFGVLLWELL 204
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
59-258 3.20e-11

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: 65.15  E-value: 3.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARrrLTGQQVAIKKIPnafdvVTNAKRTLRELKILK--HFKHDNIIA-IKDILRPT---------VP 126
Cdd:cd13998   1 EVIGKGRFGEVWKAS--LKNEPVAVKIFS-----SRDKQSWFREKEIYRtpMLKHENILQfIAADERDTalrtelwlvTA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 YGEFKSVYVVLDLMESDLHQIIHSSQPLTlehvryflyqllRGLKYMHSAQVI---------HRDLKPSNLLVNENCELK 197
Cdd:cd13998  74 FHPNGSL*DYLSLHTIDWVSLCRLALSVA------------RGLAHLHSEIPGctqgkpaiaHRDLKSKNILVKNDGTCC 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 198 IGDFGMARGLCTSPAEHQYFMTEYVATRWYRAPELM-----LSLHEYTQAIDLWSVGCIFGEMLAR 258
Cdd:cd13998 142 IADFGLAVRLSPSTGEEDNANNGQVGTKRYMAPEVLegainLRDFESFKRVDIYAMGLVLWEMASR 207
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
153-257 3.26e-11

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: 65.39  E-value: 3.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 153 PLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPaEHQYFMTEYVATRWYrAPEL 232
Cdd:cd05102 168 PLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDP-DYVRKGSARLPLKWM-APES 245
                        90       100
                ....*....|....*....|....*
gi 20986497 233 MLSlHEYTQAIDLWSVGCIFGEMLA 257
Cdd:cd05102 246 IFD-KVYTTQSDVWSFGVLLWEIFS 269
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
51-270 3.50e-11

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: 65.08  E-value: 3.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  51 VGDEYEIIETIGNGAYGVVSSARRrLTGQQVAIKKIPNAFDVVTNAKR------TLRELKILKHFKHDNIIAIKDILRPt 124
Cdd:cd14041   4 LNDRYLLLHLLGRGGFSEVYKAFD-LTEQRYVAVKIHQLNKNWRDEKKenyhkhACREYRIHKELDHPRIVKLYDYFSL- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 125 vpygEFKSVYVVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQ--VIHRDLKPSN-LLVNENC--ELKI 198
Cdd:cd14041  82 ----DTDSFCTVLEYCEgNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNiLLVNGTAcgEIKI 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 199 GDFGMARGL---CTSPAEHQYFMTEYVATRWYRAPELMLSLHE---YTQAIDLWSVGCIFGEMLARRQLFpGKNYVHQ 270
Cdd:cd14041 158 TDFGLSKIMdddSYNSVDGMELTSQGAGTYWYLPPECFVVGKEppkISNKVDVWSVGVIFYQCLYGRKPF-GHNQSQQ 234
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
53-275 3.65e-11

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: 65.81  E-value: 3.65e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGvvssarrrltgqQVAIKKIPNAFDVVtnAKRTLRELKILKHFKHDNIIAIKDILR-------PTV 125
Cdd:cd05623  72 EDFEILKVIGRGAFG------------EVAVVKLKNADKVF--AMKILNKWEMLKRAETACFREERDVLVngdsqwiTTL 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 PYG--EFKSVYVVLDL-MESDLHQIIHSSQP-LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDF 201
Cdd:cd05623 138 HYAfqDDNNLYLVMDYyVGGDLLTLLSKFEDrLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADF 217
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 202 G-----MARGLCTSPAEhqyfmteyVATRWYRAPELMLSLHE----YTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQ 272
Cdd:cd05623 218 GsclklMEDGTVQSSVA--------VGTPDYISPEILQAMEDgkgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYG 289

                ...
gi 20986497 273 LIM 275
Cdd:cd05623 290 KIM 292
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
54-275 4.22e-11

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: 65.40  E-value: 4.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNafDVVT---NAKRTLRELKILkhfkhdniiAIKDilRP---TVPY 127
Cdd:cd05615  11 DFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKK--DVVIqddDVECTMVEKRVL---------ALQD--KPpflTQLH 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 128 GEFKSV---YVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGM 203
Cdd:cd05615  78 SCFQTVdrlYFVMEYVNGgDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGM 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 204 ARglctspaEHqyfMTEYVATRW------YRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIM 275
Cdd:cd05615 158 CK-------EH---MVEGVTTRTfcgtpdYIAPEI-IAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIM 224
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
59-335 4.23e-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: 64.44  E-value: 4.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRptvpygefKSVYVVLD 138
Cdd:cd14025   2 EKVGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGICS--------EPVGLVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 139 LMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQ--VIHRDLKPSNLLVNENCELKIGDFGMAR--GLCTSpaeH 214
Cdd:cd14025  74 YMETGSLEKLLASEPLPWELRFRIIHETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKwnGLSHS---H 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 215 QYFMTEYVATRWYRAPE-LMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYvhqlqlIMMVLgtpspavIQAVGAER 293
Cdd:cd14025 151 DLSRDGLRGTIAYLPPErFKEKNRCPDTKHDVYSFAIVIWGILTQKKPFAGENN------ILHIM-------VKVVKGHR 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 20986497 294 vrayiqslPPRQPVPweTVYPGADRQALSLLGRMLRFEPSAR 335
Cdd:cd14025 218 --------PSLSPIP--RQRPSECQQMICLMKRCWDQDPRKR 249
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
35-256 4.24e-11

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 65.39  E-value: 4.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497   35 KNLALLKARSFDVTFDVG-------DEYEIIETIGNGAYGVVSSARRRLTG-QQVAIKKIPNAFDV-VTNAKRTLRELKI 105
Cdd:PTZ00426   5 KNLQLHKKKDSDSTKEPKrknkmkyEDFNFIRTLGTGSFGRVILATYKNEDfPPVAIKRFEKSKIIkQKQVDHVFSERKI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  106 LKHFKHDNIIAIkdilrptvpYGEFKS---VYVVLD-LMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHR 181
Cdd:PTZ00426  85 LNYINHPFCVNL---------YGSFKDesyLYLVLEfVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  182 DLKPSNLLVNENCELKIGDFGMAR-------GLCTSPaehqyfmtEYVatrwyrAPELMLSLHeYTQAIDLWSVGCIFGE 254
Cdd:PTZ00426 156 DLKPENLLLDKDGFIKMTDFGFAKvvdtrtyTLCGTP--------EYI------APEILLNVG-HGKAADWWTLGIFIYE 220

                 ..
gi 20986497  255 ML 256
Cdd:PTZ00426 221 IL 222
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
46-257 4.82e-11

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


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 64.64  E-value: 4.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  46 DVTFDvgdeyeiiETIGNGAYGVVSSARRRLTGQQV-AIKKIPNAFDVVTNAKRTLRELKIL-KHFKHDNIIAIKD---- 119
Cdd:cd05089   3 DIKFE--------DVIGEGNFGQVIKAMIKKDGLKMnAAIKMLKEFASENDHRDFAGELEVLcKLGHHPNIINLLGacen 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 120 -----ILRPTVPYGEFKSVYVVLDLMESD--LHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNE 192
Cdd:cd05089  75 rgylyIAIEYAPYGNLLDFLRKSRVLETDpaFAKEHGTASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGE 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 193 NCELKIGDFGMARGlctspaEHQYFMTEY--VATRWYRAPELMLSLheYTQAIDLWSVGCIFGEMLA 257
Cdd:cd05089 155 NLVSKIADFGLSRG------EEVYVKKTMgrLPVRWMAIESLNYSV--YTTKSDVWSFGVLLWEIVS 213
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
54-255 4.89e-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: 4.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRltGQQVAIKKIPNAfdvvTNAKRTLRELKILKHFKHDNIIAIKDILrptvpYGEFKSV 133
Cdd:cd05082   7 ELKLLQTIGKGEFGDVMLGDYR--GNKVAVKCIKND----ATAQAFLAEASVMTQLRHSNLVQLLGVI-----VEEKGGL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 YVVLDLM-ESDLHQIIHSSQPLTL--EHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTS 210
Cdd:cd05082  76 YIVTEYMaKGSLVDYLRSRGRSVLggDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASST 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 20986497 211 PAehqyfmTEYVATRWyRAPElMLSLHEYTQAIDLWSVGCIFGEM 255
Cdd:cd05082 156 QD------TGKLPVKW-TAPE-ALREKKFSTKSDVWSFGILLWEI 192
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
51-338 5.12e-11

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), 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. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b 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 BMPR1b, 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 BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 64.69  E-value: 5.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  51 VGDEYEIIETIGNGAYGVVSSARRRltGQQVAIKKIpnafdVVTNAKRTLRELKILKH--FKHDNIIAIkdILRPTVPYG 128
Cdd:cd14219   3 IAKQIQMVKQIGKGRYGEVWMGKWR--GEKVAVKVF-----FTTEEASWFRETEIYQTvlMRHENILGF--IAADIKGTG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMES-DLHQIIHSSQpLTLEHVRYFLYQLLRGLKYMHS--------AQVIHRDLKPSNLLVNENCELKIG 199
Cdd:cd14219  74 SWTQLYLITDYHENgSLYDYLKSTT-LDTKAMLKLAYSSVSGLCHLHTeifstqgkPAIAHRDLKSKNILVKKNGTCCIA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 200 DFGMARGLCTSPAEHQYFMTEYVATRWYRAPELM---LSLHEYTQAI--DLWSVGCIFGEmLARRQLFPGKNYVHQLQLI 274
Cdd:cd14219 153 DLGLAVKFISDTNEVDIPPNTRVGTKRYMPPEVLdesLNRNHFQSYImaDMYSFGLILWE-VARRCVSGGIVEEYQLPYH 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20986497 275 MMVLGTPSPAVIQAVgaervrAYIQSLPPRQPVPWETvyPGADRQALSLLGRMLRFEPSARISA 338
Cdd:cd14219 232 DLVPSDPSYEDMREI------VCIKRLRPSFPNRWSS--DECLRQMGKLMTECWAHNPASRLTA 287
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
67-249 6.09e-11

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 64.62  E-value: 6.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  67 GVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDilrpTVPYGEfkSVYVVLDLME----S 142
Cdd:cd08216  14 GVVHLAKHKPTNTLVAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVT----SFVVDN--DLYVVTPLMAygscR 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 143 DLHQIiHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMarglCTSPAEH---QYFMT 219
Cdd:cd08216  88 DLLKT-HFPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRY----AYSMVKHgkrQRVVH 162
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 20986497 220 EYV--ATR---WYrAPELM-LSLHEYTQAIDLWSVG 249
Cdd:cd08216 163 DFPksSEKnlpWL-SPEVLqQNLLGYNEKSDIYSVG 197
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
54-255 6.31e-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: 63.75  E-value: 6.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRltGQ-QVAIKKIPNAfdvVTNAKRTLRELKILKHFKHDNIIAIKDIL---RPTVPYGE 129
Cdd:cd05113   5 DLTFLKELGTGQFGVVKYGKWR--GQyDVAIKMIKEG---SMSEDEFIEEAKVMMNLSHEKLVQLYGVCtkqRPIFIITE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDLMESDLHQIihssQPLTLEHVryfLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCT 209
Cdd:cd05113  80 YMANGCLLNYLREMRKRF----QTQQLLEM---CKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLD 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 20986497 210 SpaEHQYFMTEYVATRWyRAPELMLsLHEYTQAIDLWSVGCIFGEM 255
Cdd:cd05113 153 D--EYTSSVGSKFPVRW-SPPEVLM-YSKFSSKSDVWAFGVLMWEV 194
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
61-299 6.43e-11

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: 63.97  E-value: 6.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRpTVPYGEfKSVYVVLDLM 140
Cdd:cd14031  18 LGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWE-SVLKGK-KCIVLVTELM 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 ES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQ--VIHRDLKPSNLLVN-ENCELKIGDFGMARGLCTSpaehqy 216
Cdd:cd14031  96 TSgTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLMRTS------ 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 217 FMTEYVATRWYRAPElMLSLHeYTQAIDLWSVGCIFGEMLARRqlFPGKNYVHQLQLIMMVLGTPSPAVIQAVGAERVRA 296
Cdd:cd14031 170 FAKSVIGTPEFMAPE-MYEEH-YDESVDVYAFGMCMLEMATSE--YPYSECQNAAQIYRKVTSGIKPASFNKVTDPEVKE 245

                ...
gi 20986497 297 YIQ 299
Cdd:cd14031 246 IIE 248
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
97-299 7.12e-11

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: 63.92  E-value: 7.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  97 KRTLRELKILKHFKHDNIIAIKDILRPtvpygEFKSVYVVLDLME-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHS 175
Cdd:cd14040  55 KHACREYRIHKELDHPRIVKLYDYFSL-----DTDTFCTVLEYCEgNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNE 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 176 AQ--VIHRDLKPSNLLVNENC---ELKIGDFGMARGLCTSP--AEHQYFMTEYVATRWYRAPELMLSLHE---YTQAIDL 245
Cdd:cd14040 130 IKppIIHYDLKPGNILLVDGTacgEIKITDFGLSKIMDDDSygVDGMDLTSQGAGTYWYLPPECFVVGKEppkISNKVDV 209
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 246 WSVGCIFGEMLARRQLFpGKNYVHQ--LQLIMMVLGTPSPAVIQAVGAERVRAYIQ 299
Cdd:cd14040 210 WSVGVIFFQCLYGRKPF-GHNQSQQdiLQENTILKATEVQFPVKPVVSNEAKAFIR 264
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
61-264 7.83e-11

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


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 63.55  E-value: 7.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTgQQVAIKKI------PNAFdvvtnakrtLRELKILKHFKHDNIIAIKDIL--RPTVPYGEFKS 132
Cdd:cd05069  20 LGQGCFGEVWMGTWNGT-TKVAIKTLkpgtmmPEAF---------LQEAQIMKKLRHDKLVPLYAVVseEPIYIVTEFMG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMESDlhqiihSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglCTSPA 212
Cdd:cd05069  90 KGSLLDFLKEG------DGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLAR--LIEDN 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 20986497 213 EHQYFMTEYVATRWyRAPELMLsLHEYTQAIDLWSVGCIFGEMLAR-RQLFPG 264
Cdd:cd05069 162 EYTARQGAKFPIKW-TAPEAAL-YGRFTIKSDVWSFGILLTELVTKgRVPYPG 212
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
61-256 8.49e-11

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: 63.91  E-value: 8.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSAR-RRLTGQQ----VAIKKIPNAFDvvtNAKRTL-RELKILKHFKHDNIIAIKDILRPTVPygefksVY 134
Cdd:cd05093  13 LGEGAFGKVFLAEcYNLCPEQdkilVAVKTLKDASD---NARKDFhREAELLTNLQHEHIVKFYGVCVEGDP------LI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 VVLDLME-SDLHQIIHSSQP-------------LTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGD 200
Cdd:cd05093  84 MVFEYMKhGDLNKFLRAHGPdavlmaegnrpaeLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGD 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20986497 201 FGMARGLCTSpaehQYFMT---EYVATRWYRAPELMlsLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd05093 164 FGMSRDVYST----DYYRVgghTMLPIRWMPPESIM--YRKFTTESDVWSLGVVLWEIF 216
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
61-264 9.33e-11

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: 63.12  E-value: 9.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRlTGQQVAIKKI-PNAFDVvtnaKRTLRELKILKHFKHDNIIAIKDIL--RPTVPYGEFKSVYVVL 137
Cdd:cd05073  19 LGAGQFGEVWMATYN-KHTKVAVKTMkPGSMSV----EAFLAEANVMKTLQHDKLVKLHAVVtkEPIYIITEFMAKGSLL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 138 DLMESDlhqiihSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLctspAEHQYF 217
Cdd:cd05073  94 DFLKSD------EGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVI----EDNEYT 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 20986497 218 MTE--YVATRWyRAPElMLSLHEYTQAIDLWSVGCIFGEMLAR-RQLFPG 264
Cdd:cd05073 164 AREgaKFPIKW-TAPE-AINFGSFTIKSDVWSFGILLMEIVTYgRIPYPG 211
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
32-205 1.24e-10

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: 63.18  E-value: 1.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  32 VAAKNLALLKArsfdvtfdvgdeyeiietIGNGAYGVVSSAR-RRLTGQ----QVAIKKIPnafDVVTNAKRT--LRELK 104
Cdd:cd05036   3 VPRKNLTLIRA------------------LGQGAFGEVYEGTvSGMPGDpsplQVAVKTLP---ELCSEQDEMdfLMEAL 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 105 ILKHFKHDNIIAIKDILRPTVPYgefksvYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLL-------RGLKYMHSA 176
Cdd:cd05036  62 IMSKFNHPNIVRCIGVCFQRLPR------FILLELMAGgDLKSFLRENRPRPEQPSSLTMLDLLqlaqdvaKGCRYLEEN 135
                       170       180       190
                ....*....|....*....|....*....|....
gi 20986497 177 QVIHRDLKPSNLLVneNCEL-----KIGDFGMAR 205
Cdd:cd05036 136 HFIHRDIAARNCLL--TCKGpgrvaKIGDFGMAR 167
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
101-272 1.30e-10

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: 62.87  E-value: 1.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 101 RELKILKHFKHDNIIAIKDILRPTVPYgefksvYVVLDLME-SDLHQII---------HSSQPLTLEHVRYFLYQLLRGL 170
Cdd:cd05046  57 RELDMFRKLSHKNVVRLLGLCREAEPH------YMILEYTDlGDLKQFLratkskdekLKPPPLSTKQKVALCTQIALGM 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 171 KYMHSAQVIHRDLKPSNLLVNENCELKIGdfgmARGLCTSPAEHQYFM--TEYVATRWYrAPELMLSlHEYTQAIDLWSV 248
Cdd:cd05046 131 DHLSNARFVHRDLAARNCLVSSQREVKVS----LLSLSKDVYNSEYYKlrNALIPLRWL-APEAVQE-DDFSTKSDVWSF 204
                       170       180
                ....*....|....*....|....*...
gi 20986497 249 GCIFGEMLARRQL-FPGKN---YVHQLQ 272
Cdd:cd05046 205 GVLMWEVFTQGELpFYGLSdeeVLNRLQ 232
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
78-262 1.84e-10

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 62.61  E-value: 1.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  78 GQQVAIKKIPnaFDVVTNAKRTLRELKILKHFKHDNII----AIKD-----ILRPTVPYGEFKsvyvvlDLMESDlhqii 148
Cdd:cd14042  30 GNLVAIKKVN--KKRIDLTREVLKELKHMRDLQHDNLTrfigACVDppnicILTEYCPKGSLQ------DILENE----- 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 149 hssqPLTLEHV-RY-FLYQLLRGLKYMHSAQVI-HRDLKPSNLLVNENCELKIGDFGMARGLCTSPA---EHQYFmteyv 222
Cdd:cd14042  97 ----DIKLDWMfRYsLIHDIVKGMHYLHDSEIKsHGNLKSSNCVVDSRFVLKITDFGLHSFRSGQEPpddSHAYY----- 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 20986497 223 ATRWYRAPELMLSLH---EYTQAIDLWSVGCIFGEMLARRQLF 262
Cdd:cd14042 168 AKLLWTAPELLRDPNpppPGTQKGDVYSFGIILQEIATRQGPF 210
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
61-264 1.85e-10

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: 62.40  E-value: 1.85e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTgQQVAIKKI------PNAFdvvtnakrtLRELKILKHFKHDNIIAIKDIL--RPTVPYGEFKS 132
Cdd:cd05071  17 LGQGCFGEVWMGTWNGT-TRVAIKTLkpgtmsPEAF---------LQEAQVMKKLRHEKLVQLYAVVseEPIYIVTEYMS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 133 VYVVLDLMESDlhqiihSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglCTSPA 212
Cdd:cd05071  87 KGSLLDFLKGE------MGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLAR--LIEDN 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 20986497 213 EHQYFMTEYVATRWyRAPELMLsLHEYTQAIDLWSVGCIFGEMLAR-RQLFPG 264
Cdd:cd05071 159 EYTARQGAKFPIKW-TAPEAAL-YGRFTIKSDVWSFGILLTELTTKgRVPYPG 209
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
54-262 2.00e-10

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: 63.51  E-value: 2.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAfdvVTNAKRTLRELKILKHF-----KHDNIIAIKDILRPtvpyg 128
Cdd:cd05618  21 DFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKE---LVNDDEDIDWVQTEKHVfeqasNHPFLVGLHSCFQT----- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR-GL 207
Cdd:cd05618  93 ESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKeGL 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 208 ctSPAEHqyfMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLF 262
Cdd:cd05618 173 --RPGDT---TSTFCGTPNYIAPEI-LRGEDYGFSVDWWALGVLMFEMMAGRSPF 221
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
169-275 2.03e-10

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 62.79  E-value: 2.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 169 GLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglctspaEHqyfMTEYVATRW------YRAPELMLSlHEYTQA 242
Cdd:cd05587 109 GLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCK-------EG---IFGGKTTRTfcgtpdYIAPEIIAY-QPYGKS 177
                        90       100       110
                ....*....|....*....|....*....|...
gi 20986497 243 IDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIM 275
Cdd:cd05587 178 VDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIM 210
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
54-277 2.30e-10

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: 62.19  E-value: 2.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRlTGQQVAIKKIPNAfdvVTNAKRTLRELKILKHFKHDNIIAIkdilrptvpYG---EF 130
Cdd:cd05114   5 ELTFMKELGSGLFGVVRLGKWR-AQYKVAIKAIREG---AMSEEDFIEEAKVMMKLTHPKLVQL---------YGvctQQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVLDLMESD--LHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglc 208
Cdd:cd05114  72 KPIYIVTEFMENGclLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTR--- 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 209 tspaehqYFM-TEYVAT-------RWyrAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLfPGKNYVHqLQLIMMV 277
Cdd:cd05114 149 -------YVLdDQYTSSsgakfpvKW--SPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKM-PFESKSN-YEVVEMV 214
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
61-266 3.17e-10

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: 62.51  E-value: 3.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNafDVVT---NAKRTLRELKILK-HFKHDNIIAIkdilrptvpYGEFKSVYVV 136
Cdd:cd05591   3 LGKGSFGKVMLAERKGTDEVYAIKVLKK--DVILqddDVDCTMTEKRILAlAAKHPFLTAL---------HSCFQTKDRL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 137 LDLME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMarglCTSPA 212
Cdd:cd05591  72 FFVMEyvngGDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGM----CKEGI 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 20986497 213 EHQYFMTEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPGKN 266
Cdd:cd05591 148 LNGKTTTTFCGTPDYIAPEILQEL-EYGPSVDWWALGVLMYEMMAGQPPFEADN 200
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
61-258 3.61e-10

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 61.50  E-value: 3.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNaFDVVTNaKRTLRELKILKHFKHDNIIAIKDILrptvpYGEfKSVYVVLDLM 140
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKVMVMKELIR-CDEETQ-KTFLTEVKVMRSLDHPNVLKFIGVL-----YKD-KRLNLLTEFI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 E-SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLC---------TS 210
Cdd:cd14222  73 EgGTLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVeekkkpppdKP 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 211 PAEHQYFMT-------EYVATRWYRAPElMLSLHEYTQAIDLWSVGCIFGEMLAR 258
Cdd:cd14222 153 TTKKRTLRKndrkkryTVVGNPYWMAPE-MLNGKSYDEKVDIFSFGIVLCEIIGQ 206
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
61-255 4.27e-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: 61.28  E-value: 4.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPnafDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYgefksvYVVLDLM 140
Cdd:cd05052  14 LGGGQYGEVYEGVWKKYNLTVAVKTLK---EDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPF------YIITEFM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 -ESDLHQIIHSSQPLTLEHVR--YFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARglctspaehqyF 217
Cdd:cd05052  85 pYGNLLDYLRECNREELNAVVllYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSR-----------L 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 20986497 218 MTE--YVA-------TRWyRAPElMLSLHEYTQAIDLWSVGCIFGEM 255
Cdd:cd05052 154 MTGdtYTAhagakfpIKW-TAPE-SLAYNKFSIKSDVWAFGVLLWEI 198
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
54-262 4.32e-10

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: 62.35  E-value: 4.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAF-------DVVTNAKRTLRELKilkhfKHDNIIAIKDILRPTvp 126
Cdd:cd05617  16 DFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELvhddediDWVQTEKHVFEQAS-----SNPFLVGLHSCFQTT-- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 ygefKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd05617  89 ----SRLFLVIEYVNGgDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCK 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 206 -GLctSPAEHqyfMTEYVATRWYRAPELmLSLHEYTQAIDLWSVGCIFGEMLARRQLF 262
Cdd:cd05617 165 eGL--GPGDT---TSTFCGTPNYIAPEI-LRGEEYGFSVDWWALGVLMFEMMAGRSPF 216
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
53-264 4.74e-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: 61.06  E-value: 4.74e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTgQQVAIKKI------PNAFdvvtnakrtLRELKILKHFKHDNIIAIKDIL--RPT 124
Cdd:cd05067   7 ETLKLVERLGAGQFGEVWMGYYNGH-TKVAIKSLkqgsmsPDAF---------LAEANLMKQLQHQRLVRLYAVVtqEPI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 125 VPYGEFKSVYVVLDLMESDlhqiihSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA 204
Cdd:cd05067  77 YIITEYMENGSLVDFLKTP------SGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLA 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 205 RGLCTspaehqyfmTEYVA-------TRWyRAPElMLSLHEYTQAIDLWSVGCIFGEMLAR-RQLFPG 264
Cdd:cd05067 151 RLIED---------NEYTAregakfpIKW-TAPE-AINYGTFTIKSDVWSFGILLTEIVTHgRIPYPG 207
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
53-347 4.82e-10

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: 61.58  E-value: 4.82e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEII-ETIGNGAYGVVSSARRRLTGQQVAIKKIPNafDVVTNAKRTLRELKILKHFKHDniiaiKDILRPTVPYGEFK 131
Cdd:cd14174   1 DLYRLTdELLGEGAYAKVQGCVSLQNGKEYAVKIIEK--NAGHSRSRVFREVETLYQCQGN-----KNILELIEFFEDDT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVYVVLD-LMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLvnenCE-------LKIGDFGM 203
Cdd:cd14174  74 RFYLVFEkLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENIL----CEspdkvspVKICDFDL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 204 ARGL-----CTSPAEHQyfMTEYVATRWYRAPELMLSLHE----YTQAIDLWSVGCIFGEMLARRQLFPGKnyvhqlqli 274
Cdd:cd14174 150 GSGVklnsaCTPITTPE--LTTPCGSAEYMAPEVVEVFTDeatfYDKRCDLWSLGVILYIMLSGYPPFVGH--------- 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 275 mmvLGT-------PSPAVIQAVGAERVRAYIQSLPprqpvpwETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14174 219 ---CGTdcgwdrgEVCRVCQNKLFESIQEGKYEFP-------DKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
53-275 5.28e-10

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: 61.56  E-value: 5.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIpnafdvvtNAKRTLRELKILKHFKHDNIIAIKD---ILRPTVPYGE 129
Cdd:cd05601   1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVL--------KKSETLAQEEVSFFEEERDIMAKANspwITKLQYAFQD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 FKSVYVVLDLMES-DLHQIIHSSQ-PLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL 207
Cdd:cd05601  73 SENLYLVMEYHPGgDLLSLLSRYDdIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKL 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 208 ctSPAEHQYFMTEyVATRWYRAPELMLSLHEYTQA-----IDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIM 275
Cdd:cd05601 153 --SSDKTVTSKMP-VGTPDYIAPEVLTSMNGGSKGtygveCDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIM 222
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
53-267 7.98e-10

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


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 60.34  E-value: 7.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIietiGNGAYGVVSSARRRLTGQQ--VAIKKIPNAFDVvTNAKRTLRELKILKHFKHDNIIAIKDILrptvpygEF 130
Cdd:cd05115   8 DEVEL----GSGNFGCVKKGVYKMRKKQidVAIKVLKQGNEK-AVRDEMMREAQIMHQLDNPYIVRMIGVC-------EA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVLDLMESD-LHQIIHSSQ-PLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSN-LLVNENCElKIGDFGMARGL 207
Cdd:cd05115  76 EALMLVMEMASGGpLNKFLSGKKdEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNvLLVNQHYA-KISDFGLSKAL 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20986497 208 ctsPAEHQYFMTEYVAT---RWYrAPELMLsLHEYTQAIDLWSVGCIFGEMLArrqlFPGKNY 267
Cdd:cd05115 155 ---GADDSYYKARSAGKwplKWY-APECIN-FRKFSSRSDVWSYGVTMWEAFS----YGQKPY 208
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
59-252 8.03e-10

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: 60.58  E-value: 8.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQVAIKKipnafdVVTNAKRTLRELKILKHF-----KHDNIIAikdiLRPTV---PYGEF 130
Cdd:cd13975   6 RELGRGQYGVVYACDSWGGHFPCALKS------VVPPDDKHWNDLALEFHYtrslpKHERIVS----LHGSVidySYGGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVL--DLMESDLHQIIHSSqpLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFgmarGLC 208
Cdd:cd13975  76 SSIAVLLimERLHRDLYTGIKAG--LSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDL----GFC 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 20986497 209 TSPAehqyFMT-EYVATRWYRAPELmLSLHeYTQAIDLWSVGCIF 252
Cdd:cd13975 150 KPEA----MMSgSIVGTPIHMAPEL-FSGK-YDNSVDVYAFGILF 188
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
51-277 8.37e-10

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


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 60.82  E-value: 8.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  51 VGDEYEIIETIGNGAYGVVSSARRRltgQQVAIKKI------PNAFDVVTNakrtlrELKILKHFKHDNIIAI-----KD 119
Cdd:cd14149  10 EASEVMLSTRIGSGSFGTVYKGKWH---GDVAVKILkvvdptPEQFQAFRN------EVAVLRKTRHVNILLFmgymtKD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 120 ILRPTVPYGEFKSVYVVLDLMESDLH--QIIHSSQpltlehvryflyQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELK 197
Cdd:cd14149  81 NLAIVTQWCEGSSLYKHLHVQETKFQmfQLIDIAR------------QTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVK 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 198 IGDFGMARGLCTSPAEHQyfMTEYVATRWYRAPEL--MLSLHEYTQAIDLWSVGCIFGEMLARRqlFPGKNYVHQLQLIM 275
Cdd:cd14149 149 IGDFGLATVKSRWSGSQQ--VEQPTGSILWMAPEVirMQDNNPFSFQSDVYSYGIVLYELMTGE--LPYSHINNRDQIIF 224

                ..
gi 20986497 276 MV 277
Cdd:cd14149 225 MV 226
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
59-258 9.22e-10

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 60.36  E-value: 9.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRltGQQVAIKKIPNafdvvTNAKRTLRELKI--LKHFKHDNI---IA--IKDILRPT-----VP 126
Cdd:cd14056   1 KTIGKGRYGEVWLGKYR--GEKVAVKIFSS-----RDEDSWFRETEIyqTVMLRHENIlgfIAadIKSTGSWTqlwliTE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 YGEFKSVYVVLdlmesdlhqiihSSQPLTLEHVRYFLYQLLRGLKYMHSA--------QVIHRDLKPSNLLVNENCELKI 198
Cdd:cd14056  74 YHEHGSLYDYL------------QRNTLDTEEALRLAYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNILVKRDGTCCI 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497 199 GDFGMA------RGLCTSPAEHQyfmteyVATRWYRAPEL------MLSLHEYTQAiDLWSVGCIFGEMLAR 258
Cdd:cd14056 142 ADLGLAvrydsdTNTIDIPPNPR------VGTKRYMAPEVlddsinPKSFESFKMA-DIYSFGLVLWEIARR 206
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
53-275 1.03e-09

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: 60.37  E-value: 1.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVV--SSARRRLTGQ---QVAIKKIpNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPy 127
Cdd:cd05061   6 EKITLLRELGQGSFGMVyeGNARDIIKGEaetRVAVKTV-NESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQP- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 128 gefksVYVVLDLM-ESDLHQIIHS----------SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCEL 196
Cdd:cd05061  84 -----TLVVMELMaHGDLKSYLRSlrpeaennpgRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 197 KIGDFGMARGLctspaehqyFMTEY--------VATRWYrAPElmlSLHE--YTQAIDLWSVGCIFGEM--LArRQLFPG 264
Cdd:cd05061 159 KIGDFGMTRDI---------YETDYyrkggkglLPVRWM-APE---SLKDgvFTTSSDMWSFGVVLWEItsLA-EQPYQG 224
                       250
                ....*....|.
gi 20986497 265 KNYVHQLQLIM 275
Cdd:cd05061 225 LSNEQVLKFVM 235
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
61-282 1.21e-09

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: 60.05  E-value: 1.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRltGQQVAIKKIpnafdVVTNAKRTLRELKILKH--FKHDNIIAIkdILRPTVPYGEFKSVYVVLD 138
Cdd:cd14220   3 IGKGRYGEVWMGKWR--GEKVAVKVF-----FTTEEASWFRETEIYQTvlMRHENILGF--IAADIKGTGSWTQLYLITD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 139 LMES-DLHQIIHSSQpLTLEHVRYFLYQLLRGLKYMHS--------AQVIHRDLKPSNLLVNENCELKIGDFGMARGLCT 209
Cdd:cd14220  74 YHENgSLYDFLKCTT-LDTRALLKLAYSAACGLCHLHTeiygtqgkPAIAHRDLKSKNILIKKNGTCCIADLGLAVKFNS 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 210 SPAEHQYFMTEYVATRWYRAPELM---LSLHEYTQAI--DLWSVGCIFGEMlARRQLFPGKNYVHQLQLIMMVLGTPS 282
Cdd:cd14220 153 DTNEVDVPLNTRVGTKRYMAPEVLdesLNKNHFQAYImaDIYSFGLIIWEM-ARRCVTGGIVEEYQLPYYDMVPSDPS 229
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
159-347 1.29e-09

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


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 60.53  E-value: 1.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 159 VRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENC-ELKIGDFGMARGLCT---------------SPAEhQYFMTeyv 222
Cdd:cd14013 122 IKSIMRQILVALRKLHSTGIVHRDVKPQNIIVSEGDgQFKIIDLGAAADLRIginyipkeflldpryAPPE-QYIMS--- 197
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 223 aTRWYRAPEL--------MLSLHEYTQAIDLWSVGCIFGEM------------LARRQLfpgKNYVHQLQLIMMVLGtps 282
Cdd:cd14013 198 -TQTPSAPPApvaaalspVLWQMNLPDRFDMYSAGVILLQMafpnlrsdsnliAFNRQL---KQCDYDLNAWRMLVE--- 270
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 283 paviqAVGAERVRAYIQSLPPRQPVPWEtvypgadrqalsLLGRMLRFEPSARISAAAALRHPFL 347
Cdd:cd14013 271 -----PRASADLREGFEILDLDDGAGWD------------LVTKLIRYKPRGRLSASAALAHPYF 318
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
164-256 1.42e-09

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: 60.03  E-value: 1.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 164 YQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLctspaEHQYFMTEYVATRW---YRAPELMLSlHEYT 240
Cdd:cd05098 142 YQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDI-----HHIDYYKKTTNGRLpvkWMAPEALFD-RIYT 215
                        90
                ....*....|....*.
gi 20986497 241 QAIDLWSVGCIFGEML 256
Cdd:cd05098 216 HQSDVWSFGVLLWEIF 231
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
53-256 1.68e-09

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 60.63  E-value: 1.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKkipnafdvvtnakrTLRELKILKHFKHDNIIAIKDIL----RPTVP-- 126
Cdd:cd05629   1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMK--------------TLLKSEMFKKDQLAHVKAERDVLaesdSPWVVsl 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 YGEFK-SVYVVLdLME----SDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDF 201
Cdd:cd05629  67 YYSFQdAQYLYL-IMEflpgGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDF 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 202 GMARGL-----------------CTSPAEHQYFMT--------------------------EYVATRWYRAPELMLSlHE 238
Cdd:cd05629 146 GLSTGFhkqhdsayyqkllqgksNKNRIDNRNSVAvdsinltmsskdqiatwkknrrlmaySTVGTPDYIAPEIFLQ-QG 224
                       250
                ....*....|....*...
gi 20986497 239 YTQAIDLWSVGCIFGEML 256
Cdd:cd05629 225 YGQECDWWSLGAIMFECL 242
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
58-256 1.70e-09

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 59.62  E-value: 1.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  58 IETIGNGAYGVV--SSARRRLTGQQVAIKKIpNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYgefksvyv 135
Cdd:cd05087   2 LKEIGHGWFGKVflGEVNSGLSSTQVVVKEL-KASASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPY-------- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 136 vLDLME----SDLHQIIHSSQ--------PLTLEHVRYflyQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGM 203
Cdd:cd05087  73 -LLVMEfcplGDLKGYLRSCRaaesmapdPLTLQRMAC---EVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGL 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20986497 204 ARglCTSpaEHQYFMTE---YVATRWYrAPELMLSLH------EYTQAIDLWSVGCIFGEML 256
Cdd:cd05087 149 SH--CKY--KEDYFVTAdqlWVPLRWI-APELVDEVHgnllvvDQTKQSNVWSLGVTIWELF 205
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
136-348 1.70e-09

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: 59.56  E-value: 1.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 136 VLDLMESDLhqIIHSS-QPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLL--VNENCeLKIGDFGMarglcTSPA 212
Cdd:cd14020  90 LLDVSVSEL--LLRSSnQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILwsAEDEC-FKLIDFGL-----SFKE 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 213 EHQyfMTEYVATRWYRAPELML----------SLHEYTQAIDLWSVGCIFGEMlarrqlFPGKNYVHQLQliMMVLGTPS 282
Cdd:cd14020 162 GNQ--DVKYIQTDGYRAPEAELqnclaqaglqSETECTSAVDLWSLGIVLLEM------FSGMKLKHTVR--SQEWKDNS 231
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 283 PAVIQAVGAERVRAYiQSLPprqpvpwetVYPGADrqalsLLGRMLRFEPSARISAAAALRHPFLA 348
Cdd:cd14020 232 SAIIDHIFASNAVVN-PAIP---------AYHLRD-----LIKSMLHNDPGKRATAEAALCSPFFS 282
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
141-264 1.88e-09

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: 60.42  E-value: 1.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 ESDLHQII--HSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCtspAEHQYFM 218
Cdd:cd05105 219 DSEVKNLLsdDGSEGLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIM---HDSNYVS 295
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 20986497 219 --TEYVATRWYrAPELMLSlHEYTQAIDLWSVGCIFGEMLAR-RQLFPG 264
Cdd:cd05105 296 kgSTFLPVKWM-APESIFD-NLYTTLSDVWSYGILLWEIFSLgGTPYPG 342
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
71-257 1.88e-09

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: 59.72  E-value: 1.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  71 SARRRLTGQQVAIKKIPNAFD---VVTNAKRTLRELKILKHFKHDNIIAIKDILrpTVPYGefkSVYVVLDLMESDLHQI 147
Cdd:cd14001  21 SPRGGSSRSPWAVKKINSKCDkgqRSLYQERLKEEAKILKSLNHPNIVGFRAFT--KSEDG---SLCLAMEYGGKSLNDL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 148 IH-----SSQPLTLEHVRYFLYQLLRGLKYMHS-AQVIHRDLKPSNLLVNENCE-LKIGDFGMARGL------CTSPAEH 214
Cdd:cd14001  96 IEeryeaGLGPFPAATILKVALSIARALEYLHNeKKILHGDIKSGNVLIKGDFEsVKLCDFGVSLPLtenlevDSDPKAQ 175
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 20986497 215 qyfmteYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLA 257
Cdd:cd14001 176 ------YVGTEPWKAKEALEEGGVITDKADIFAYGLVLWEMMT 212
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
56-263 1.91e-09

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: 59.70  E-value: 1.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  56 EIIETIGNGAYGVVSSAR-----RRLTGQQVAIKKI-PNAFDVVTNAKRtlRELKILKHFKHDNIIAIKDILRPTVPYGe 129
Cdd:cd05048   8 RFLEELGEGAFGKVYKGEllgpsSEESAISVAIKTLkENASPKTQQDFR--REAELMSDLQHPNIVCLLGVCTKEQPQC- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 130 fksvyVVLDLME-SDLHQIIHSSQPLT--------------LEH--VRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNE 192
Cdd:cd05048  85 -----MLFEYMAhGDLHEFLVRHSPHSdvgvssdddgtassLDQsdFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 193 NCELKIGDFGMARGLCTspaeHQYFMTEY---VATRWYrAPELMLSlHEYTQAIDLWSVGCI------------FG---- 253
Cdd:cd05048 160 GLTVKISDFGLSRDIYS----SDYYRVQSkslLPVRWM-PPEAILY-GKFTTESDVWSFGVVlweifsyglqpyYGysnq 233
                       250
                ....*....|...
gi 20986497 254 ---EMLARRQLFP 263
Cdd:cd05048 234 eviEMIRSRQLLP 246
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
53-205 2.21e-09

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: 59.89  E-value: 2.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLR-ELKILKHFKHDNIIAIKDILRPTvpygefK 131
Cdd:cd05610   4 EEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQaERDALALSKSPFIVHLYYSLQSA------N 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 132 SVYVVLD-LMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd05610  78 NVYLVMEyLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSK 152
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
58-256 2.45e-09

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


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 59.20  E-value: 2.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  58 IETIGNGAYG--VVSSARRRLTGQQVAIKKI-PNAFDVvtNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYgefksvy 134
Cdd:cd14206   2 LQEIGNGWFGkvILGEIFSDYTPAQVVVKELrVSAGPL--EQRKFISEAQPYRSLQHPNILQCLGLCTETIPF------- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 135 vvLDLME----SDLHQIIHSSQP---LT-------LEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGD 200
Cdd:cd14206  73 --LLIMEfcqlGDLKRYLRAQRKadgMTpdlptrdLRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGD 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20986497 201 FGMARglctSPAEHQYFMTE---YVATRWYrAPELMLSLH------EYTQAIDLWSVGCIFGEML 256
Cdd:cd14206 151 YGLSH----NNYKEDYYLTPdrlWIPLRWV-APELLDELHgnlivvDQSKESNVWSLGVTIWELF 210
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
61-299 2.66e-09

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: 59.29  E-value: 2.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPyGEfKSVYVVLDLM 140
Cdd:cd14030  33 IGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTVK-GK-KCIVLVTELM 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 141 ES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHS--AQVIHRDLKPSNLLVN-ENCELKIGDFGMArglctsPAEHQY 216
Cdd:cd14030 111 TSgTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTrtPPIIHRDLKCDNIFITgPTGSVKIGDLGLA------TLKRAS 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 217 FMTEYVATRWYRAPELMlsLHEYTQAIDLWSVGCIFGEMLARRqlFPGKNYVHQLQLIMMVLGTPSPAVIQAVGAERVRA 296
Cdd:cd14030 185 FAKSVIGTPEFMAPEMY--EEKYDESVDVYAFGMCMLEMATSE--YPYSECQNAAQIYRRVTSGVKPASFDKVAIPEVKE 260

                ...
gi 20986497 297 YIQ 299
Cdd:cd14030 261 IIE 263
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
53-251 3.21e-09

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: 58.70  E-value: 3.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  53 DEYEIIETIGNGAYGVVSSA--RRRLTGQQVAIKkipnAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTvpygef 130
Cdd:cd14112   3 GRFSFGSEIFRGRFSVIVKAvdSTTETDAHCAVK----IFEVSDEASEAVREFESLRTLQHENVQRLIAAFKPS------ 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 131 KSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVN--ENCELKIGDFGMAR--- 205
Cdd:cd14112  73 NFAYLVMEKLQEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQsvRSWQVKLVDFGRAQkvs 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 20986497 206 GLCTSPAEhqyfmteyVATRWyRAPELMLSLHEYTQAIDLWSVGCI 251
Cdd:cd14112 153 KLGKVPVD--------GDTDW-ASPEFHNPETPITVQSDIWGLGVL 189
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
58-274 3.22e-09

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: 59.68  E-value: 3.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  58 IETIGNGAYGVVSSARRRLTGQQVAIKkipnafdvvtnakrTLRELKILKHFKHDNIIAIKDIL---------RPTVPYG 128
Cdd:cd05625   6 IKTLGIGAFGEVCLARKVDTKALYATK--------------TLRKKDVLLRNQVAHVKAERDILaeadnewvvRLYYSFQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 129 EFKSVYVVLDLMES-DLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGL 207
Cdd:cd05625  72 DKDNLYFVMDYIPGgDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 208 CTSPAEHQY------------FMTEY-------------------------------VATRWYRAPELMLSLHeYTQAID 244
Cdd:cd05625 152 RWTHDSKYYqsgdhlrqdsmdFSNEWgdpencrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLLRTG-YTQLCD 230
                       250       260       270
                ....*....|....*....|....*....|.
gi 20986497 245 LWSVGCIFGEMLARRQLFPGKNYVH-QLQLI 274
Cdd:cd05625 231 WWSVGVILFEMLVGQPPFLAQTPLEtQMKVI 261
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
151-256 4.13e-09

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: 58.88  E-value: 4.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 151 SQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLcTSPAEHQYFMTEYVATRWYrAP 230
Cdd:cd05100 128 EEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDV-HNIDYYKKTTNGRLPVKWM-AP 205
                        90       100
                ....*....|....*....|....*.
gi 20986497 231 ELMLSlHEYTQAIDLWSVGCIFGEML 256
Cdd:cd05100 206 EALFD-RVYTHQSDVWSFGVLLWEIF 230
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
61-257 4.28e-09

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: 58.28  E-value: 4.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRlTGQQVAIKKIPNAFDVVTNAKRTlRELKILKHFKHDNIIAIKD---------ILRPTVPYGEFK 131
Cdd:cd14664   1 IGRGGAGTVYKGVMP-NGTLVAVKRLKGEGTQGGDHGFQ-AEIQTLGMIRHRNIVRLRGycsnpttnlLVYEYMPNGSLG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 132 SVyvvldlmesdLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMH---SAQVIHRDLKPSNLLVNENCELKIGDFGMARgLC 208
Cdd:cd14664  79 EL----------LHSRPESQPPLDWETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAK-LM 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 20986497 209 TSPAEHqyFMTEYVATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLA 257
Cdd:cd14664 148 DDKDSH--VMSSVAGSYGYIAPEYAYTG-KVSEKSDVYSYGVVLLELIT 193
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
54-256 4.92e-09

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: 58.50  E-value: 4.92e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  54 EYEIIETIGNGAYGVVSSARRRLTGQQVaikKIPNAFDVVTNA------KRTLRELKILKHFKHDNIIAIKDI-LRPTV- 125
Cdd:cd05108   8 EFKKIKVLGSGAFGTVYKGLWIPEGEKV---KIPVAIKELREAtspkanKEILDEAYVMASVDNPHVCRLLGIcLTSTVq 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 ------PYGefksvyVVLDLMESDLHQIihSSQpltleHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIG 199
Cdd:cd05108  85 litqlmPFG------CLLDYVREHKDNI--GSQ-----YLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKIT 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20986497 200 DFGMARGLCTSPAEHQYFMTEyVATRWYrAPELMLSlHEYTQAIDLWSVGCIFGEML 256
Cdd:cd05108 152 DFGLAKLLGAEEKEYHAEGGK-VPIKWM-ALESILH-RIYTHQSDVWSYGVTVWELM 205
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
59-257 5.04e-09

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: 58.47  E-value: 5.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVSSARRRLTGQQV--AIKKIPNaFDVVTNAKRTLRELKIL-KHFKHDNIIAI------KDILRPTV---P 126
Cdd:cd05088  13 DVIGEGNFGQVLKARIKKDGLRMdaAIKRMKE-YASKDDHRDFAGELEVLcKLGHHPNIINLlgacehRGYLYLAIeyaP 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 YGEFKSVYVVLDLMESDLHQIIHSSQPLTL--EHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMA 204
Cdd:cd05088  92 HGNLLDFLRKSRVLETDPAFAIANSTASTLssQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 171
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 205 RGlctspaeHQYFMTEYVA---TRWYRAPELMLSLheYTQAIDLWSVGCIFGEMLA 257
Cdd:cd05088 172 RG-------QEVYVKKTMGrlpVRWMAIESLNYSV--YTTNSDVWSYGVLLWEIVS 218
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
157-262 5.24e-09

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: 58.59  E-value: 5.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 157 EHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR-----GLCTSpaehqyfmtEYVATRWYRAPE 231
Cdd:cd05588  96 EHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKeglrpGDTTS---------TFCGTPNYIAPE 166
                        90       100       110
                ....*....|....*....|....*....|.
gi 20986497 232 lMLSLHEYTQAIDLWSVGCIFGEMLARRQLF 262
Cdd:cd05588 167 -ILRGEDYGFSVDWWALGVLMFEMLAGRSPF 196
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
61-327 5.33e-09

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: 58.05  E-value: 5.33e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSaRRRLTGQQVAIKK-----------IPN--------AFDVVTNAKRTLRELKILKHFKHDNIIAIKDI- 120
Cdd:cd14067   1 LGQGGSGTVIY-RARYQGQPVAVKRfhikkckkrtdGSAdtmlkhlrAADAMKNFSEFRQEASMLHSLQHPCIVYLIGIs 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 121 LRPT------VPYGEFKSVyvvldlmesdLHQIIHSSQPLTLEHVRYF--LYQLLRGLKYMHSAQVIHRDLKPSNLLV-- 190
Cdd:cd14067  80 IHPLcfalelAPLGSLNTV----------LEENHKGSSFMPLGHMLTFkiAYQIAAGLAYLHKKNIIFCDLKSDNILVws 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 191 ---NENCELKIGDFGMARglctspaehQYFMTEYV---ATRWYRAPELMLSLhEYTQAIDLWSVGCIFGEMLARRQLFPG 264
Cdd:cd14067 150 ldvQEHINIKLSDYGISR---------QSFHEGALgveGTPGYQAPEIRPRI-VYDEKVDMFSYGMVLYELLSGQRPSLG 219
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 265 KnyvHQLQL-------IMMVLGTPspaviQAVGAERVRAYIQSLpprqpvpWETvYPGADRQALSLLGRM 327
Cdd:cd14067 220 H---HQLQIakklskgIRPVLGQP-----EEVQFFRLQALMMEC-------WDT-KPEKRPLACSVVEQM 273
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
61-278 6.61e-09

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: 58.01  E-value: 6.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIK--KIPNAFdVVTNAKRTLRELKILKHFKHDNIIAIKDILRptvpygEFKSVYVVLD 138
Cdd:cd14026   5 LSRGAFGTVSRARHADWRVTVAIKclKLDSPV-GDSERNCLLKEAEILHKARFSYILPILGICN------EPEFLGIVTE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 139 LMES-DLHQIIHSSQ--PLTLEHVRY-FLYQLLRGLKYMH--SAQVIHRDLKPSNLLVNENCELKIGDFGMA--RGLCTS 210
Cdd:cd14026  78 YMTNgSLNELLHEKDiyPDVAWPLRLrILYEIALGVNYLHnmSPPLLHHDLKTQNILLDGEFHVKIADFGLSkwRQLSIS 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 211 PAEHQYFMTEYvATRWYRAPELMLSLHEYTQAI--DLWSVGCIFGEMLARRQlfPGKNYVHQLQLIMMVL 278
Cdd:cd14026 158 QSRSSKSAPEG-GTIIYMPPEEYEPSQKRRASVkhDIYSYAIIMWEVLSRKI--PFEEVTNPLQIMYSVS 224
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
61-202 6.74e-09

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: 55.14  E-value: 6.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRLTGQQVAIKKIpnafDVVTNAKR--TLRELKILKHFKhdniIAIKDILRPTVPYGEFKSVYVVLD 138
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIG----DDVNNEEGedLESEMDILRRLK----GLELNIPKVLVTEDVDGPNILLME 72
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20986497 139 LME----SDLHQIIHSSQPLTlehvRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFG 202
Cdd:cd13968  73 LVKggtlIAYTQEEELDEKDV----ESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
61-256 9.96e-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: 57.15  E-value: 9.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  61 IGNGAYGVVSSARRRltGQQVAIKKI-PNAFDVVTNAKRTLRELKILKHFKHDNIIA-----IKDilrPTvpygEFKSV- 133
Cdd:cd14064   1 IGSGSFGKVYKGRCR--NKIVAIKRYrANTYCSKSDVDMFCREVSILCRLNHPCVIQfvgacLDD---PS----QFAIVt 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 134 -YVVLDLMESDLHQiihSSQPLTLEHVRYFLYQLLRGLKYMH-SAQ-VIHRDLKPSNLLVNENCELKIGDFGMARGLCTS 210
Cdd:cd14064  72 qYVSGGSLFSLLHE---QKRVIDLQSKLIIAVDVAKGMEYLHnLTQpIIHRDLNSHNILLYEDGHAVVADFGESRFLQSL 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 20986497 211 PAEHqyfMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEML 256
Cdd:cd14064 149 DEDN---MTKQPGNLRWMAPEVFTQCTRYSIKADVFSYALCLWELL 191
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
126-256 1.20e-08

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: 58.10  E-value: 1.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 126 PYGEFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMAR 205
Cdd:cd05107 208 NYESPYDQYLPSAPERTRRDTLINESPALSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLAR 287
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 20986497 206 GLCTspaEHQYFM--TEYVATRWYrAPELMLSlHEYTQAIDLWSVGCIFGEML 256
Cdd:cd05107 288 DIMR---DSNYISkgSTFLPLKWM-APESIFN-NLYTTLSDVWSFGILLWEIF 335
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
59-317 1.91e-08

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 56.60  E-value: 1.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497  59 ETIGNGAYGVVssARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKilkHFKHDNI---IAIKDilRPTVP--------- 126
Cdd:cd14054   1 QLIGQGRYGTV--WKGSLDERPVAVKVFPARHRQNFQNEKDIYELP---LMEHSNIlrfIGADE--RPTADgrmeyllvl 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 127 -YGEFKSVYVVLDLMESDLHQIIHSSQPLTlehvryflyqllRGLKYMHS---------AQVIHRDLKPSNLLVNENCEL 196
Cdd:cd14054  74 eYAPKGSLCSYLRENTLDWMSSCRMALSLT------------RGLAYLHTdlrrgdqykPAIAHRDLNSRNVLVKADGSC 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20986497 197 KIGDFGMARGLCTSPAEH-QYFMTEY-----VATRWYRAPELM---LSLHEYTQA---IDLWSVGCIFGEMLAR-RQLFP 263
Cdd:cd14054 142 VICDFGLAMVLRGSSLVRgRPGAAENasiseVGTLRYMAPEVLegaVNLRDCESAlkqVDVYALGLVLWEIAMRcSDLYP 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20986497 264 GKNYV-HQLQLIMMVLGTPSPAVIQ-AVGAERVRAYIqslpprqPVPWETVYPGAD 317
Cdd:cd14054 222 GESVPpYQMPYEAELGNHPTFEDMQlLVSREKARPKF-------PDAWKENSLAVR 270
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH